A database of hormones and their receptors |
|
|
|
|
|
|
HMRbase accession number | 10001 |
Swiss-prot Accession number | Q95JC9 (Sequence in FASTA format) |
Description | Basic proline-rich protein precursor [Contains: Proline-rich peptideSP-A (PRP-SP-A); Proline-rich peptide SP-B (PRP-SP-B); Parotid hormone(PH-Ab)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | N/A |
Tissue Specificity | Acinar cells and secretory granules of the parotid gland |
Post translational modification | N/A |
Function | The parotid hormone stimulates dentinal fluid transport in teeth |
Protein Length | 676 Amino acids |
Molecular weight | 62283 |
References | 1 PubMed abstract 15805110 2 PubMed abstract 16112392 3 PubMed abstract 7371600 |
Domain Name | N/A |
Hormone Name | Parotid hormone |
Mature Hormone Sequence | APPGARPPPGPPPPPPGPSPPRPPPGPPPQ |
Position of mature hormone in Pre-Hormone protein | 30 Residues from position (647-676) |
Receptor | N/A |
Gene ID | 100049648 100113399 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10115 |
Swiss-prot Accession number | Q9GKY5 (Sequence in FASTA format) |
Description | Appetite-regulating hormone precursor (Growth hormone secretagogue)(Growth hormone-releasing peptide) (Motilin-related peptide)[Contains: Ghrelin; Obestatin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein (By similarity) |
Developmental Stage | N/A |
Similarity | Belongs to the motilin family. |
Tissue Specificity | N/A |
Post translational modification | O-n-octanoylation is essential for ghrelin activity (By similarity). Amidation of Leu-99 is essential for obestatin activity (By similarity). |
Function | Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation |
Protein Length | 118 Amino acids |
Molecular weight | 12786 |
References | 1 Kojima M.; Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
2 Rousselle J., Lacroix D., Dubreuil P.; Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. 3 Ying M., Yang Z.; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Motilin_assoc Motilin_ghrelin |
Hormone Name | Ghrelin |
Mature Hormone Sequence | GSSFLSPEHQKVQQRKESKKPAAKLKPR |
Position of mature hormone in Pre-Hormone protein | 28 Residues from position (25-52) |
Receptor | P34999
Detail in HMRbase |
Gene ID | 396728 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 10239 |
Swiss-prot Accession number | Q95274 (Sequence in FASTA format) |
Description | Thymosin beta-4 (T beta-4) [Contains: Hematopoietic system regulatorypeptide (Seraspenide)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Cytoplasm (By similarity) |
Developmental Stage | N/A |
Similarity | Belongs to the thymosin beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Plays an important role in the organization of the cytoskeleton (By similarity). Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization |
Protein Length | 44 Amino acids |
Molecular weight | 5053 |
References | 1 Winteroe A.K., Fredholm M., Davies W.; "Evaluation and characterization of a porcine small intestine cDNAlibrary."; Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 16971568 |
Domain Name | Thymosin |
Hormone Name | Thymosin beta-4 |
Mature Hormone Sequence | SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES |
Position of mature hormone in Pre-Hormone protein | 43 Residues from position (2-44) |
Receptor | N/A |
Gene ID | 733606 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10240 |
Swiss-prot Accession number | Q95274 (Sequence in FASTA format) |
Description | Thymosin beta-4 (T beta-4) [Contains: Hematopoietic system regulatorypeptide (Seraspenide)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Cytoplasm (By similarity) |
Developmental Stage | N/A |
Similarity | Belongs to the thymosin beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Seraspenide inhibits the entry of hematopoietic pluripotent stem cells into the S-phase |
Protein Length | 44 Amino acids |
Molecular weight | 5053 |
References | 1 Winteroe A.K., Fredholm M., Davies W.; "Evaluation and characterization of a porcine small intestine cDNAlibrary."; Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 16971568 |
Domain Name | Thymosin |
Hormone Name | Hematopoietic system regulatory peptide |
Mature Hormone Sequence | SDKP |
Position of mature hormone in Pre-Hormone protein | 4 Residues from position (2-5) |
Receptor | N/A |
Gene ID | 733606 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10278 |
Swiss-prot Accession number | P63298 (Sequence in FASTA format) |
Description | Secretin precursor (Fragment). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Stimulates formation of NaHCO(3)-rich pancreatic juice and secretion of NaHCO(3)-rich bile and inhibits HCl production by the stomach |
Protein Length | 131 Amino acids |
Molecular weight | 14278 |
References | 1 PubMed abstract 2315322 2 PubMed abstract 8618828 3 PubMed abstract 5465996 4 PubMed abstract 2395872 5 PubMed abstract 5978238 6 PubMed abstract 2831051 7 PubMed abstract 2883029 |
Domain Name | Hormone_2 |
Hormone Name | Secretin |
Mature Hormone Sequence | HSDGTFTSELSRLRDSARLQRLLQGLV |
Position of mature hormone in Pre-Hormone protein | 27 Residues from position (30-56) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10290 |
Swiss-prot Accession number | Q8HY17 (Sequence in FASTA format) |
Description | Relaxin-3 precursor (Insulin-like peptide INSL7) (Insulin-like peptide7) [Contains: Relaxin-3 B chain; Relaxin-3 A chain]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | May play a role in neuropeptide signaling processes. Ligand for LGR7, relaxin-3 receptor-1 and relaxin-3 receptor-2 |
Protein Length | 140 Amino acids |
Molecular weight | 15360 |
References | 1 PubMed abstract 12686464 2 PubMed abstract 12506116 3 PubMed abstract 14522968 |
Domain Name | Insulin |
Hormone Name | Relaxin-3 B chain |
Mature Hormone Sequence | RASPYGVKLCGREFIRAVIFTCGGSRW |
Position of mature hormone in Pre-Hormone protein | 27 Residues from position (27-53) |
Receptor | N/A |
Gene ID | 503836 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10291 |
Swiss-prot Accession number | Q8HY17 (Sequence in FASTA format) |
Description | Relaxin-3 precursor (Insulin-like peptide INSL7) (Insulin-like peptide7) [Contains: Relaxin-3 B chain; Relaxin-3 A chain]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | May play a role in neuropeptide signaling processes. Ligand for LGR7, relaxin-3 receptor-1 and relaxin-3 receptor-3 |
Protein Length | 140 Amino acids |
Molecular weight | 15360 |
References | 1 PubMed abstract 12686464 2 PubMed abstract 12506116 3 PubMed abstract 14522968 |
Domain Name | Insulin |
Hormone Name | Relaxin-3 A chain |
