COLI2_ONCMY
ID COLI2_ONCMY Reviewed; 240 AA.
AC Q04618;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Pro-opiomelanocortin B;
DE Short=POMC-B;
DE AltName: Full=Corticotropin-lipotropin B;
DE Contains:
DE RecName: Full=NPP 2;
DE Contains:
DE RecName: Full=Corticotropin;
DE AltName: Full=Adrenocorticotropic hormone;
DE Short=ACTH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone alpha 2;
DE Short=Alpha-MSH 2;
DE AltName: Full=Melanotropin alpha 2;
DE Contains:
DE RecName: Full=Corticotropin-like intermediary peptide 2;
DE Short=CLIP-2;
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 2;
DE Short=Beta-MSH 2;
DE AltName: Full=Melanotropin beta 2;
DE Contains:
DE RecName: Full=Beta-endorphin 2;
DE Contains:
DE RecName: Full=Met-enkephalin;
DE Flags: Precursor;
GN Name=pomcb;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=1448114; DOI=10.1210/mend.6.10.1448114;
RA Salbert G., Chauveau I., Bonnec G., Valotaire Y., Jego P.;
RT "One of the two trout proopiomelanocortin messenger RNAs potentially
RT encodes new peptides.";
RL Mol. Endocrinol. 6:1605-1613(1992).
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: Pituitary and hypothalamus of adult diploid
CC animals.
CC -!- DEVELOPMENTAL STAGE: Expressed only in sexually active fish.
CC -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC different active peptides.
CC -!- PTM: Acetylation of beta-endorphin occurs in a tissue-specific manner.
CC -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X69809; CAA49467.1; -; mRNA.
DR PIR; B45359; B45359.
DR RefSeq; NP_001118191.1; NM_001124719.1.
DR AlphaFoldDB; Q04618; -.
DR GeneID; 100136772; -.
DR KEGG; omy:100136772; -.
DR OrthoDB; 1168862at2759; -.
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 Acetylation; Amidation; Cleavage on pair of basic residues; Endorphin;
KW Hormone; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT PEPTIDE 37..108
FT /note="NPP 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025103"
FT PROPEP 111
FT /evidence="ECO:0000255"
FT /id="PRO_0000025104"
FT PEPTIDE 112..152
FT /note="Corticotropin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025105"
FT PEPTIDE 112..124
FT /note="Melanocyte-stimulating hormone alpha 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025106"
FT PEPTIDE 130..152
FT /note="Corticotropin-like intermediary peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025107"
FT PEPTIDE 155..240
FT /note="Lipotropin beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025108"
FT PEPTIDE 155..209
FT /note="Lipotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025109"
FT PEPTIDE 193..209
FT /note="Melanocyte-stimulating hormone beta 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025110"
FT PEPTIDE 212..240
FT /note="Beta-endorphin 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025111"
FT PEPTIDE 212..216
FT /note="Met-enkephalin"
FT /id="PRO_0000025112"
FT MOD_RES 37
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 112
FT /note="N-acetylserine; in Corticotropin"
FT /evidence="ECO:0000250"
FT MOD_RES 124
FT /note="Isoleucine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 240 AA; 26719 MW; 4F715CE8E6424F6C CRC64;
MFGTFLQNQS VRLNMVCAPW LLAVVVVCVC NPGVEGQCWD SSHCKDLPSE DKILECIHLF
RSGLQDESPE PRSAAQQSTE ESLSLGILLA ALTSGERALD ADPEPHSDKR HSYSMEHFRW
GKPIGHKRRP IKVYASSLEG GDSSEGTFPL QARRQLSSWE DEMVGALGNQ GAKAQTKVVP
RTLTVTGLQD KKDGSYRMGH FRWGSPTAIK RYGGFMKPYT QQSHKPLITL LKHVTLKNEQ
