COLI1_ONCMY
ID COLI1_ONCMY Reviewed; 253 AA.
AC Q04617;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Pro-opiomelanocortin A;
DE Short=POMC-A;
DE AltName: Full=Corticotropin-lipotropin A;
DE Contains:
DE RecName: Full=NPP 1;
DE Contains:
DE RecName: Full=Corticotropin;
DE AltName: Full=Adrenocorticotropic hormone;
DE Short=ACTH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone alpha 1;
DE Short=Alpha-MSH 1;
DE AltName: Full=Melanotropin alpha 1;
DE Contains:
DE RecName: Full=Corticotropin-like intermediary peptide 1;
DE Short=CLIP-1;
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 1;
DE Short=Beta-MSH 1;
DE AltName: Full=Melanotropin beta 1;
DE Contains:
DE RecName: Full=Beta-endorphin 1;
DE Contains:
DE RecName: Full=Met-enkephalin;
DE Contains:
DE RecName: Full=C-terminal peptide 1;
DE Contains:
DE RecName: Full=C-terminal peptide 2;
DE Flags: Precursor;
GN Name=pomca;
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).
RN [2]
RP PROTEIN SEQUENCE OF 231-240 AND 243-252, AMIDATION AT GLN-252, AND MASS
RP SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=9299569; DOI=10.1006/bbrc.1997.7356;
RA Tollemer H., Leprince J., Galas L., Vandesande F., Mevel J.C., Tonon M.C.,
RA Conlon J.M., Vaudry H.;
RT "Isolation and structural characterization of two novel peptides derived
RT from proopiomelanocortin in the pituitary of the rainbow trout.";
RL Biochem. Biophys. Res. Commun. 238:653-657(1997).
RN [3]
RP IDENTIFICATION OF C-TERMINAL PEPTIDES, AND AMIDATION AT GLN-252.
RX PubMed=8977395; DOI=10.1210/endo.138.1.4856;
RA Tollemer H., Leprince J., Bailhache T., Chauveau I., Vandesande F.,
RA Tonon M.C., Jego P., Vaudry H.;
RT "Characterization of a novel alpha-amidated decapeptide derived from
RT proopiomelanocortin-A in the trout pituitary.";
RL Endocrinology 138:128-137(1997).
RN [4]
RP TISSUE SPECIFICITY OF C-TERMINAL PEPTIDES.
RX PubMed=10022961; DOI=10.1007/s004410051247;
RA Tollemer H., Teitsma C.A., Leprince J., Bailhache T., Vandesande F.,
RA Kah O., Tonon M.C., Vaudry H.;
RT "Immunohistochemical localization and biochemical characterization of two
RT novel decapeptides derived from POMC-A in the trout hypothalamus.";
RL Cell Tissue Res. 295:409-417(1999).
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: C-terminal peptide 1 and C-terminal peptide 2 are
CC detected in the anterior part of the nucleus lateralis tuberis of
CC hypothalamus, in dorsal hypothalamus, thalamus, telencephalon, optic
CC tectum and medulla oblongata (at protein level). Expressed in pituitary
CC and hypothalamus of adult diploid animals, and hypothalamus of triploid
CC and ovulated female trout. {ECO:0000269|PubMed:10022961}.
CC -!- DEVELOPMENTAL STAGE: Expressed in sexually active or inactive 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 -!- MASS SPECTROMETRY: [C-terminal peptide 2]: Mass=1246.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9299569};
CC -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
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DR EMBL; X69808; CAA49466.1; -; mRNA.
DR PIR; A45359; A45359.
DR RefSeq; NP_001118190.1; NM_001124718.1.
DR AlphaFoldDB; Q04617; -.
DR Ensembl; ENSOMYT00000033728; ENSOMYP00000030934; ENSOMYG00000014502.
DR GeneID; 100136771; -.
DR KEGG; omy:100136771; -.
DR GeneTree; ENSGT00390000016811; -.
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 1: Evidence at protein level;
KW Acetylation; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Endorphin; Hormone;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PEPTIDE 22..101
FT /note="NPP 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025093"
FT PEPTIDE 104..142
FT /note="Corticotropin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025094"
FT PEPTIDE 104..116
FT /note="Melanocyte-stimulating hormone alpha 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025095"
FT PEPTIDE 122..142
FT /note="Corticotropin-like intermediary peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025096"
FT PEPTIDE 145..228
FT /note="Lipotropin beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025097"
FT PEPTIDE 145..196
FT /note="Lipotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025098"
FT PEPTIDE 180..196
FT /note="Melanocyte-stimulating hormone beta 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025099"
FT PEPTIDE 199..228
FT /note="Beta-endorphin 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025100"
FT PEPTIDE 199..203
FT /note="Met-enkephalin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025101"
FT PEPTIDE 231..240
FT /note="C-terminal peptide 1"
FT /id="PRO_0000411981"
FT PEPTIDE 243..252
FT /note="C-terminal peptide 2"
FT /id="PRO_0000411982"
FT REGION 228..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 104
FT /note="N-acetylserine; in Corticotropin"
FT /evidence="ECO:0000250"
FT MOD_RES 116
FT /note="Valine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 252
FT /note="Glutamine amide; partial"
FT /evidence="ECO:0000269|PubMed:8977395,
FT ECO:0000269|PubMed:9299569"
FT DISULFID 23..45
FT /evidence="ECO:0000250"
FT DISULFID 29..41
FT /evidence="ECO:0000250"
SQ SEQUENCE 253 AA; 28559 MW; 75A3C3E11C7386D5 CRC64;
MLCPAWLLAV AVVGVVRGVK GQCWENPRCH DLSSENNLLE CIQLCRSDLT TKSPIFPVKV
HLQPPSPSDS DSPPLYLPLS LLSPSSPLYP TEQQNSVSPQ AKRSYSMEHF RWGKPVGRKR
RPVKVYTNGV EEESSEAFPS EMRRELGTDD AVYPSLEAGT AEGGEAEGME GVFSLQEKKD
GSYKMNHFRW SGPPASKRYG GFMKSWDERS QKPLLTLFKN VIIKDGQQKR EQWGREEGEE
KRALGERKYH FQG
