COLI1_XENLA
ID COLI1_XENLA Reviewed; 259 AA.
AC P06298; P87464; Q91824; Q9PU10;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pro-opiomelanocortin A;
DE Short=POMC-A;
DE AltName: Full=Corticotropin-lipotropin A;
DE Contains:
DE RecName: Full=NPP;
DE Contains:
DE RecName: Full=Melanotropin gamma;
DE AltName: Full=Gamma-MSH;
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-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3754961; DOI=10.1093/nar/14.9.3791;
RA Martens G.J.M.;
RT "Expression of two proopiomelanocortin genes in the pituitary gland of
RT Xenopus laevis: complete structures of the two preprohormones.";
RL Nucleic Acids Res. 14:3791-3798(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1584015; DOI=10.1093/oxfordjournals.molbev.a040736;
RA Deen P.M., Bussemakers M.J., Terwel D., Roubos E.W., Martens G.J.M.;
RT "Comparative structural analysis of the transcriptionally active
RT proopiomelanocortin genes A and B of Xenopus laevis.";
RL Mol. Biol. Evol. 9:483-494(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 57-259.
RX PubMed=3840481; DOI=10.1016/s0021-9258(17)38779-3;
RA Martens G.J.M., Civelli O., Herbert E.;
RT "Nucleotide sequence of cloned cDNA for pro-opiomelanocortin in the
RT amphibian Xenopus laevis.";
RL J. Biol. Chem. 260:13685-13689(1985).
RN [5]
RP PROTEIN SEQUENCE OF 140-149 AND 210-225.
RX PubMed=2564347; DOI=10.1016/0014-5793(89)80224-8;
RA Rouille Y., Michel G., Chauvet M.T., Chauvet J., Acher R.;
RT "Particular processing of pro-opiomelanocortin in Xenopus laevis
RT intermediate pituitary. Sequencing of alpha- and beta-melanocyte-
RT stimulating hormones.";
RL FEBS Lett. 245:215-218(1989).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27465.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X03843; CAA27460.1; -; mRNA.
DR EMBL; X03843; CAA27461.1; ALT_SEQ; mRNA.
DR EMBL; X03843; CAA27462.1; ALT_SEQ; mRNA.
DR EMBL; X03843; CAA27463.1; ALT_SEQ; mRNA.
DR EMBL; X03843; CAA27464.1; ALT_SEQ; mRNA.
DR EMBL; X03843; CAA27465.1; ALT_INIT; mRNA.
DR EMBL; X59370; CAA42013.2; -; Genomic_DNA.
DR EMBL; BC054160; AAH54160.1; -; mRNA.
DR EMBL; M11346; AAA49932.1; -; mRNA.
DR PIR; A01460; CTXLPA.
DR RefSeq; NP_001080838.1; NM_001087369.2.
DR AlphaFoldDB; P06298; -.
DR SMR; P06298; -.
DR DNASU; 380532; -.
DR GeneID; 380532; -.
DR KEGG; xla:380532; -.
DR CTD; 380532; -.
DR Xenbase; XB-GENE-483707; pomc.L.
DR OrthoDB; 1168862at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 380532; Expressed in brain and 4 other tissues.
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; 3.
DR Pfam; PF08384; NPP; 1.
DR Pfam; PF08035; Op_neuropeptide; 1.
DR PRINTS; PR00383; MELANOCORTIN.
DR SMART; SM01363; ACTH_domain; 3.
DR SMART; SM01364; NPP; 1.
DR SMART; SM01365; Op_neuropeptide; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Endorphin; Glycoprotein; Hormone; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT PEPTIDE 26..101
FT /note="NPP"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025150"
FT PEPTIDE 76..86
FT /note="Melanotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025151"
FT PROPEP 104..137
FT /id="PRO_0000025152"
FT PEPTIDE 140..178
FT /note="Corticotropin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025153"
FT PEPTIDE 140..152
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000025154"
FT PEPTIDE 158..178
FT /note="Corticotropin-like intermediary peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025155"
FT PEPTIDE 181..259
FT /note="Lipotropin beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025156"
FT PEPTIDE 181..226
FT /note="Lipotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025157"
FT PEPTIDE 210..226
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000025158"
FT PEPTIDE 229..259
FT /note="Beta-endorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025159"
FT PEPTIDE 229..233
FT /note="Met-enkephalin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025160"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 86
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="Valine amide"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT CONFLICT 57
FT /note="S -> L (in Ref. 4; AAA49932)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="E -> K (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29879 MW; 4D3804ABEE3EED20 CRC64;
MFRPLWGCFL AILGICIFHI GEVQSQCWES SRCADLSSED GVLECIKACK TDLSAESPVF
PGNGHLQPLS ESIRKYVMTH FRWNKFGRRN STGNDGSNTG YKREDISSYP VFSLFPLSDQ
NAPGDNMEEE PLDRQENKRA YSMEHFRWGK PVGRKRRPIK VYPNGVEEES AESYPMELRR
ELSLELDYPE IDLDEDIEDN EVESALTKKN GNYRMHHFRW GSPPKDKRYG GFMTPERSQT
PLMTLFKNAI IKNSHKKGQ
