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Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanocyte-stimulating hormone beta (Beta-MSH) (Melanotropin beta); Beta-endorphin; Met-enkephalin]

 COLI_BOVIN              Reviewed;         265 AA.
P01190; Q05B64; Q28166; Q28167; Q28168;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 140.
RecName: Full=Pro-opiomelanocortin;
Short=POMC;
AltName: Full=Corticotropin-lipotropin;
Contains:
RecName: Full=NPP;
Contains:
RecName: Full=Melanotropin gamma;
AltName: Full=Gamma-MSH;
Contains:
RecName: Full=Corticotropin;
AltName: Full=Adrenocorticotropic hormone;
Short=ACTH;
Contains:
RecName: Full=Melanocyte-stimulating hormone alpha;
Short=Alpha-MSH;
AltName: Full=Melanotropin alpha;
Contains:
RecName: Full=Corticotropin-like intermediary peptide;
Short=CLIP;
Contains:
RecName: Full=Lipotropin beta;
AltName: Full=Beta-LPH;
Contains:
RecName: Full=Lipotropin gamma;
AltName: Full=Gamma-LPH;
Contains:
RecName: Full=Melanocyte-stimulating hormone beta;
Short=Beta-MSH;
AltName: Full=Melanotropin beta;
Contains:
RecName: Full=Beta-endorphin;
Contains:
RecName: Full=Met-enkephalin;
Flags: Precursor;
Name=POMC;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=221818; DOI=10.1038/278423a0;
Nakanishi S., Inoue A., Kita T., Nakamura M., Chang A.C.Y.,
Cohen S.N., Numa S.;
"Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-
lipotropin precursor.";
Nature 278:423-427(1979).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6249166; DOI=10.1111/j.1749-6632.1980.tb47270.x;
Cohen S.N., Chang A.C.Y., Nakanishi S., Inoue A., Kita T.,
Nakamura M., Numa S.;
"Studies of cloned DNA encoding the structure for the bovine
corticotropin-beta-lipotropin precursor protein.";
Ann. N. Y. Acad. Sci. 343:415-425(1980).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6263630;
Nakanishi S., Teranishi Y., Watanabe Y., Notake M., Noda M.,
Kakidani H., Jingami H., Numa S.;
"Isolation and characterization of the bovine corticotropin/beta-
lipotropin precursor gene.";
Eur. J. Biochem. 115:429-438(1981).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Hypothalamus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 75-265.
Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,
Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,
Zhvirblis G.S., Skryabin K.G., Baev A.A.;
"Genetic engineering of peptide hormones.";
Mol. Biol. (Mosk.) 19:226-235(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 132-200.
PubMed=216007; DOI=10.1073/pnas.75.12.6021;
Nakanishi G., Inoue A., Kita T., Numa S., Chang A.C.Y., Cohen S.N.,
Nunberg J., Schimke R.T.;
"Construction of bacterial plasmids that contain the nucleotide
sequence for bovine corticotropin-beta-lipotropin precursor.";
Proc. Natl. Acad. Sci. U.S.A. 75:6021-6025(1978).
[7]
PROTEIN SEQUENCE OF 77-87, AND AMIDATION AT PHE-87.
PubMed=7274457; DOI=10.1016/0014-5793(81)81081-2;
Boehlen P., Esch F., Shibasaki T., Baird A., Ling N., Guillemin R.;
"Isolation and characterization of a gamma 1-melanotropin-like peptide
from bovine neurointermediate pituitary.";
FEBS Lett. 128:67-70(1981).
[8]
PROTEIN SEQUENCE OF 131-144, AND AMIDATION AT VAL-144.
PubMed=13642798;
Li C.H.;
"The relation of chemical structure to the biologic activity of
pituitary hormones.";
Lab. Invest. 8:574-587(1959).
[9]
PROTEIN SEQUENCE OF 132-170.
Li C.H., Dixon J.S., Chung D.;
"Isolation of melatonin, the pineal gland factor that lightens
melanocytes.";
J. Am. Chem. Soc. 80:2587-2588(1958).
[10]
SEQUENCE REVISION (CORTICOTROPIN).
PubMed=4344689; DOI=10.1016/0006-291X(72)90486-X;
Li C.H.;
"Adrenocorticotropin 45. Revised amino acid sequences for sheep and
bovine hormones.";
Biochem. Biophys. Res. Commun. 49:835-839(1972).
[11]
PROTEIN SEQUENCE OF 173-265.
Pankov Y.A.;
"Primary structure of the bovine beta-lipotropic hormone.";
Vopr. Med. Khim. 19:330-332(1973).
