ID   COLI_PIG                Reviewed;         267 AA.
AC   P01192; Q95246;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-1986, sequence version 1.
DT   04-NOV-2026, entry version 123.
DE   RecName: Full=Pro-opiomelanocortin;
DE            Short=POMC;
DE   AltName: Full=Corticotropin-lipotropin;
DE   Contains:
DE     RecName: Full=NPP;
DE   Contains:
DE     RecName: Full=Melanotropin gamma;
DE     AltName: Full=Gamma-MSH;
DE   Contains:
DE     RecName: Full=Corticotropin;
DE     AltName: Full=Adrenocorticotropic hormone;
DE              Short=ACTH;
DE   Contains:
DE     RecName: Full=Melanocyte-stimulating hormone alpha;
DE              Short=Alpha-MSH;
DE     AltName: Full=Melanotropin alpha;
DE   Contains:
DE     RecName: Full=Corticotropin-like intermediary peptide;
DE              Short=CLIP;
DE   Contains:
DE     RecName: Full=Lipotropin beta;
DE     AltName: Full=Beta-LPH;
DE   Contains:
DE     RecName: Full=Lipotropin gamma;
DE     AltName: Full=Gamma-LPH;
DE   Contains:
DE     RecName: Full=Melanocyte-stimulating hormone beta;
DE              Short=Beta-MSH;
DE     AltName: Full=Melanotropin beta;
DE   Contains:
DE     RecName: Full=Beta-endorphin;
DE   Contains:
DE     RecName: Full=Met-enkephalin;
DE   Flags: Precursor;
GN   Name=POMC;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3753882; DOI=10.1016/0167-4781(86)90102-8;
RA   Gossard F.J., Chang A.C.Y., Cohen S.N.;
RT   "Sequence of the cDNA encoding porcine pro-opiomelanocortin.";
RL   Biochim. Biophys. Acta 866:68-74(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6196724; DOI=10.1093/nar/11.22.8063;
RA   Boileau G., Barbeau C., Jeannotte L., Chretien M., Drouin J.;
RT   "Complete structure of the porcine pro-opiomelanocortin mRNA derived from
RT   the nucleotide sequence of cloned cDNA.";
RL   Nucleic Acids Res. 11:8063-8071(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7958386; DOI=10.1016/0303-7207(94)90075-2;
RA   Gen K., Hirai T., Kato T., Kato Y.;
RT   "Presence of the same transcript of pro-opiomelanocortin (POMC) genes in
RT   the porcine anterior and intermediate pituitary lobes.";
RL   Mol. Cell. Endocrinol. 103:101-108(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6547437; DOI=10.1016/s0021-9258(17)42807-9;
RA   Oates E., Herbert E.;
RT   "5' sequence of porcine and rat pro-opiomelanocortin mRNA. One porcine and
RT   two rat forms.";
RL   J. Biol. Chem. 259:7421-7425(1984).
RN   [5]
RP   PROTEIN SEQUENCE OF 136-174.
RA   Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,
RA   Davis S.B., Eigner E.A., Shakespeare N.E.;
RT   "Studies with corticotropin. III. Determination of the structure of beta-
RT   corticotropin and its active degradation products.";
RL   J. Am. Chem. Soc. 78:5067-5076(1956).
RN   [6]
RP   SEQUENCE REVISION TO 160 AND 165.
RX   PubMed=4334191; DOI=10.1038/newbio235114b0;
RA   Riniker B., Sieber P., Rittel W., Zuber H.;
RT   "Revised amino-acid sequences for porcine and human adrenocorticotrophic
RT   hormone.";
RL   Nature New Biol. 235:114-115(1972).
RN   [7]
RP   SEQUENCE REVISION (CORTICOTROPIN).
RX   PubMed=4369114;
RA   Graf L.;
RT   "Re-examination of the sequence of the C-terminal tryptic fragment from
RT   porcine adrenocorticotropic hormone.";
RL   Acta Biochim. Biophys. Acad. Sci. Hung. 7:293-297(1972).
RN   [8]
RP   PROTEIN SEQUENCE OF 136-174.
