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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_PIG                Reviewed;         267 AA.
P01192; Q95246;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-OCT-1986, sequence version 1.
25-OCT-2017, entry version 98.
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;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3753882; DOI=10.1016/0167-4781(86)90102-8;
Gossard F.J., Chang A.C.Y., Cohen S.N.;
"Sequence of the cDNA encoding porcine pro-opiomelanocortin.";
Biochim. Biophys. Acta 866:68-74(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6196724; DOI=10.1093/nar/11.22.8063;
Boileau G., Barbeau C., Jeannotte L., Chretien M., Drouin J.;
"Complete structure of the porcine pro-opiomelanocortin mRNA derived
from the nucleotide sequence of cloned cDNA.";
Nucleic Acids Res. 11:8063-8071(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7958386; DOI=10.1016/0303-7207(94)90075-2;
Gen K., Hirai T., Kato T., Kato Y.;
"Presence of the same transcript of pro-opiomelanocortin (POMC) genes
in the porcine anterior and intermediate pituitary lobes.";
Mol. Cell. Endocrinol. 103:101-108(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6547437;
Oates E., Herbert E.;
"5' sequence of porcine and rat pro-opiomelanocortin mRNA. One porcine
and two rat forms.";
J. Biol. Chem. 259:7421-7425(1984).
[5]
PROTEIN SEQUENCE OF 136-174.
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 of
beta-corticotropin and its active degradation products.";
J. Am. Chem. Soc. 78:5067-5076(1956).
[6]
SEQUENCE REVISION TO 160 AND 165.
PubMed=4334191;
Riniker B., Sieber P., Rittel W., Zuber H.;
"Revised amino-acid sequences for porcine and human
adrenocorticotrophic hormone.";
Nature New Biol. 235:114-115(1972).
[7]
SEQUENCE REVISION (CORTICOTROPIN).
PubMed=4369114;
Graf L.;
"Re-examination of the sequence of the C-terminal tryptic fragment
from porcine adrenocorticotropic hormone.";
Acta Biochim. Biophys. Acad. Sci. Hung. 7:293-297(1972).
[8]
PROTEIN SEQUENCE OF 136-174.
PubMed=2174774; DOI=10.1111/j.1432-1033.1990.tb19447.x;
Voigt K., Stegmaier W., McGregor G.P., Roesch H., Seliger H.;
"Isolation and full structural characterisation of six
adrenocorticotropin-like peptides from porcine pituitary gland.
Identification of three novel fragments of adrenocorticotropin and of
two forms of a novel adrenocorticotropin-like peptide.";
Eur. J. Biochem. 194:225-236(1990).
[9]
PROTEIN SEQUENCE OF 136-148, AND AMIDATION AT VAL-148.
PubMed=13451616; DOI=10.1038/1791346a0;
Harris J.I., Lerner A.B.;
"Amino-acid sequence of the alpha-melanocyte-stimulating hormone.";
Nature 179:1346-1347(1957).
[10]
PROTEIN SEQUENCE OF 177-267.
PubMed=5543613;
Graf L., Barat E., Cseh G., Sajgo M.;
"Amino acid sequence of porcine beta-lipotropic hormone.";
Biochim. Biophys. Acta 229:276-278(1971).
[11]
SEQUENCE REVISION (LIPOTROPIN).
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]
SEQUENCE REVISION TO 211.
PubMed=4673865;
Pankov Y.A., Yudaev N.A.;
"Complete amino acid sequence in the molecule of porcine beta-
lipotropin.";
Biokhimiia 37:991-1004(1972).
[13]
PROTEIN SEQUENCE OF 217-234.
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 217-234.
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]
PROTEIN SEQUENCE OF 237-241.
PubMed=1207728; DOI=10.1038/258577a0;
Hughes J., Smith T.W., Kosterlitz H.W., Fothergill L.A., Morgan B.A.,
Morris H.R.;
"Identification of two related pentapeptides from the brain with
potent opiate agonist activity.";
Nature 258:577-579(1975).
[16]
PROTEIN SEQUENCE OF 237-267.