Mature Hormone Sequence | DVLAGLSSNCCKWGCSKSEISSLC |
Position of mature hormone in Pre-Hormone protein | 24 Residues from position (117-140) |
Receptor | N/A |
Gene ID | 503836 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10352 |
Swiss-prot Accession number | Q9GKY5 (Sequence in FASTA format) |
Description | Appetite-regulating hormone precursor (Growth hormone secretagogue)(Growth hormone-releasing peptide) (Motilin-related peptide)[Contains: Ghrelin; Obestatin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein (By similarity) |
Developmental Stage | N/A |
Similarity | Belongs to the motilin family. |
Tissue Specificity | N/A |
Post translational modification | O-n-octanoylation is essential for ghrelin activity (By similarity). Amidation of Leu-99 is essential for obestatin activity (By similarity). |
Function | Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility |
Protein Length | 118 Amino acids |
Molecular weight | 12786 |
References | 1 Kojima M.; Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
2 Rousselle J., Lacroix D., Dubreuil P.; Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. 3 Ying M., Yang Z.; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Motilin_assoc Motilin_ghrelin |
Hormone Name | Obestatin |
Mature Hormone Sequence | FNAPCDVGIKLSGAQSDQHGQPL |
Position of mature hormone in Pre-Hormone protein | 23 Residues from position (77-99) |
Receptor | P34999
Detail in HMRbase |
Gene ID | 396728 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 10473 |
Swiss-prot Accession number | P62968 (Sequence in FASTA format) |
Description | Thyroliberin (Thyrotropin-releasing hormone) (TRH) (Thyrotropin-releasing factor) (TRF) (TSH-releasing factor) (Protirelin). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the TRH family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems |
Protein Length | 3 Amino acids |
Molecular weight | 380 |
References | 1 PubMed abstract 4984938 2 PubMed abstract 4982117 |
Domain Name | N/A |
Hormone Name | Thyroliberin |
Mature Hormone Sequence | QHP |
Position of mature hormone in Pre-Hormone protein | 3 Residues from position (1-3) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10477 |
Swiss-prot Accession number | P63153 (Sequence in FASTA format) |
Description | Gastrin-releasing peptide (GRP) [Contains: Neuromedin-C (GRP-10)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the bombesin/neuromedin-B/ranatensin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | GRP stimulates gastrin release as well as other gastrointestinal hormones. Operates as a negative feedback regulating fear and established a causal relationship between GRP-receptor gene expression, long-term potentiation, and amygdala-dependent memory for fear |
Protein Length | 27 Amino acids |
Molecular weight | 2806 |
References | 1 PubMed abstract 496973 2 PubMed abstract 6546686 |
Domain Name | N/A |
Hormone Name | Gastrin-releasing peptide |
Mature Hormone Sequence | APVSVGGGTVLAKMYPRGNHWAVGHLM |
Position of mature hormone in Pre-Hormone protein | 27 Residues from position (1-27) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10478 |
Swiss-prot Accession number | P63153 (Sequence in FASTA format) |
Description | Gastrin-releasing peptide (GRP) [Contains: Neuromedin-C (GRP-10)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the bombesin/neuromedin-B/ranatensin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | N/A |
Protein Length | 27 Amino acids |
Molecular weight | 2806 |
References | 1 PubMed abstract 496973 2 PubMed abstract 6546686 |
Domain Name | N/A |
Hormone Name | Neuromedin-C |
Mature Hormone Sequence | GNHWAVGHLM |
Position of mature hormone in Pre-Hormone protein | 10 Residues from position (18-27) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10506 |
Swiss-prot Accession number | P79295 (Sequence in FASTA format) |
Description | Muellerian-inhibiting factor precursor (MIS) (Anti-Muellerian hormone)(AMH) (Muellerian-inhibiting substance). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein (By similarity) |
Developmental Stage | N/A |
Similarity | Belongs to the TGF-beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | This glycoprotein, produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. It is also able to inhibit the growth of tumors derived from tissues of Muellerian duct origin |
Protein Length | 575 Amino acids |
Molecular weight | 61505 |
References | 1 Daneau I., Silversides D.W.; Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
|
Domain Name | N/A |
Hormone Name | Muellerian-inhibiting factor |
Mature Hormone Sequence | REEVSSTPALPREPRTGTEGLIFHWDWNWPPPGAWPPGGPQDPLCLVTLNGTPGNGSSPFLWVVGTLSSYEQAFLEAVRHARWGPQDLANFGLCPPSLRQAALPLLQQLQAWLGEPRGQRLVVLHLEEVSWEPTPLLKFQEPLPGEASPLELALLVLYPGPGPEVTVTGAGLPGAQSLCPTRDSGFLALAVDRPERAWRGSGLALTLRRRGNGASLSTAQLQALLFGADSRCFTRMTPALLLLPPQGPVPMPAHGRVDSMPFPQPRLSPEPEEPLPSTDPFLETLTRLVRALRGPPARIPPPSLALDPGALAGFPQGQVNLSDPAALERLLNSEEPLLLLLPPPTAVTAGVPAPLQGPVTEMWASSLARRVATEFQSAAAELRGFPGLPPTATLLLARLLALCPGDRGDPGGPLRAVLLLKALQGLRTEWRWRERSGPARAQRSAGTAVSNGPCALRELSVDLRAERSVLIPETYQANNCQGTCGWPQSDRNPRYGNHVVLLLKMQARGAALARPPCCVPTAYAGKLLISLSEERISAHHVPNMVATECGCR |
Position of mature hormone in Pre-Hormone protein | 552 Residues from position (24-575) |
Receptor | N/A |
Gene ID | 397578 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10591 |
Swiss-prot Accession number | P06296 (Sequence in FASTA format) |
Description | Corticoliberin precursor (Corticotropin-releasing factor) (CRF)(Corticotropin-releasing hormone). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | This hormone from hypothalamus regulates the release of corticotropin from pituitary gland |
Protein Length | 191 Amino acids |
Molecular weight | 21042 |
References | 1 PubMed abstract 9734873 2 PubMed abstract 12030933 3 PubMed abstract 3878520 |
Domain Name | CRF |
Hormone Name | Corticoliberin |
Mature Hormone Sequence | SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII |
Position of mature hormone in Pre-Hormone protein | 41 Residues from position (149-189) |
Receptor | N/A |
Gene ID | 100127468 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10687 |
Swiss-prot Accession number | P01300 (Sequence in FASTA format) |
Description | Pancreatic hormone precursor (Pancreatic polypeptide) (PP) (Fragment). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the NPY family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions |
Protein Length | 65 Amino acids |
Molecular weight | 7290 |
References | 1 Chance R.E., Johnson M.G., Hoffmann J.A., Lin T.-M.; (In) Baba S., Kaneko T., Yanaihara N. (eds.);Proinsulin, insulin, c-peptide, pp.419-425, Excerpta Medica, Amsterdam(1979).