RX   PubMed=2174774; DOI=10.1111/j.1432-1033.1990.tb19447.x;
RA   Voigt K., Stegmaier W., McGregor G.P., Roesch H., Seliger H.;
RT   "Isolation and full structural characterisation of six adrenocorticotropin-
RT   like peptides from porcine pituitary gland. Identification of three novel
RT   fragments of adrenocorticotropin and of two forms of a novel
RT   adrenocorticotropin-like peptide.";
RL   Eur. J. Biochem. 194:225-236(1990).
RN   [9]
RP   PROTEIN SEQUENCE OF 136-148, AND AMIDATION AT VAL-148.
RX   PubMed=13451616; DOI=10.1038/1791346a0;
RA   Harris J.I., Lerner A.B.;
RT   "Amino-acid sequence of the alpha-melanocyte-stimulating hormone.";
RL   Nature 179:1346-1347(1957).
RN   [10]
RP   PROTEIN SEQUENCE OF 177-267.
RX   PubMed=5543613; DOI=10.1016/0005-2795(71)90344-8;
RA   Graf L., Barat E., Cseh G., Sajgo M.;
RT   "Amino acid sequence of porcine beta-lipotropic hormone.";
RL   Biochim. Biophys. Acta 229:276-278(1971).
RN   [11]
RP   SEQUENCE REVISION (LIPOTROPIN).
RA   Gilardeau C., Chretien M.;
RT   "Complete amino acid sequence of porcine beta-lipotropic hormone (beta-
RT   LPH).";
RL   (In) Meienhofer J. (eds.);
RL   Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub., Ann
RL   Arbor (1972).
RN   [12]
RP   SEQUENCE REVISION TO 211.
RX   PubMed=4673865;
RA   Pankov Y.A., Yudaev N.A.;
RT   "Complete amino acid sequence in the molecule of porcine beta-lipotropin.";
RL   Biokhimiia 37:991-1004(1972).
RN   [13]
RP   PROTEIN SEQUENCE OF 217-234.
RX   PubMed=13348631; DOI=10.1038/178090a0;
RA   Harris J.I., Roos P.;
RT   "Amino-acid sequence of a melanophore-stimulating peptide.";
RL   Nature 178:90-90(1956).
RN   [14]
RP   PROTEIN SEQUENCE OF 217-234.
RA   Geschwind I.I., Li C.H., Barnafi L.;
RT   "The structure of the beta-melanocyte-stimulating hormone.";
RL   J. Am. Chem. Soc. 79:620-625(1957).
RN   [15]
RP   PROTEIN SEQUENCE OF 237-241.
RX   PubMed=1207728; DOI=10.1038/258577a0;
RA   Hughes J., Smith T.W., Kosterlitz H.W., Fothergill L.A., Morgan B.A.,
RA   Morris H.R.;
RT   "Identification of two related pentapeptides from the brain with potent
RT   opiate agonist activity.";
RL   Nature 258:577-579(1975).
RN   [16]
RP   PROTEIN SEQUENCE OF 237-267.
RX   PubMed=1007884;
RA   Graf L., Barat E., Patthy A.;
RT   "Isolation of a COOH-terminal beta-lipotropin fragment (residues 61-91)
RT   with morphine-like analgesic activity from porcine pituitary glands.";
RL   Acta Biochim. Biophys. Acad. Sci. Hung. 11:121-122(1976).
CC   -!- FUNCTION: Precursor protein of pituitary hormones that are involved in
CC       diverse physiological processes, including the regulation of energy
CC       balance, stress response, immune function and skin pigmentation.
CC       {ECO:0000250|UniProtKB:P01189}.
CC   -!- FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release
CC       cortisol.
CC   -!- FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide.
CC       Increases the pigmentation of skin by increasing melanin production in
CC       melanocytes.
CC   -!- FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the
CC       pigmentation of skin by increasing melanin production in melanocytes.
CC   -!- FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.
CC   -!- FUNCTION: [Met-enkephalin]: Endogenous opiate.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}.
CC       Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored
CC       in separate granules in hypothalamic POMC neurons, suggesting that
CC       secretion may be under the control of different regulatory mechanisms.