[12]
PROTEIN SEQUENCE OF 215-232.
Geschwind I.I., Li C.H., Barnafi L.;
"The isolation and structure of a melanocyte-stimulating hormone from
bovine pituitary glands.";
J. Am. Chem. Soc. 79:1003-1004(1957).
[13]
PROTEIN SEQUENCE OF 215-232.
PubMed=13348631; DOI=10.1038/178090a0;
Harris J.I., Roos P.;
"Amino-acid sequence of a melanophore-stimulating peptide.";
Nature 178:90-90(1956).
[14]
PROTEIN SEQUENCE OF 235-239.
PubMed=1065904; DOI=10.1073/pnas.73.7.2515;
Simantov R., Snyder S.H.;
"Morphine-like peptides in mammalian brain: isolation, structure
elucidation, and interactions with the opiate receptor.";
Proc. Natl. Acad. Sci. U.S.A. 73:2515-2519(1976).
[15]
GLYCOSYLATION AT THR-71 AND ASN-91, AND DISULFIDE BONDS.
PubMed=4030947; DOI=10.1016/S0021-9673(01)87458-6;
James S., Bennett H.P.J.;
"Use of reversed-phase and ion-exchange batch extraction in the
purification of bovine pituitary peptides.";
J. Chromatogr. A 326:329-338(1985).
[16]
SULFATION AT TYR-200, AND PYROGLUTAMATE FORMATION AT GLU-173.
PubMed=2266117;
Bateman A., Solomon S., Bennett H.P.J.;
"Post-translational modification of bovine pro-opiomelanocortin.
Tyrosine sulfation and pyroglutamate formation, a mass spectrometric
study.";
J. Biol. Chem. 265:22130-22136(1990).
-!- FUNCTION: Corticotropin: Stimulates the adrenal glands to release
cortisol.
-!- FUNCTION: Melanocyte-stimulating hormone alpha: Anorexigenic
peptide. Increases the pigmentation of skin by increasing melanin
production in melanocytes.
-!- FUNCTION: Beta-endorphin: Endogenous orexigenic opiate.
-!- FUNCTION: Met-enkephalin: Endogenous opiate.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}.
Note=Melanocyte-stimulating hormone alpha and beta-endorphin are
stored in separate granules in hypothalamic POMC neurons,
suggesting that secretion may be under the control of different
regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
-!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary
gland.
-!- PTM: Specific enzymatic cleavages at paired basic residues yield
the different active peptides.
-!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA30414.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V00107; CAA23441.1; -; mRNA.
EMBL; V00107; CAA23440.1; -; mRNA.
EMBL; M25587; AAA30354.1; -; mRNA.
EMBL; J00021; AAB59262.1; -; Genomic_DNA.
EMBL; J00019; AAB59262.1; JOINED; Genomic_DNA.
EMBL; BC122728; AAI22729.1; -; mRNA.
EMBL; M23814; AAA30414.1; ALT_INIT; mRNA.
EMBL; M10723; AAA30718.1; -; mRNA.
PIR; A93206; CTBOP.
RefSeq; NP_776576.1; NM_174151.1.
RefSeq; XP_005212977.1; XM_005212920.2.
UniGene; Bt.8797; -.
STRING; 9913.ENSBTAP00000010386; -.
UniCarbKB; P01190; -.
PaxDb; P01190; -.
Ensembl; ENSBTAT00000010386; ENSBTAP00000010386; ENSBTAG00000007897.
GeneID; 281416; -.
KEGG; bta:281416; -.
CTD; 5443; -.
eggNOG; ENOG410IKR5; Eukaryota.
eggNOG; ENOG410Z5R4; LUCA.
GeneTree; ENSGT00390000016811; -.
HOGENOM; HOG000111887; -.
HOVERGEN; HBG004341; -.
InParanoid; P01190; -.
KO; K05228; -.
OMA; RACKPDL; -.
OrthoDB; EOG091G0V3J; -.
TreeFam; TF333215; -.
Reactome; R-BTA-111885; Opioid Signalling.
Reactome; R-BTA-193048; Androgen biosynthesis.
Reactome; R-BTA-194002; Glucocorticoid biosynthesis.
Reactome; R-BTA-202040; G-protein activation.
Reactome; R-BTA-209952; Peptide hormone biosynthesis.
Reactome; R-BTA-211976; Endogenous sterols.
Reactome; R-BTA-375276; Peptide ligand-binding receptors.
Reactome; R-BTA-418555; G alpha (s) signalling events.
Reactome; R-BTA-418594; G alpha (i) signalling events.