2 Han X.G., Tuch B.E.; "Partial porcine pancreatic polypeptide cDNA sequence (3'end)."; Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Hormone_3 |
Hormone Name | Pancreatic hormone |
Mature Hormone Sequence | APLEPVYPGDDATPEQMAQYAAELRRYINMLTRPRY |
Position of mature hormone in Pre-Hormone protein | 36 Residues from position (1-36) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10688 |
Swiss-prot Accession number | P01300 (Sequence in FASTA format) |
Description | Pancreatic hormone precursor (Pancreatic polypeptide) (PP) (Fragment). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the NPY family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | The physiological role for the icosapeptide has not yet been elucidated |
Protein Length | 65 Amino acids |
Molecular weight | 7290 |
References | 1 Chance R.E., Johnson M.G., Hoffmann J.A., Lin T.-M.; (In) Baba S., Kaneko T., Yanaihara N. (eds.);Proinsulin, insulin, c-peptide, pp.419-425, Excerpta Medica, Amsterdam(1979).
2 Han X.G., Tuch B.E.; "Partial porcine pancreatic polypeptide cDNA sequence (3'end)."; Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Hormone_3 |
Hormone Name | Pancreatic icosapeptide |
Mature Hormone Sequence | DEEDLLDLKCSSLHAAAPR |
Position of mature hormone in Pre-Hormone protein | 19 Residues from position (40-58) |
Receptor | N/A |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10879 |
Swiss-prot Accession number | P01315 (Sequence in FASTA format) |
Description | Insulin precursor [Contains: Insulin B chain; Insulin A chain]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver |
Protein Length | 108 Amino acids |
Molecular weight | 11672 |
References | 1 Han X.G., Tuch B.E.; "Complete porcine preproinsulin cDNA sequence."; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 12140686 3 PubMed abstract 14574411 4 PubMed abstract 5657063 5 Chance R.E.; Submitted (JUL-1970) to the PIR data bank. 6 Blundell T.L., Dodson G.G., Hodgkin D., Mercola D.; "Insulin. The structure in the crystal and its reflection in chemistryand biology."; Adv. Protein Chem. 26:279-402(1972). 7 Isaacs N.W., Agarwal R.C.; "Experience with fast Fourier least squares in the refinement of thecrystal structure of rhombohedral 2-zinc insulin at 1.5-Aresolution."; Acta Crystallogr. A 34:782-791(1978). 8 PubMed abstract 2905485 9 PubMed abstract 1772633 10 PubMed abstract 2025410 11 PubMed abstract 15299880 |
Domain Name | Insulin |
Hormone Name | Insulin B chain |
Mature Hormone Sequence | FVNQHLCGSHLVEALYLVCGERGFFYTPKA |
Position of mature hormone in Pre-Hormone protein | 30 Residues from position (25-54) |
Receptor | N/A |
Gene ID | 397415 |
PDB ID | 1B17 1B18 1B19 1B2A 1B2B 1B2C 1B2D 1B2E 1B2F 1B2G 1DEI 1IZA 1IZB 1M5A 1MPJ 1SDB 1WAV 1ZEI 1ZNI 2EFA 2G4M 2TCI 3INS 3MTH 4INS 6INS 7INS 9INS |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 10880 |
Swiss-prot Accession number | P01315 (Sequence in FASTA format) |
Description | Insulin precursor [Contains: Insulin B chain; Insulin A chain]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver |
Protein Length | 108 Amino acids |
Molecular weight | 11672 |
References | 1 Han X.G., Tuch B.E.; "Complete porcine preproinsulin cDNA sequence."; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 12140686 3 PubMed abstract 14574411 4 PubMed abstract 5657063 5 Chance R.E.; Submitted (JUL-1970) to the PIR data bank. 6 Blundell T.L., Dodson G.G., Hodgkin D., Mercola D.; "Insulin. The structure in the crystal and its reflection in chemistryand biology."; Adv. Protein Chem. 26:279-402(1972). 7 Isaacs N.W., Agarwal R.C.; "Experience with fast Fourier least squares in the refinement of thecrystal structure of rhombohedral 2-zinc insulin at 1.5-Aresolution."; Acta Crystallogr. A 34:782-791(1978). 8 PubMed abstract 2905485 9 PubMed abstract 1772633 10 PubMed abstract 2025410 11 PubMed abstract 15299880 |
Domain Name | Insulin |
Hormone Name | Insulin A chain |
Mature Hormone Sequence | GIVEQCCTSICSLYQLENYCN |
Position of mature hormone in Pre-Hormone protein | 21 Residues from position (88-108) |
Receptor | N/A |
Gene ID | 397415 |
PDB ID | 1B17 1B18 1B19 1B2A 1B2B 1B2C 1B2D 1B2E 1B2F 1B2G 1DEI 1IZA 1IZB 1M5A 1MPJ 1SDB 1WAV 1ZEI 1ZNI 2EFA 2G4M 2TCI 3INS 3MTH 4INS 6INS 7INS 9INS |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11049 |
Swiss-prot Accession number | P21753 (Sequence in FASTA format) |
Description | Thymosin beta-10 (Thymosin beta-9). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Cytoplasm |
Developmental Stage | N/A |
Similarity | Belongs to the thymosin beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization |
Protein Length | 42 Amino acids |
Molecular weight | 4823 |
References | 1 Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.; "Generation and analysis of cDNA sequences derived from a porcineskeletal muscle library."; Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2774558 3 PubMed abstract 2090639 |
Domain Name | Thymosin |
Hormone Name | Thymosin beta-10 |
Mature Hormone Sequence | ADKPDMGEINSFDKAKLKKTETQEKNTLPTKETIEQEKQAK |
Position of mature hormone in Pre-Hormone protein | 41 Residues from position (2-42) |
Receptor | N/A |
Gene ID | 100037998 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11112 |
Swiss-prot Accession number | P01274 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP1 and GLP2 are also secreted in selected neurons in the brain |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | Glicentin may modulate gastric acid secretion and gastro-pyloro-duodenal activity |
Protein Length | 180 Amino acids |
Molecular weight | 21029 |
References | 1 Siggers R.H., Goldade B.G., Laarveld B., Van Kessel A.G.; "Cloning of porcine proglucagon."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6894800 3 PubMed abstract 7045833 4 Bromer W.W., Sinn L.G., Behrens O.K.; "The amino acid sequence of glucagon. V. Location of amide groups,acid degradation studies and summary of sequential evidence."; J. Am. Chem. Soc. 79:2807-2810(1957). 5 PubMed abstract 2753890 6 PubMed abstract 3379036 7 PubMed abstract 3530719 8 PubMed abstract 12554744 9 PubMed abstract 12626323 10 PubMed abstract 10322410 11 PubMed abstract 10605628 12 PubMed abstract 171582 |
Domain Name | Hormone_2 |
Hormone Name | Glicentin |
Mature Hormone Sequence | RSLQNTEEKSRSFPAPQTDPLDDPDQMTEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIA |
Position of mature hormone in Pre-Hormone protein | 69 Residues from position (21-89) |
Receptor | N/A |
Gene ID | 397595 |
PDB ID | 1GCN |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11113 |
Swiss-prot Accession number | P01274 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP1 and GLP2 are also secreted in selected neurons in the brain |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | Oxyntomodulin significantly reduces food intake |
Protein Length | 180 Amino acids |
Molecular weight | 21029 |
