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