CC       {ECO:0000250|UniProtKB:P01193}.
CC   -!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland.
CC   -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC       different active peptides.
CC   -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
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DR   EMBL; X03561; CAA27248.1; -; mRNA.
DR   EMBL; X00135; CAA24968.1; -; mRNA.
DR   EMBL; S73519; AAB32312.1; -; mRNA.
DR   PIR; A93496; CTPGP.
DR   RefSeq; NP_999023.1; NM_213858.1.
DR   AlphaFoldDB; P01192; -.
DR   BMRB; P01192; -.
DR   SMR; P01192; -.
DR   FunCoup; P01192; 842.
DR   STRING; 9823.ENSSSCP00000024582; -.
DR   GlyCosmos; P01192; 1 site, No reported glycans.
DR   GlyGen; P01192; 1 site.
DR   MetOSite; P01192; -.
DR   PaxDb; 9823-ENSSSCP00000024582; -.
DR   GeneID; 396863; -.
DR   KEGG; ssc:396863; -.
DR   CTD; 5443; -.
DR   eggNOG; ENOG502RZNY; Eukaryota.
DR   InParanoid; P01192; -.
DR   OMA; AAGPYKM; -.
DR   OrthoDB; 8962839at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0033059; P:cellular pigmentation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR013531; Mcrtin_ACTH_cent.
DR   InterPro; IPR013593; Melanocortin_N.
DR   InterPro; IPR013532; Opioid_neuropept.
DR   InterPro; IPR001941; PMOC.
DR   InterPro; IPR050878; POMC-derived_peptides.
DR   PANTHER; PTHR11416; PRO-OPIOMELANOCORTIN; 1.
DR   PANTHER; PTHR11416:SF7; PRO-OPIOMELANOCORTIN; 1.
DR   Pfam; PF00976; ACTH_domain; 3.
DR   Pfam; PF08384; NPP; 1.
DR   Pfam; PF08035; Op_neuropeptide; 1.
DR   PRINTS; PR00383; MELANOCORTIN.
DR   SMART; SM01363; ACTH_domain; 2.
DR   SMART; SM01364; NPP; 1.
DR   SMART; SM01365; Op_neuropeptide; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Endorphin; Glycoprotein; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         27..106
FT                   /note="NPP"
FT                   /id="PRO_0000025015"
FT   PEPTIDE         77..87
FT                   /note="Melanotropin gamma"
FT                   /id="PRO_0000025016"
FT   PROPEP          109..133
FT                   /id="PRO_0000025017"
FT   PEPTIDE         136..174
FT                   /note="Corticotropin"
FT                   /id="PRO_0000025018"
FT   PEPTIDE         136..148
FT                   /note="Melanocyte-stimulating hormone alpha"
FT                   /id="PRO_0000025019"
FT   PEPTIDE         154..174
FT                   /note="Corticotropin-like intermediary peptide"
FT                   /id="PRO_0000025020"
FT   PEPTIDE         177..267
FT                   /note="Lipotropin beta"
FT                   /id="PRO_0000025021"
FT   PEPTIDE         177..234
FT                   /note="Lipotropin gamma"
FT                   /id="PRO_0000025022"
FT   PEPTIDE         217..234
FT                   /note="Melanocyte-stimulating hormone beta"
FT                   /id="PRO_0000025023"
FT   PEPTIDE         237..267
FT                   /note="Beta-endorphin"
FT                   /id="PRO_0000025024"
FT   PEPTIDE         237..241
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000025025"
FT   REGION          88..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..105
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P01190"
FT   MOD_RES         136
FT                   /note="N-acetylserine; in Corticotropin"
FT                   /evidence="ECO:0000250|UniProtKB:P01191"
FT   MOD_RES         148
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:13451616"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         143
FT                   /note="R -> T"
FT   CONFLICT        6
FT                   /note="G -> S (in Ref. 3 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="T -> A (in Ref. 3 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="G -> E (in Ref. 3 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="A -> S (in Ref. 4)"
FT                   /evidence="ECO:0000305"
SQ   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
//