References | 1 Siggers R.H., Goldade B.G., Laarveld B., Van Kessel A.G.; "Cloning of porcine proglucagon."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6894800 3 PubMed abstract 7045833 4 Bromer W.W., Sinn L.G., Behrens O.K.; "The amino acid sequence of glucagon. V. Location of amide groups,acid degradation studies and summary of sequential evidence."; J. Am. Chem. Soc. 79:2807-2810(1957). 5 PubMed abstract 2753890 6 PubMed abstract 3379036 7 PubMed abstract 3530719 8 PubMed abstract 12554744 9 PubMed abstract 12626323 10 PubMed abstract 10322410 11 PubMed abstract 10605628 12 PubMed abstract 171582 |
Domain Name | Hormone_2 |
Hormone Name | Oxyntomodulin |
Mature Hormone Sequence | HSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIA |
Position of mature hormone in Pre-Hormone protein | 37 Residues from position (53-89) |
Receptor | N/A |
Gene ID | 397595 |
PDB ID | 1GCN |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11114 |
Swiss-prot Accession number | P01274 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP1 and GLP2 are also secreted in selected neurons in the brain |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia |
Protein Length | 180 Amino acids |
Molecular weight | 21029 |
References | 1 Siggers R.H., Goldade B.G., Laarveld B., Van Kessel A.G.; "Cloning of porcine proglucagon."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6894800 3 PubMed abstract 7045833 4 Bromer W.W., Sinn L.G., Behrens O.K.; "The amino acid sequence of glucagon. V. Location of amide groups,acid degradation studies and summary of sequential evidence."; J. Am. Chem. Soc. 79:2807-2810(1957). 5 PubMed abstract 2753890 6 PubMed abstract 3379036 7 PubMed abstract 3530719 8 PubMed abstract 12554744 9 PubMed abstract 12626323 10 PubMed abstract 10322410 11 PubMed abstract 10605628 12 PubMed abstract 171582 |
Domain Name | Hormone_2 |
Hormone Name | Glucagon |
Mature Hormone Sequence | HSQGTFTSDYSKYLDSRRAQDFVQWLMNT |
Position of mature hormone in Pre-Hormone protein | 29 Residues from position (53-81) |
Receptor | N/A |
Gene ID | 397595 |
PDB ID | 1GCN |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11115 |
Swiss-prot Accession number | P01274 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP1 and GLP2 are also secreted in selected neurons in the brain |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | GLP-1 is a potent stimulator of glucose-dependent insulin release. Play important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Have growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin |
Protein Length | 180 Amino acids |
Molecular weight | 21029 |
References | 1 Siggers R.H., Goldade B.G., Laarveld B., Van Kessel A.G.; "Cloning of porcine proglucagon."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6894800 3 PubMed abstract 7045833 4 Bromer W.W., Sinn L.G., Behrens O.K.; "The amino acid sequence of glucagon. V. Location of amide groups,acid degradation studies and summary of sequential evidence."; J. Am. Chem. Soc. 79:2807-2810(1957). 5 PubMed abstract 2753890 6 PubMed abstract 3379036 7 PubMed abstract 3530719 8 PubMed abstract 12554744 9 PubMed abstract 12626323 10 PubMed abstract 10322410 11 PubMed abstract 10605628 12 PubMed abstract 171582 |
Domain Name | Hormone_2 |
Hormone Name | Glucagon-like peptide 1 |
Mature Hormone Sequence | HDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG |
Position of mature hormone in Pre-Hormone protein | 37 Residues from position (92-128) |
Receptor | N/A |
Gene ID | 397595 |
PDB ID | 1GCN |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11116 |
Swiss-prot Accession number | P01274 (Sequence in FASTA format) |
Description | Glucagon precursor [Contains: Glicentin; Glicentin-related polypeptide(GRPP); Oxyntomodulin (OXY) (OXM); Glucagon; Glucagon-like peptide 1(GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-likepeptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP1 and GLP2 are also secreted in selected neurons in the brain |
Post translational modification | Proglucagon is posttranslationally processed in a tissue- specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by posttranslational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas (By similarity). |
Function | GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability |
Protein Length | 180 Amino acids |
Molecular weight | 21029 |
References | 1 Siggers R.H., Goldade B.G., Laarveld B., Van Kessel A.G.; "Cloning of porcine proglucagon."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 6894800 3 PubMed abstract 7045833 4 Bromer W.W., Sinn L.G., Behrens O.K.; "The amino acid sequence of glucagon. V. Location of amide groups,acid degradation studies and summary of sequential evidence."; J. Am. Chem. Soc. 79:2807-2810(1957). 5 PubMed abstract 2753890 6 PubMed abstract 3379036 7 PubMed abstract 3530719 8 PubMed abstract 12554744 9 PubMed abstract 12626323 10 PubMed abstract 10322410 11 PubMed abstract 10605628 12 PubMed abstract 171582 |
Domain Name | Hormone_2 |
Hormone Name | Glucagon-like peptide 2 |
Mature Hormone Sequence | HADGSFSDEMNTVLDNLATRDFINWLLHTKITDSL |
Position of mature hormone in Pre-Hormone protein | 35 Residues from position (146-180) |
Receptor | N/A |
Gene ID | 397595 |
PDB ID | 1GCN |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11152 |
Swiss-prot Accession number | P01351 (Sequence in FASTA format) |
Description | Gastrin precursor [Contains: Big gastrin (Gastrin 34) (G34); Gastrin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine |
Protein Length | 104 Amino acids |
Molecular weight | 11558 |
References | 1 PubMed abstract 6951161 2 PubMed abstract 6930858 3 PubMed abstract 14248711 4 PubMed abstract 14248712 |
Domain Name | Gastrin |
Hormone Name | Big gastrin |
Mature Hormone Sequence | QLGLQGPPHLVADLAKKQGPWMEEEEEAYGWMDF |
Position of mature hormone in Pre-Hormone protein | 34 Residues from position (59-92) |
Receptor | N/A |
Gene ID | 445524 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11153 |
Swiss-prot Accession number | P01351 (Sequence in FASTA format) |
Description | Gastrin precursor [Contains: Big gastrin (Gastrin 34) (G34); Gastrin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine |
Protein Length | 104 Amino acids |
Molecular weight | 11558 |
References | 1 PubMed abstract 6951161 2 PubMed abstract 6930858 3 PubMed abstract 14248711 4 PubMed abstract 14248712 |
Domain Name | Gastrin |
Hormone Name | Gastrin |
Mature Hormone Sequence | QGPWMEEEEEAYGWMDF |
Position of mature hormone in Pre-Hormone protein | 17 Residues from position (76-92) |
Receptor | N/A |
Gene ID | 445524 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11183 |
Swiss-prot Accession number | P01356 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | Synthesized in both cerebral cortex and duodenal mucosa |
