ID   COLI_MACNE              Reviewed;         264 AA.
AC   P01201; P19403;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   25-MAY-2022, entry version 87.
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=Potential peptide;
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   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-87; GLU-131 AND VAL-147.
RX   PubMed=3229286; DOI=10.1089/dna.1988.7.627;
RA   Patel P.D., Sherman T.G., Watson S.J.;
RT   "Characterization of pro-opiomelanocortin cDNA from the Old World monkey,
RT   Macaca nemestrina.";
RL   DNA 7:627-635(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 135-147 AND 214-231, AND AMIDATION AT VAL-147.
RX   PubMed=13760276;
RA   Lee T.H., Lerner A.B., Buettner-Janusch V.;
RT   "The isolation and structure of alpha- and beta-melanocyte-stimulating
RT   hormones from monkey pituitary glands.";
RL   J. Biol. Chem. 236:1390-1394(1961).
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; M19658; AAA66022.1; -; mRNA.
DR   PIR; A31855; CTMKP.
DR   AlphaFoldDB; P01201; -.
DR   BMRB; P01201; -.
DR   SMR; P01201; -.
DR   STRING; 9545.ENSMNEP00000005588; -.
DR   Proteomes; UP000233120; Whole Genome Shotgun Assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013531; Mcrtin_ACTH_cent.
DR   InterPro; IPR013593; Melanocortin_N.
DR   InterPro; IPR013532; Opioid_neuropept.
DR   InterPro; IPR001941; PMOC.
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; 3.
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   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         27..99
FT                   /note="NPP"
FT                   /id="PRO_0000024985"
FT   PEPTIDE         77..87
FT                   /note="Melanotropin gamma"
FT                   /id="PRO_0000024986"
FT   PEPTIDE         91..131
FT                   /note="Potential peptide"
FT                   /id="PRO_0000024987"
FT   PEPTIDE         135..173
FT                   /note="Corticotropin"
FT                   /id="PRO_0000024988"
FT   PEPTIDE         135..147
FT                   /note="Melanocyte-stimulating hormone alpha"
FT                   /id="PRO_0000024989"
FT   PEPTIDE         153..173
FT                   /note="Corticotropin-like intermediary peptide"
FT                   /id="PRO_0000024990"
FT   PEPTIDE         176..264
FT                   /note="Lipotropin beta"
FT                   /id="PRO_0000024991"
FT   PEPTIDE         176..231
FT                   /note="Lipotropin gamma"
FT                   /id="PRO_0000024992"
FT   PEPTIDE         214..231
FT                   /note="Melanocyte-stimulating hormone beta"
FT                   /id="PRO_0000024993"
FT   PEPTIDE         234..264
FT                   /note="Beta-endorphin"
FT                   /id="PRO_0000024994"
FT   PEPTIDE         234..238
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000024995"
FT   REGION          88..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:3229286"
FT   MOD_RES         131
FT                   /note="Glutamic acid 1-amide"
FT                   /evidence="ECO:0000269|PubMed:3229286"
FT   MOD_RES         135
FT                   /note="N-acetylserine; in Corticotropin"
FT                   /evidence="ECO:0000250|UniProtKB:P01191"
FT   MOD_RES         147
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:13760276,
FT                   ECO:0000269|PubMed:3229286"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01189"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   264 AA;  29172 MW;  BC73B100D9BAD052 CRC64;
     MPRSCCSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLECIRAC KPDLSAETPV
     FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NSSSGSAHQK REDVAAGEDR GLLPEGGPEP
     RGDGAGPGPR EGKRSYSMEH FRWGKPVGKK RRPVKVYPNG AEDESAEAFP LEFKRELTGQ
     RPRAGDGPDG PADDGAGPRA DLEHSLLVAA EKKDEGPYRM EHFRWGSPPK DKRYGGFMTS
     EKSQTPLVTL FKNAIIKNAY KKGQ