PubMed=1007884;
Graf L., Barat E., Patthy A.;
"Isolation of a COOH-terminal beta-lipotropin fragment (residues 61-
91) with morphine-like analgesic activity from porcine pituitary
glands.";
Acta Biochim. Biophys. Acad. Sci. Hung. 11:121-122(1976).
-!- 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.
-!- 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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X03561; CAA27248.1; -; mRNA.
EMBL; X00135; CAA24968.1; -; mRNA.
EMBL; S73519; AAB32312.1; -; mRNA.
PIR; A93496; CTPGP.
RefSeq; NP_999023.1; NM_213858.1.
UniGene; Ssc.14556; -.
STRING; 9823.ENSSSCP00000024582; -.
PaxDb; P01192; -.
PRIDE; P01192; -.
GeneID; 396863; -.
KEGG; ssc:396863; -.
CTD; 5443; -.
eggNOG; ENOG410IKR5; Eukaryota.
eggNOG; ENOG410Z5R4; LUCA.
HOVERGEN; HBG004341; -.
InParanoid; P01192; -.
KO; K05228; -.
Proteomes; UP000008227; Unplaced.
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:0005179; F:hormone activity; IMP:AgBase.
GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
GO; GO:0043400; P:cortisol secretion; IMP:AgBase.
GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
GO; GO:2000852; P:regulation of corticosterone secretion; IBA:GO_Central.
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; 2.
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; Endorphin; Glycoprotein;
Hormone; Reference proteome; Secreted; Signal.
SIGNAL 1 26 {ECO:0000250}.
PEPTIDE 27 106 NPP.
/FTId=PRO_0000025015.
PEPTIDE 77 87 Melanotropin gamma.
/FTId=PRO_0000025016.
PROPEP 109 133
/FTId=PRO_0000025017.
PEPTIDE 136 174 Corticotropin.
/FTId=PRO_0000025018.
PEPTIDE 136 148 Melanocyte-stimulating hormone alpha.
/FTId=PRO_0000025019.
PEPTIDE 154 174 Corticotropin-like intermediary peptide.
/FTId=PRO_0000025020.
PEPTIDE 177 267 Lipotropin beta.
/FTId=PRO_0000025021.
PEPTIDE 177 234 Lipotropin gamma.
/FTId=PRO_0000025022.
PEPTIDE 217 234 Melanocyte-stimulating hormone beta.
/FTId=PRO_0000025023.
PEPTIDE 237 267 Beta-endorphin.
/FTId=PRO_0000025024.
PEPTIDE 237 241 Met-enkephalin.
/FTId=PRO_0000025025.
MOD_RES 87 87 Phenylalanine amide.
{ECO:0000250|UniProtKB:P01190}.
MOD_RES 136 136 N-acetylserine; in Corticotropin.
{ECO:0000250|UniProtKB:P01191}.
MOD_RES 148 148 Valine amide.
{ECO:0000269|PubMed:13451616}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 143 143 R -> T.
CONFLICT 6 6 G -> S (in Ref. 3 and 4). {ECO:0000305}.
CONFLICT 15 15 T -> A (in Ref. 3 and 4). {ECO:0000305}.
CONFLICT 23 23 G -> E (in Ref. 3 and 4). {ECO:0000305}.
CONFLICT 49 49 A -> S (in Ref. 4). {ECO:0000305}.
SEQUENCE 267 AA; 28895 MW; A6DB487A5032B648 CRC64;
MPRLCGSRSG ALLLTLLLQA SMGVRGWCLE SSQCQDLSTE SNLLACIRAC KPDLSAETPV
FPGNGDAQPL TENPRKYVMG HFRWDRFGRR NGSSSGGGGG GGGAGQKREE EEVAAGEGPG
PRGDGVAPGP RQDKRSYSME HFRWGKPVGK KRRPVKVYPN GAEDELAEAF PLEFRRELAG
APPEPARDPE APAEGAAARA ELEYGLVAEA EAAEKKDEGP YKMEHFRWGS PPKDKRYGGF
MTSEKSQTPL VTLFKNAIVK NAHKKGQ


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