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COLI_THUOB
ID   COLI_THUOB              Reviewed;         222 AA.
AC   Q9YGK2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 58.
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   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   Thunnus obesus (Bigeye tuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX   NCBI_TaxID=8241;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Amemiya Y., Takahashi A., Kawauchi H.;
RT   "Tuna proopiomelanocortin cDNA.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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; AB020971; BAA35125.1; -; mRNA.
DR   AlphaFoldDB; Q9YGK2; -.
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   Cleavage on pair of basic residues; Endorphin; Hormone; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..90
FT                   /id="PRO_0000025113"
FT   PEPTIDE         93..132
FT                   /note="Corticotropin"
FT                   /id="PRO_0000025114"
FT   PEPTIDE         93..107
FT                   /note="Melanocyte-stimulating hormone alpha"
FT                   /id="PRO_0000025115"
FT   PEPTIDE         111..132
FT                   /note="Corticotropin-like intermediary peptide"
FT                   /id="PRO_0000025116"
FT   PEPTIDE         136..222
FT                   /note="Lipotropin beta"
FT                   /id="PRO_0000025117"
FT   PEPTIDE         136..188
FT                   /note="Lipotropin gamma"
FT                   /id="PRO_0000025118"
FT   PEPTIDE         172..188
FT                   /note="Melanocyte-stimulating hormone beta"
FT                   /id="PRO_0000025119"
FT   PEPTIDE         191..222
FT                   /note="Beta-endorphin"
FT                   /id="PRO_0000025120"
FT   PEPTIDE         191..195
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000025121"
FT   REGION          56..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   222 AA;  24970 MW;  7868C713D6360B70 CRC64;
     MCPVWLLVAV VVVGGSRGAV SQCWEHPSCQ ELNSDSSMME CIQLCHSDLT AEKPVIPGNA
     HLQPPPLPDP SSSSSFILPS SSSSSSSPQS KRSYSMEHFR WGKPVGRKRR PVKVYTSNGV
     EEESAEVFPG EMRRRELASE LLAAAEEEEE KAQEVMAEEE EEQKQLLQEK KDGSYKMKHF
     RWSGPPASKR YGGFMKSWDE RSQRPLLTLF KNVINKDGQQ QK
 
 
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