Proteomes; UP000009136; Chromosome 11.
Bgee; ENSBTAG00000007897; -.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central.
GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
GO; GO:0070996; F:type 1 melanocortin receptor binding; IEA:Ensembl.
GO; GO:0031781; F:type 3 melanocortin receptor binding; IEA:Ensembl.
GO; GO:0031782; F:type 4 melanocortin receptor binding; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
GO; GO:0033059; P:cellular pigmentation; IEA:Ensembl.
GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0032098; P:regulation of appetite; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:2000852; P:regulation of corticosterone secretion; IBA:GO_Central.
GO; GO:0070873; P:regulation of glycogen metabolic process; IEA:Ensembl.
InterPro; IPR013531; Mcrtin_ACTH_cent.
InterPro; IPR013593; Melanocortin_N.
InterPro; IPR013532; Opioid_neuropept.
InterPro; IPR001941; PMOC.
Pfam; PF00976; ACTH_domain; 3.
Pfam; PF08384; NPP; 1.
Pfam; PF08035; Op_neuropeptide; 1.
PRINTS; PR00383; MELANOCORTIN.
SMART; SM01363; ACTH_domain; 3.
SMART; SM01364; NPP; 1.
SMART; SM01365; Op_neuropeptide; 1.
1: Evidence at protein level;
Acetylation; Amidation; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endorphin; Glycoprotein; Hormone; Phosphoprotein;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
Sulfation.
SIGNAL 1 26 {ECO:0000250}.
PEPTIDE 27 103 NPP.
/FTId=PRO_0000024943.
PEPTIDE 77 87 Melanotropin gamma.
/FTId=PRO_0000024944.
PROPEP 106 129
/FTId=PRO_0000024945.
PEPTIDE 132 170 Corticotropin.
/FTId=PRO_0000024946.
PEPTIDE 132 144 Melanocyte-stimulating hormone alpha.
/FTId=PRO_0000024947.
PEPTIDE 150 170 Corticotropin-like intermediary peptide.
/FTId=PRO_0000024948.
PEPTIDE 173 265 Lipotropin beta.
/FTId=PRO_0000024949.
PEPTIDE 173 232 Lipotropin gamma.
/FTId=PRO_0000024950.
PEPTIDE 215 232 Melanocyte-stimulating hormone beta.
/FTId=PRO_0000024951.
PEPTIDE 235 265 Beta-endorphin.
/FTId=PRO_0000024952.
PEPTIDE 235 239 Met-enkephalin.
/FTId=PRO_0000024953.
MOD_RES 87 87 Phenylalanine amide.
{ECO:0000269|PubMed:7274457}.
MOD_RES 132 132 N-acetylserine; in Corticotropin.
{ECO:0000250|UniProtKB:P01191}.
MOD_RES 144 144 Valine amide.
{ECO:0000269|PubMed:13642798}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P01189}.
MOD_RES 173 173 Pyrrolidone carboxylic acid (Glu);
partial. {ECO:0000269|PubMed:2266117}.
MOD_RES 200 200 Sulfotyrosine.
{ECO:0000269|PubMed:2266117}.
CARBOHYD 71 71 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:4030947}.
/FTId=CAR_000202.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:4030947}.
/FTId=CAR_000034.
DISULFID 28 50 {ECO:0000269|PubMed:4030947}.
DISULFID 34 46 {ECO:0000269|PubMed:4030947}.
CONFLICT 10 10 G -> A (in Ref. 2; AAA30354).
{ECO:0000305}.
CONFLICT 139 139 R -> P (in Ref. 2; AAA30354).
{ECO:0000305}.
CONFLICT 161 161 Missing (in Ref. 6; AAA30718).
{ECO:0000305}.
CONFLICT 188 188 Q -> G (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 190 191 ES -> D (in Ref. 6; AAA30718).
{ECO:0000305}.
CONFLICT 196 196 A -> P (in Ref. 2; AAA30354).
{ECO:0000305}.
SEQUENCE 265 AA; 29260 MW; 303E9A0BCB073B3F CRC64;
MPRLCSSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLACIRAC KPDLSAETPV
FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NGSSSSGVGG AAQKREEEVA VGEGPGPRGD
DAETGPREDK RSYSMEHFRW GKPVGKKRRP VKVYPNGAED ESAQAFPLEF KRELTGERLE
QARGPEAQAE SAAARAELEY GLVAEAEAEA AEKKDSGPYK MEHFRWGSPP KDKRYGGFMT
SEKSQTPLVT LFKNAIIKNA HKKGQ


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