Post translational modification | The precursor is cleaved by enzymes to produce a number of active cholecystokinins. Brain contains CCK-octapeptide (CCK8) and several CCK-desoctapeptides; whereas pig gut contains intact CCK33, CCK39, and CCK58 as well as CCK-octapeptide and the CCK- desoctapeptides. Distribution differences are due to tissue- specific post-translational processing events. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. |
Protein Length | 114 Amino acids |
Molecular weight | 12526 |
References | 1 PubMed abstract 6205394 2 Mutt V., Jorpes J.E.; Submitted (AUG-1970) to the PIR data bank. 3 PubMed abstract 5410106 4 PubMed abstract 8443599 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin |
Mature Hormone Sequence | QPVPPADSAVPGAQEEEAHRRQLRAVQKVDGESRAHLGALLARYIQQARKAPSGRVSMIKNLQSLDPSHRISDRDYMGWMDFGRRSAEEYEYTS |
Position of mature hormone in Pre-Hormone protein | 94 Residues from position (21-114) |
Receptor | N/A |
Gene ID | 397468 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11184 |
Swiss-prot Accession number | P01356 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | Synthesized in both cerebral cortex and duodenal mucosa |
Post translational modification | The precursor is cleaved by enzymes to produce a number of active cholecystokinins. Brain contains CCK-octapeptide (CCK8) and several CCK-desoctapeptides; whereas pig gut contains intact CCK33, CCK39, and CCK58 as well as CCK-octapeptide and the CCK- desoctapeptides. Distribution differences are due to tissue- specific post-translational processing events. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. |
Protein Length | 114 Amino acids |
Molecular weight | 12526 |
References | 1 PubMed abstract 6205394 2 Mutt V., Jorpes J.E.; Submitted (AUG-1970) to the PIR data bank. 3 PubMed abstract 5410106 4 PubMed abstract 8443599 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-58 |
Mature Hormone Sequence | AVQKVDGESRAHLGALLARYIQQARKAPSGRVSMIKNLQSLDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 58 Residues from position (45-102) |
Receptor | N/A |
Gene ID | 397468 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11185 |
Swiss-prot Accession number | P01356 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | Synthesized in both cerebral cortex and duodenal mucosa |
Post translational modification | The precursor is cleaved by enzymes to produce a number of active cholecystokinins. Brain contains CCK-octapeptide (CCK8) and several CCK-desoctapeptides; whereas pig gut contains intact CCK33, CCK39, and CCK58 as well as CCK-octapeptide and the CCK- desoctapeptides. Distribution differences are due to tissue- specific post-translational processing events. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. |
Protein Length | 114 Amino acids |
Molecular weight | 12526 |
References | 1 PubMed abstract 6205394 2 Mutt V., Jorpes J.E.; Submitted (AUG-1970) to the PIR data bank. 3 PubMed abstract 5410106 4 PubMed abstract 8443599 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-39 |
Mature Hormone Sequence | YIQQARKAPSGRVSMIKNLQSLDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 39 Residues from position (64-102) |
Receptor | N/A |
Gene ID | 397468 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11186 |
Swiss-prot Accession number | P01356 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | Synthesized in both cerebral cortex and duodenal mucosa |
Post translational modification | The precursor is cleaved by enzymes to produce a number of active cholecystokinins. Brain contains CCK-octapeptide (CCK8) and several CCK-desoctapeptides; whereas pig gut contains intact CCK33, CCK39, and CCK58 as well as CCK-octapeptide and the CCK- desoctapeptides. Distribution differences are due to tissue- specific post-translational processing events. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. |
Protein Length | 114 Amino acids |
Molecular weight | 12526 |
References | 1 PubMed abstract 6205394 2 Mutt V., Jorpes J.E.; Submitted (AUG-1970) to the PIR data bank. 3 PubMed abstract 5410106 4 PubMed abstract 8443599 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-33 |
Mature Hormone Sequence | KAPSGRVSMIKNLQSLDPSHRISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 33 Residues from position (70-102) |
Receptor | N/A |
Gene ID | 397468 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11187 |
Swiss-prot Accession number | P01356 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | Synthesized in both cerebral cortex and duodenal mucosa |
Post translational modification | The precursor is cleaved by enzymes to produce a number of active cholecystokinins. Brain contains CCK-octapeptide (CCK8) and several CCK-desoctapeptides; whereas pig gut contains intact CCK33, CCK39, and CCK58 as well as CCK-octapeptide and the CCK- desoctapeptides. Distribution differences are due to tissue- specific post-translational processing events. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. |
Protein Length | 114 Amino acids |
Molecular weight | 12526 |
References | 1 PubMed abstract 6205394 2 Mutt V., Jorpes J.E.; Submitted (AUG-1970) to the PIR data bank. 3 PubMed abstract 5410106 4 PubMed abstract 8443599 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-12 |
Mature Hormone Sequence | ISDRDYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 12 Residues from position (91-102) |
Receptor | N/A |
Gene ID | 397468 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11188 |
Swiss-prot Accession number | P01356 (Sequence in FASTA format) |
Description | Cholecystokinins precursor (CCK) [Contains: Cholecystokinin 58(CCK58); Cholecystokinin 39 (CCK39); Cholecystokinin 33 (CCK33);Cholecystokinin 12 (CCK12); Cholecystokinin 8 (CCK8)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the gastrin/cholecystokinin family. |
Tissue Specificity | Synthesized in both cerebral cortex and duodenal mucosa |
Post translational modification | The precursor is cleaved by enzymes to produce a number of active cholecystokinins. Brain contains CCK-octapeptide (CCK8) and several CCK-desoctapeptides; whereas pig gut contains intact CCK33, CCK39, and CCK58 as well as CCK-octapeptide and the CCK- desoctapeptides. Distribution differences are due to tissue- specific post-translational processing events. |
Function | This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. |
Protein Length | 114 Amino acids |
Molecular weight | 12526 |
References | 1 PubMed abstract 6205394 2 Mutt V., Jorpes J.E.; Submitted (AUG-1970) to the PIR data bank. 3 PubMed abstract 5410106 4 PubMed abstract 8443599 |
Domain Name | Gastrin |
Hormone Name | Cholecystokinin-8 |
Mature Hormone Sequence | DYMGWMDF |
Position of mature hormone in Pre-Hormone protein | 8 Residues from position (95-102) |
Receptor | N/A |
Gene ID | 397468 |
PDB ID | N/A |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11221 |
Swiss-prot Accession number | P01348 (Sequence in FASTA format) |
Description | Prorelaxin precursor [Contains: Relaxin B chain; Relaxin A chain]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals |
Protein Length | 182 Amino acids |
