ID   COLI_RABIT              Reviewed;          39 AA.
AC   P06297;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
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=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   Flags: Fragment;
GN   Name=POMC;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-31, AND TISSUE SPECIFICITY.
RX   PubMed=3013598; DOI=10.1210/endo-119-1-70;
RA   Mulay S., Bennett H.P.J., Routhier R., Solomon S.;
RT   "Isolation, characterization, and corticotropic activity of rabbit
RT   adrenocorticotropin.";
RL   Endocrinology 119:70-76(1986).
CC   -!- FUNCTION: Precursor protein for pituitary hormones that regulate stress
CC       and environmental adaptation.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pituitary gland.
CC       {ECO:0000269|PubMed:3013598}.
CC   -!- MISCELLANEOUS: Residues 16-17 were deduced from the amino acid
CC       composition and by homology with other mammalian corticotropins.
CC   -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
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DR   PIR; A01457; A01457.
DR   AlphaFoldDB; P06297; -.
DR   iPTMnet; P06297; -.
DR   eggNOG; ENOG502RZNY; Eukaryota.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013531; Mcrtin_ACTH_cent.
DR   InterPro; IPR001941; PMOC.
DR   Pfam; PF00976; ACTH_domain; 1.
DR   PRINTS; PR00383; MELANOCORTIN.
DR   SMART; SM01363; ACTH_domain; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Hormone; Phosphoprotein; Reference proteome;
KW   Secreted.
FT   PEPTIDE         1..39
FT                   /note="Corticotropin"
FT                   /id="PRO_0000025026"
FT   PEPTIDE         1..13
FT                   /note="Melanocyte-stimulating hormone alpha"
FT                   /id="PRO_0000025027"
FT   PEPTIDE         19..39
FT                   /note="Corticotropin-like intermediary peptide"
FT                   /id="PRO_0000025028"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01191"
FT   MOD_RES         13
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P01190"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:3013598"
FT   NON_TER         1
FT   NON_TER         39
SQ   SEQUENCE   39 AA;  4478 MW;  5D1FC92E28945A6E CRC64;
     SYSMEHFRWG KPVGKKRRPV KVYPNGAENE SAEAFPVEV