ID   COLI_LEPOS              Reviewed;         259 AA.
AC   Q91082;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Pro-opiomelanocortin;
DE            Short=POMC;
DE   AltName: Full=Corticotropin-lipotropin;
DE   Contains:
DE     RecName: Full=NPP;
DE   Contains:
DE     RecName: Full=Gamma-melanotropin-like segment;
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=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   Lepisosteus osseus (Long-nosed gar) (Esox osseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=34771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=9268621; DOI=10.1006/gcen.1997.6947;
RA   Dores R.M., Smith T.R., Rubin D.A., Danielson P., Marra L.E., Youson J.H.;
RT   "Deciphering posttranslational processing events in the pituitary of a
RT   neopterygian fish: cloning of a gar proopiomelanocortin cDNA.";
RL   Gen. Comp. Endocrinol. 107:401-413(1997).
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   -!- 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; U59910; AAB03227.1; -; mRNA.
DR   AlphaFoldDB; Q91082; -.
DR   SMR; Q91082; -.
DR   PRIDE; Q91082; -.
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; 2.
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   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond; Endorphin;
KW   Hormone; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..132
FT                   /note="NPP"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025075"
FT   PEPTIDE         72..94
FT                   /note="Gamma-melanotropin-like segment"
FT                   /id="PRO_0000025076"
FT   PEPTIDE         135..173
FT                   /note="Corticotropin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025077"
FT   PEPTIDE         135..147
FT                   /note="Melanocyte-stimulating hormone alpha"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025078"
FT   PEPTIDE         153..204
FT                   /note="Corticotropin-like intermediary peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025079"
FT   PEPTIDE         207..223
FT                   /note="Melanocyte-stimulating hormone beta"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025080"
FT   PEPTIDE         226..259
FT                   /note="Beta-endorphin"
FT                   /id="PRO_0000025081"
FT   PEPTIDE         226..230
FT                   /note="Met-enkephalin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025082"
FT   REGION          113..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         147
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        24..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..42
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   259 AA;  29675 MW;  6C0533AB20020EED CRC64;
     MLRSVWVYSL GLAVLLQQSG REQCWEHSQC RDLSSEENIL ECIQACNSDL TAESPIFPGN
     GHLQPPSEAD RNYAKSHFRS TALGRRTNGS VGSSKQAGEN AALSILFAAL APPQAEEEME
     ESESSQQQRR EDKRSYSMEH FRWGKPVGRK RRPVKVYPNG VEEESAEAYP TEMRRDLMSD
     LDYPLLEEVE EELGGENEVL NLQEKKDGSY KMHHFRWSRP PKDKRYGGFM KSWDERSQKP
     LLTLFKNVII KDGHQKKGQ