Molecular weight | 20818 |
References | 1 PubMed abstract 6897721 2 PubMed abstract 2442155 3 PubMed abstract 876374 4 PubMed abstract 851452 5 PubMed abstract 843375 6 PubMed abstract 938497 7 PubMed abstract 887933 8 PubMed abstract 622170 |
Domain Name | Insulin |
Hormone Name | Relaxin B chain |
Mature Hormone Sequence | QSTNDFIKACGRELVRLWVEICGSVSWGRTAL |
Position of mature hormone in Pre-Hormone protein | 32 Residues from position (25-56) |
Receptor | N/A |
Gene ID | 396891 |
PDB ID | 1RLX 2RLX 3RLX 4RLX |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11222 |
Swiss-prot Accession number | P01348 (Sequence in FASTA format) |
Description | Prorelaxin precursor [Contains: Relaxin B chain; Relaxin A chain]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the insulin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals |
Protein Length | 182 Amino acids |
Molecular weight | 20818 |
References | 1 PubMed abstract 6897721 2 PubMed abstract 2442155 3 PubMed abstract 876374 4 PubMed abstract 851452 5 PubMed abstract 843375 6 PubMed abstract 938497 7 PubMed abstract 887933 8 PubMed abstract 622170 |
Domain Name | Insulin |
Hormone Name | Relaxin A chain |
Mature Hormone Sequence | RMTLSEKCCQVGCIRKDIARLC |
Position of mature hormone in Pre-Hormone protein | 22 Residues from position (161-182) |
Receptor | N/A |
Gene ID | 396891 |
PDB ID | 1RLX 2RLX 3RLX 4RLX |
Drugpedia | wiki |
Comments | !Receptor for this Hormone are either unknown or have not yet been curated |
HMRbase accession number | 11246 |
Swiss-prot Accession number | P01168 (Sequence in FASTA format) |
Description | Somatostatin precursor [Contains: Somatostatin-28; Somatostatin-14]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the somatostatin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Somatostatin inhibits the release of somatotropin |
Protein Length | 116 Amino acids |
Molecular weight | 12689 |
References | 1 Liu D., Zhang Y., Zhang X., Yang G.; "Study on SNPs of porcine somatostatin gene."; Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2567292 3 PubMed abstract 2865169 4 PubMed abstract 7353633 5 PubMed abstract 6107906 6 PubMed abstract 1252409 7 Riquet J.; Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Somatostatin |
Hormone Name | Somatostatin-28 |
Mature Hormone Sequence | SANSNPAMAPRERKAGCKNFFWKTFTSC |
Position of mature hormone in Pre-Hormone protein | 28 Residues from position (89-116) |
Receptor | P34994 Detail in HMRbase Q2Q1V0 Detail in HMRbase Q6YEX9 Detail in HMRbase Q6YEY1 Detail in HMRbase Q866U3 Detail in HMRbase |
Gene ID | 494469 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11247 |
Swiss-prot Accession number | P01168 (Sequence in FASTA format) |
Description | Somatostatin precursor [Contains: Somatostatin-28; Somatostatin-14]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the somatostatin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Somatostatin inhibits the release of somatotropin |
Protein Length | 116 Amino acids |
Molecular weight | 12689 |
References | 1 Liu D., Zhang Y., Zhang X., Yang G.; "Study on SNPs of porcine somatostatin gene."; Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 2567292 3 PubMed abstract 2865169 4 PubMed abstract 7353633 5 PubMed abstract 6107906 6 PubMed abstract 1252409 7 Riquet J.; Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Somatostatin |
Hormone Name | Somatostatin-14 |
Mature Hormone Sequence | AGCKNFFWKTFTSC |
Position of mature hormone in Pre-Hormone protein | 14 Residues from position (103-116) |
Receptor | P34994 Detail in HMRbase Q2Q1V0 Detail in HMRbase Q6YEX9 Detail in HMRbase Q6YEY1 Detail in HMRbase Q866U3 Detail in HMRbase |
Gene ID | 494469 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11248 |
Swiss-prot Accession number | P01177 (Sequence in FASTA format) |
Description | Oxytocin-neurophysin 1 precursor (OT-NPI) [Contains: Oxytocin(Ocytocin); Neurophysin 1]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the vasopressin/oxytocin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland |
Protein Length | 125 Amino acids |
Molecular weight | 12887 |
References | 1 PubMed abstract 1971513 2 PubMed abstract 13022701 3 PubMed abstract 428540 |
Domain Name | Hormone_5 |
Hormone Name | Oxytocin |
Mature Hormone Sequence | CYIQNCPLG |
Position of mature hormone in Pre-Hormone protein | 9 Residues from position (20-28) |
Receptor | P32306
Detail in HMRbase |
Gene ID | 100152272 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11274 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Melanotropin gamma (Gamma-MSH) |
Mature Hormone Sequence | YVMGHFRWDRF |
Position of mature hormone in Pre-Hormone protein | 11 Residues from position (77-87) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11275 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | ACTH stimulates the adrenal glands to release cortisol |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Corticotropin |
Mature Hormone Sequence | SYSMEHFRWGKPVGKKRRPVKVYPNGAEDELAEAFPLEF |
Position of mature hormone in Pre-Hormone protein | 39 Residues from position (136-174) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11276 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Melanotropin alpha (Alpha-MSH) |
Mature Hormone Sequence | SYSMEHFRWGKPV |
Position of mature hormone in Pre-Hormone protein | 13 Residues from position (136-148) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11277 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | Stimulates melanocytes to produce melanin. It performs lipid-mobilizing functions such as lipolysis and steroidogenesis. |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Lipotropin beta (Beta-LPH) |
Mature Hormone Sequence | ELAGAPPEPARDPEAPAEGAAARAELEYGLVAEAEAAEKKDEGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIVKNAHKKGQ |
Position of mature hormone in Pre-Hormone protein | 91 Residues from position (177-267) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11278 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | Stimulates melanocytes to produce melanin. It performs lipid-mobilizing functions such as lipolysis and steroidogenesis. |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Lipotropin gamma (Gamma-LPH) |
Mature Hormone Sequence | ELAGAPPEPARDPEAPAEGAAARAELEYGLVAEAEAAEKKDEGPYKMEHFRWGSPPKD |
Position of mature hormone in Pre-Hormone protein | 58 Residues from position (177-234) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11279 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Melanotropin beta (Beta-MSH) |
Mature Hormone Sequence | DEGPYKMEHFRWGSPPKD |
Position of mature hormone in Pre-Hormone protein | 18 Residues from position (217-234) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11280 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | Beta-endorphin is an endogenous opiate |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Beta-endorphin |
