ID   COLI_CAVPO              Reviewed;         256 AA.
AC   P19402;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 104.
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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=1662166; DOI=10.1016/0303-7207(91)90012-h;
RA   Keightley M.C., Funder J.W., Fuller P.J.;
RT   "Molecular cloning and sequencing of a guinea-pig pro-opiomelanocortin
RT   cDNA.";
RL   Mol. Cell. Endocrinol. 82:89-98(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 125-163.
RX   PubMed=2830360; DOI=10.1677/joe.0.115r005;
RA   Smith A.I., Wallace C.A., Moritz R.L., Simpson R.J., Schmauk-White L.B.,
RA   Woodcock E.A., Funder J.W.;
RT   "Isolation, amino acid sequence and action of guinea-pig ACTH on
RT   aldosterone production by glomerulosa cells.";
RL   J. Endocrinol. 115:R5-R8(1987).
CC   -!- FUNCTION: ACTH stimulates the adrenal glands to release cortisol.
CC   -!- FUNCTION: MSH (melanocyte-stimulating hormone) increases the
CC       pigmentation of skin by increasing melanin production in melanocytes.
CC   -!- FUNCTION: Beta-endorphin and Met-enkephalin are endogenous opiates.
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; S78260; AAB20814.2; -; mRNA.
DR   PIR; A54322; A54322.
DR   AlphaFoldDB; P19402; -.
DR   SMR; P19402; -.
DR   STRING; 10141.ENSCPOP00000020054; -.
DR   eggNOG; ENOG502RZNY; Eukaryota.
DR   InParanoid; P19402; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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; 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; Disulfide bond; Endorphin; Glycoprotein;
KW   Hormone; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         27..97
FT                   /note="NPP"
FT                   /id="PRO_0000024955"
FT   PEPTIDE         77..87
FT                   /note="Melanotropin gamma"
FT                   /id="PRO_0000024956"
FT   PROPEP          100..122
FT                   /id="PRO_0000024957"
FT   PEPTIDE         125..163
FT                   /note="Corticotropin"
FT                   /id="PRO_0000024958"
FT   PEPTIDE         125..137
FT                   /note="Melanocyte-stimulating hormone alpha"
FT                   /id="PRO_0000024959"
FT   PEPTIDE         143..163
FT                   /note="Corticotropin-like intermediary peptide"
FT                   /id="PRO_0000024960"
FT   PEPTIDE         166..256
FT                   /note="Lipotropin beta"
FT                   /id="PRO_0000024961"
FT   PEPTIDE         166..223
FT                   /note="Lipotropin gamma"
FT                   /id="PRO_0000024962"
FT   PEPTIDE         206..223
FT                   /note="Melanocyte-stimulating hormone beta"
FT                   /id="PRO_0000024963"
FT   PEPTIDE         226..256
FT                   /note="Beta-endorphin"
FT                   /id="PRO_0000024964"
FT   PEPTIDE         226..230
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000024965"
FT   REGION          88..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P01190"
FT   MOD_RES         125
FT                   /note="N-acetylserine; in Corticotropin"
FT                   /evidence="ECO:0000250|UniProtKB:P01191"
FT   MOD_RES         137
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P01190"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01189"
FT   CARBOHYD        71
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..50
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   256 AA;  28264 MW;  02619BE7C0A0DA54 CRC64;
     MPRSCYSRSG TLLLALLLQI SMEVRGWCLE SSQCQDLTTE RHLLECLRAC KPDLSAETPV
     FPGGADEQTP TESPRKYVTG HFRWGRFGRG NSSGASQKRE EEAAAADPGF HGDGVEPGLR
     EDKRSYSMEH FRWGKPVGKK RRPVKVYANG AEEESAEAFP LEFKRELTGE RPAAAPGPDG
     LGFGLVAEAE AEAAAAEKKD AAEKKDDGSY RMEHFRWGTP RKGKRYGGFM TSEKSQTPLV
     TLFKNAIVKN AHKKGQ