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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_SHEEP              Reviewed;         263 AA.
P01191; Q28826; Q8MIC5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
11-DEC-2013, sequence version 3.
25-OCT-2017, entry version 96.
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;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=Ile de France; TISSUE=Hypothalamus;
PubMed=14636633; DOI=10.1016/S0016-6480(03)00266-1;
Pillon D., Caraty A., Fabre-Nys C., Bruneau G.;
"Early decrease of proopiomelanocortin but not neuropeptide Y mRNA
expression in the mediobasal hypothalamus of the ewe, during the
estradiol-induced preovulatory LH surge.";
Gen. Comp. Endocrinol. 134:264-272(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 52-136.
PubMed=8384993; DOI=10.1210/endo.132.4.8384993;
Levin N., Wallace C., Bengani N., Blum M., Farnworth P., Smith A.I.,
Roberts J.L.;
"Ovine anterior pituitary proopiomelanocortin gene expression is not
increased by ACTH secretagogues in vitro.";
Endocrinology 132:1692-1700(1993).
[3]
PROTEIN SEQUENCE OF 132-170.
Leonis J., Li C.H., Chung D.;
"Corticotropins (ACTH). XV. The action of chymotrypsin on alpha-
corticotropin.";
J. Am. Chem. Soc. 81:419-423(1959).
[4]
PROTEIN SEQUENCE OF 132-170, AND SEQUENCE REVISION.
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).
[5]
PROTEIN SEQUENCE OF 132-170, AND SEQUENCE REVISION.
PubMed=4370084; DOI=10.1016/0014-5793(74)80838-0;
Joehl A., Riniker B., Schenkel-Hulliger L.;
"Identity of structure of ovine and bovine ACTH: correction of revised
structure of the ovine hormone.";
FEBS Lett. 45:172-174(1974).
[6]
PROTEIN SEQUENCE OF 132-144 AND 213-230, ACETYLATION AT SER-132, AND
AMIDATION AT VAL-144.
PubMed=13929167; DOI=10.1016/0006-3002(63)91144-2;
Lee T.H., Lerner A.B., Buettner-Janusch V.;
"Melanocyte-stimulating hormones from sheep pituitary glands.";
Biochim. Biophys. Acta 71:706-709(1963).
[7]
PROTEIN SEQUENCE OF 173-263.
PubMed=4162144; DOI=10.1038/2081093b0;
Li C.H., Barnafi L., Chretien M., Chung D.;
"Isolation and amino-acid sequence of beta-LPH from sheep pituitary
glands.";
Nature 208:1093-1094(1965).
[8]
PROTEIN SEQUENCE OF 173-263, AND SEQUENCE REVISION.
PubMed=4675453;
Chretien M., Gilardeau C., Li C.H.;
"Revised structure of sheep beta-lipotropic hormone.";
Int. J. Pept. Protein Res. 4:263-265(1972).
[9]
PROTEIN SEQUENCE OF 173-263, AND SEQUENCE REVISION.
PubMed=4270658; DOI=10.1016/0006-291X(73)90607-4;
Graf L., Li C.H.;
"Action of plasmin on ovine beta-lipotropin: revision of the carboxyl
terminal sequence.";
Biochem. Biophys. Res. Commun. 53:1304-1309(1973).
[10]
PROTEIN SEQUENCE OF 233-263.
PubMed=843377; DOI=10.1016/0006-291X(77)90616-7;
Seidah N.G., Dragon N., Benjannet S., Routhier R., Chretien M.;
"The complete sequence of sheep beta-endorphin.";
Biochem. Biophys. Res. Commun. 74:1528-1535(1977).
-!- 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: Melanocyte-stimulating hormone beta: 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.
-!- INDUCTION: Repressed by treatment with estradiol.
{ECO:0000269|PubMed:14636633}.
-!- PTM: Specific enzymatic cleavages at paired basic residues yield
the different active peptides.
-!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ507201; CAD45184.1; -; mRNA.
EMBL; S57982; AAB26022.1; -; mRNA.
PIR; A49188; CTSHP.
RefSeq; NP_001009266.1; NM_001009266.1.
UniGene; Oar.508; -.
iPTMnet; P01191; -.
GeneID; 443212; -.
KEGG; oas:443212; -.
CTD; 5443; -.
HOVERGEN; HBG004341; -.
KO; K05228; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
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:0000255}.
PEPTIDE 27 103 NPP.
/FTId=PRO_0000025039.
PEPTIDE 77 87 Melanotropin gamma.
/FTId=PRO_0000025040.
PROPEP 106 129
/FTId=PRO_0000424695.
PEPTIDE 132 170 Corticotropin.
/FTId=PRO_0000025041.
PEPTIDE 132 144 Melanocyte-stimulating hormone alpha.
/FTId=PRO_0000025042.
PEPTIDE 150 170 Corticotropin-like intermediary peptide.
/FTId=PRO_0000025043.
PEPTIDE 173 263 Lipotropin beta.
/FTId=PRO_0000025044.
PEPTIDE 173 230 Lipotropin gamma.
/FTId=PRO_0000025045.
PEPTIDE 213 230 Melanocyte-stimulating hormone beta.
/FTId=PRO_0000025046.
PEPTIDE 233 263 Beta-endorphin.
/FTId=PRO_0000025047.
PEPTIDE 233 237 Met-enkephalin.
/FTId=PRO_0000025048.
MOD_RES 87 87 Phenylalanine amide.
{ECO:0000250|UniProtKB:P01190}.
MOD_RES 132 132 N-acetylserine; in Corticotropin.
{ECO:0000269|PubMed:13929167}.
MOD_RES 144 144 Valine amide.
{ECO:0000269|PubMed:13929167}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P01189}.
MOD_RES 173 173 Pyrrolidone carboxylic acid (Glu);
partial. {ECO:0000250}.
MOD_RES 200 200 Sulfotyrosine. {ECO:0000250}.
CARBOHYD 71 71 O-linked (GalNAc...) threonine.
{ECO:0000250}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 50 {ECO:0000250}.
DISULFID 34 46 {ECO:0000250}.
CONFLICT 65 65 G -> C (in Ref. 2; AAB26022).
{ECO:0000305}.
SEQUENCE 263 AA; 29062 MW; ECB3A6E9AFB9DE81 CRC64;
MPRLCSSRSG ALLLVLLLQA SMEVRGWCLE SSQCQDLTTE SNLLACIRAC KPDLSAETPV
FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NGSSSFGAGG AAQKREEEVA VGEGPGPRGD
GAETGPREDK RSYSMEHFRW GKPVGKKRRP VKVYPNGAED ESAQAFPLEF KRELTGERLE
QARGPEAQAE SAAARAELEY GLVAEAEAAE KKDSGPYKME HFRWGSPPKD KRYGGFMTSE
KSQTPLVTLF KNAIIKNAHK KGQ


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