Mature Hormone Sequence | YGGFMTSEKSQTPLVTLFKNAIVKNAHKKGQ |
Position of mature hormone in Pre-Hormone protein | 31 Residues from position (237-267) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11281 |
Swiss-prot Accession number | P01192 (Sequence in FASTA format) |
Description | Corticotropin-lipotropin precursor (Pro-opiomelanocortin) (POMC)[Contains: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin(Adrenocorticotropic hormone) (ACTH); Melanotropin alpha (Alpha-MSH);Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanotropin beta (Beta-MSH);Beta-endorphin; Met-enkephalin]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | N/A |
Developmental Stage | N/A |
Similarity | Belongs to the POMC family. |
Tissue Specificity | ACTH and MSH are produced by the pituitary gland |
Post translational modification | Specific enzymatic cleavages at paired basic residues yield the different active peptides. |
Function | Met-enkephalin is an endogenous opiate |
Protein Length | 267 Amino acids |
Molecular weight | 28895 |
References | 1 PubMed abstract 3753882 2 PubMed abstract 6196724 3 PubMed abstract 7958386 4 PubMed abstract 6547437 5 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 6 PubMed abstract 4334191 7 PubMed abstract 4369114 8 PubMed abstract 2174774 9 PubMed abstract 13451616 10 PubMed abstract 5543613 11 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 12 PubMed abstract 4673865 13 PubMed abstract 13348631 14 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 15 PubMed abstract 1207728 16 PubMed abstract 1007884 17 PubMed abstract 3753882 18 PubMed abstract 6196724 19 PubMed abstract 7958386 20 PubMed abstract 6547437 21 Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,Davis S.B., Eigner E.A., Shakespeare N.E.; "Studies with corticotropin. III. Determination of the structure ofbeta-corticotropin and its active degradation products."; J. Am. Chem. Soc. 78:5067-5076(1956). 22 PubMed abstract 4334191 23 PubMed abstract 4369114 24 PubMed abstract 2174774 25 PubMed abstract 13451616 26 PubMed abstract 5543613 27 Gilardeau C., Chretien M.; "Complete amino acid sequence of porcine beta-lipotropic hormone(beta-LPH)."; (In) Meienhofer J. (eds.);Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub.,Ann Arbor (1972). 28 PubMed abstract 4673865 29 PubMed abstract 13348631 30 Geschwind I.I., Li C.H., Barnafi L.; "The structure of the beta-melanocyte-stimulating hormone."; J. Am. Chem. Soc. 79:620-625(1957). 31 PubMed abstract 1207728 32 PubMed abstract 1007884 |
Domain Name | ACTH_domain NPP Op_neuropeptide |
Hormone Name | Met-enkephalin |
Mature Hormone Sequence | YGGFM |
Position of mature hormone in Pre-Hormone protein | 5 Residues from position (237-241) |
Receptor | Q9TU05
Detail in HMRbase |
Gene ID | 396863 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11303 |
Swiss-prot Accession number | P01219 (Sequence in FASTA format) |
Description | Glycoprotein hormones alpha chain precursor (Anterior pituitaryglycoprotein hormones common subunit alpha) (Follitropin alpha chain)(Follicle-stimulating hormone alpha chain) (FSH-alpha) (Lutropin alphachain) (Luteinizing hormone alpha chain) (LSH-alpha) (Thyrotropinalpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit alpha family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | N/A |
Protein Length | 120 Amino acids |
Molecular weight | 13532 |
References | 1 PubMed abstract 2473932 2 Kato Y., Ezashi T., Hirai T., Kato T.; Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases. 3 PubMed abstract 4770796 4 Closset J., Maghuin-Rogister G., Hennen G.; Endocrinol. Exp. 8:164-164(1974). 5 PubMed abstract 4448287 6 PubMed abstract 2473932 7 Kato Y., Ezashi T., Hirai T., Kato T.; Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases. 8 PubMed abstract 4770796 9 Closset J., Maghuin-Rogister G., Hennen G.; Endocrinol. Exp. 8:164-164(1974). 10 PubMed abstract 4448287 |
Domain Name | Hormone_6 |
Hormone Name | Glycoprotein hormones alpha chain |
Mature Hormone Sequence | FPDGEFTMQGCPECKLKENKYFSKLGAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNARVENHTECHCSTCYYHKS |
Position of mature hormone in Pre-Hormone protein | 96 Residues from position (25-120) |
Receptor | P49059 Detail in HMRbase P16582 Detail in HMRbase Q8SPP9 Detail in HMRbase |
Gene ID | 406869 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11307 |
Swiss-prot Accession number | P01224 (Sequence in FASTA format) |
Description | Thyrotropin subunit beta precursor (Thyroid-stimulating hormonesubunit beta) (TSH-beta) (TSH-B) (Thyrotropin beta chain). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Indispensable for the control of thyroid structure and metabolism |
Protein Length | 138 Amino acids |
Molecular weight | 15761 |
References | 1 PubMed abstract 2473932 2 PubMed abstract 8880412 3 PubMed abstract 1245181 |
Domain Name | Cys_knot |
Hormone Name | Thyroid-stimulating hormone subunit beta (TSH-B) (Thyrotropin beta chain) |
Mature Hormone Sequence | FCIPTEYMMHVERKECAYCLTINTTICAGYCMTRDFNGKLFLPKYALSQDVCTYRDFMYKTVEIPGCPHHVTPYFSYPVAISCKCGKCNTDYSDCIHEAIKTNYCTKPQKSY |
Position of mature hormone in Pre-Hormone protein | 112 Residues from position (21-132) |
Receptor | Q8SPP9
Detail in HMRbase |
Gene ID | 397658 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11310 |
Swiss-prot Accession number | P01228 (Sequence in FASTA format) |
Description | Follitropin subunit beta precursor (Follicle-stimulating hormone betasubunit) (FSH-beta) (FSH-B) (Follitropin beta chain). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Stimulates development of follicle and spermatogenesis in the reproductive organs |
Protein Length | 129 Amino acids |
Molecular weight | 14605 |
References | 1 PubMed abstract 2174241 2 PubMed abstract 10690358 3 PubMed abstract 3129323 4 PubMed abstract 658036 5 PubMed abstract 2174241 6 PubMed abstract 10690358 7 PubMed abstract 3129323 8 PubMed abstract 658036 |
Domain Name | Cys_knot |
Hormone Name | Follicle-stimulating hormone beta subunit |
Mature Hormone Sequence | CELTNITITVEKEECNFCISINTTWCAGYCYTRDLVYKDPARPNIQKTCTFKELVYETVKVPGCAHHADSLYTYPVATECHCGKCDSDSTDCTVRGLGPSYCSFSEMKE |
Position of mature hormone in Pre-Hormone protein | 109 Residues from position (21-129) |
Receptor | P49059
Detail in HMRbase |
Gene ID | 396895 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11313 |
Swiss-prot Accession number | P01232 (Sequence in FASTA format) |
Description | Lutropin subunit beta precursor (Luteinizing hormone subunit beta)(LSH-beta) (LSH-B) (LH-B) (Lutropin beta chain). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the glycoprotein hormones subunit beta family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids |
Protein Length | 141 Amino acids |
Molecular weight | 14889 |
References | 1 PubMed abstract 2744222 2 PubMed abstract 1701088 3 Lv X., Gao R., Liu S., Li J.; "The sequence and expression of Meishan porcine LH-beta gene."; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. 4 PubMed abstract 4770795 |
Domain Name | Cys_knot |
Hormone Name | Luteinizing hormone subunit beta (LSH-B) (LH-B)(Lutropin subunit beta) |
Mature Hormone Sequence | SRGPLRPLCRPINATLAAENEACPVCITFTTSICAGYCPSMVRVLPAALPPVPQPVCTYRELSFASIRLPGCPPGVDPTVSFPVALSCHCGPCRLSSSDCGGPRAQPLACDRPLLPGLLFL |
Position of mature hormone in Pre-Hormone protein | 121 Residues from position (21-141) |
Receptor | P16582
Detail in HMRbase |
Gene ID | 397153 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11316 |
Swiss-prot Accession number | P01238 (Sequence in FASTA format) |
Description | Prolactin precursor (PRL). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the somatotropin/prolactin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Prolactin acts primarily on the mammary gland by promoting lactation |
Protein Length | 229 Amino acids |
Molecular weight | 26141 |
References | 1 PubMed abstract 2726463 2 PubMed abstract 2344390 3 PubMed abstract 1270193 |
Domain Name | Hormone_1 |
Hormone Name | Prolactin |
Mature Hormone Sequence | LPICPSGAVNCQVSLRDLFDRAVILSHYIHNLSSEMFNEFDKRYAQGRGFITKAINSCHTSSLSTPEDKEQAQQIHHEVLLNLILRVLRSWNDPLYHLVTEVRGMQEAPDAILSRAIEIEEQNKRLLEGMEKIVGQVHPGIKENEVYSVWSGLPSLQMADEDTRLFAFYNLLHCLRRDSHKIDNYLKLLKCRIIYDSNC |
Position of mature hormone in Pre-Hormone protein | 199 Residues from position (31-229) |
Receptor | Q6JTA8
Detail in HMRbase |
Gene ID | 396965 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11322 |
Swiss-prot Accession number | P01248 (Sequence in FASTA format) |
Description | Somatotropin precursor (Growth hormone). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the somatotropin/prolactin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues |
Protein Length | 216 Amino acids |
Molecular weight | 24429 |
References | 1 PubMed abstract 3666458 2 PubMed abstract 2182128 3 PubMed abstract 2491309 4 PubMed abstract 4918150 5 PubMed abstract 6303731 6 PubMed abstract 1343826 7 Jiang Z.H., Rottmann O.J., Pirchner F.; Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. |
Domain Name | Hormone_1 |
Hormone Name | Growth hormone (Somatotropin) (GH) |
Mature Hormone Sequence | FPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF |
Position of mature hormone in Pre-Hormone protein | 190 Residues from position (27-216) |
Receptor | P19756
Detail in HMRbase |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11325 |
Swiss-prot Accession number | P01259 (Sequence in FASTA format) |
Description | Calcitonin. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted |
Developmental Stage | N/A |
Similarity | Belongs to the calcitonin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones |
Protein Length | 32 Amino acids |
Molecular weight | 3607 |
References | 1 PubMed abstract 5240032 2 PubMed abstract 5462122 3 PubMed abstract 5693288 |
Domain Name | Calc_CGRP_IAPP |
Hormone Name | Calcitonin |
Mature Hormone Sequence | CSNLSTCVLSAYWRNLNNFHRFSGMGFGPETP |
Position of mature hormone in Pre-Hormone protein | 32 Residues from position (1-32) |
Receptor | P25117
Detail in HMRbase |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11327 |
Swiss-prot Accession number | P01269 (Sequence in FASTA format) |
Description | Parathyroid hormone precursor (Parathyrin) (PTH). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the parathyroid hormone family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion |
Protein Length | 115 Amino acids |
Molecular weight | 12852 |
References | 1 PubMed abstract 3628009 2 PubMed abstract 1164500 3 PubMed abstract 4840833 |
Domain Name | Parathyroid |
Hormone Name | Parathyroid hormone (Parathyrin) (PTH) |
Mature Hormone Sequence | SVSEIQLMHNLGKHLSSLERVEWLRKKLQDVHNFVALGASIVHRDGGSQRPRKKEDNVLVESHQKSLGEADKAAVDVLIKAKPQ |
Position of mature hormone in Pre-Hormone protein | 84 Residues from position (32-115) |
Receptor | P50133
Detail in HMRbase |
Gene ID | 399502 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11335 |
Swiss-prot Accession number | P01287 (Sequence in FASTA format) |
Description | Somatoliberin (Growth hormone-releasing factor) (GRF) (Growth hormone-releasing hormone) (GHRH). |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the glucagon family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone |
Protein Length | 44 Amino acids |
Molecular weight | 5110 |
References | 1 PubMed abstract 6418166 |
Domain Name | Hormone_2 |
Hormone Name | Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH) |
Mature Hormone Sequence | YADAIFTNSYRKVLGQLSARKLLQDIMSRQQGERNQEQGARVRL |
Position of mature hormone in Pre-Hormone protein | 44 Residues from position (1-44) |
Receptor | P34999
Detail in HMRbase |
Gene ID | N/A |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11470 |
Swiss-prot Accession number | P49921 (Sequence in FASTA format) |
Description | Progonadoliberin-1 precursor (Progonadoliberin I) [Contains:Gonadoliberin-1 (Gonadoliberin I) (Luteinizing hormone-releasinghormone I) (LH-RH I) (Gonadotropin-releasing hormone I) (GnRH-I)(Luliberin I); GnRH-associated peptide 1 (GnRH-associated peptide I)]. |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted protein |
Developmental Stage | N/A |
Similarity | Belongs to the GnRH family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones |
Protein Length | 91 Amino acids |
Molecular weight | 10090 |
References | 1 Weesner G.D., Matteri R.L., Becker B.A.; Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
2 PubMed abstract 4946067 3 PubMed abstract 4942726 4 PubMed abstract 4946275 |
Domain Name | N/A |
Hormone Name | Gonadoliberin-1 |
Mature Hormone Sequence | QHWSYGLRPG |
Position of mature hormone in Pre-Hormone protein | 10 Residues from position (24-33) |
Receptor | P49922
Detail in HMRbase |
Gene ID | 397516 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |
HMRbase accession number | 11537 |
Swiss-prot Accession number | Q29406 (Sequence in FASTA format) |
Description | Leptin;Alternative Name: Obesity factor; Precursor |
Source organism | Sus scrofa (Pig) |
Taxonomical Classification | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;Sus. |
Subcellular location | Secreted (Probable) |
Developmental Stage | N/A |
Similarity | Belongs to the leptin family. |
Tissue Specificity | N/A |
Post translational modification | N/A |
Function | May function as part of a signaling pathway that acts to regulate the size of the body fat depot. An increase in the level of LEP may act directly or indirectly on the CNS to inhibit food intake and/or regulate energy expenditure as part of a homeostatic mechanism to maintain constancy of the adipose mass. |
Protein Length | 167 Amino acids |
Molecular weight | 18661 |
References | 1 PubMed abstract 8856925 |
Domain Name | Leptin |
Hormone Name | Leptin |
Mature Hormone Sequence | |
Position of mature hormone in Pre-Hormone protein | |
Receptor | O02671 Detail in HMRbase |
Gene ID | 396832 |
PDB ID | N/A |
Drugpedia | wiki |
Comments |