COLI2_XENLA
ID COLI2_XENLA Reviewed; 260 AA.
AC P06299;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Pro-opiomelanocortin B;
DE Short=POMC-B;
DE AltName: Full=Corticotropin-lipotropin B;
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-b;
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 [GENOMIC DNA].
RX PubMed=1915355; DOI=10.1111/j.1432-1033.1991.tb16265.x;
RA Deen P.M.T., Terwel D., Bussemakers M.J.M., Roubos E.W., Martens J.M.;
RT "Structural analysis of the entire proopiomelanocortin gene of Xenopus
RT laevis.";
RL Eur. J. Biochem. 201:129-137(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3595598; DOI=10.1111/j.1432-1033.1987.tb11462.x;
RA Martens G.J.M.;
RT "Structural organization of the proopiomelanocortin gene in Xenopus laevis.
RT 5'-end homologies within the toad and mammalian genes.";
RL Eur. J. Biochem. 165:467-472(1987).
RN [4]
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=CAA27471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X59369; CAA42012.1; -; Genomic_DNA.
DR EMBL; X03844; CAA27466.1; -; mRNA.
DR EMBL; X03844; CAA27467.1; ALT_SEQ; mRNA.
DR EMBL; X03844; CAA27468.1; ALT_SEQ; mRNA.
DR EMBL; X03844; CAA27469.1; ALT_SEQ; mRNA.
DR EMBL; X03844; CAA27470.1; ALT_SEQ; mRNA.
DR EMBL; X03844; CAA27471.1; ALT_INIT; mRNA.
DR EMBL; X05940; CAA29374.1; -; Genomic_DNA.
DR EMBL; X05941; CAA29374.1; JOINED; Genomic_DNA.
DR PIR; A01461; CTXLPB.
DR RefSeq; NP_001156862.1; NM_001163390.1.
DR AlphaFoldDB; P06299; -.
DR SMR; P06299; -.
DR GeneID; 373802; -.
DR KEGG; xla:373802; -.
DR CTD; 373802; -.
DR Xenbase; XB-GENE-6252423; pomc.S.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 373802; 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_0000025161"
FT PEPTIDE 76..86
FT /note="Melanotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025162"
FT PROPEP 104..138
FT /id="PRO_0000025163"
FT PEPTIDE 141..179
FT /note="Corticotropin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025164"
FT PEPTIDE 141..153
FT /note="Melanocyte-stimulating hormone alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025165"
FT PEPTIDE 159..179
FT /note="Corticotropin-like intermediary peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025166"
FT PEPTIDE 182..260
FT /note="Lipotropin beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025167"
FT PEPTIDE 182..227
FT /note="Lipotropin gamma"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025168"
FT PEPTIDE 211..227
FT /note="Melanocyte-stimulating hormone beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025169"
FT PEPTIDE 230..260
FT /note="Beta-endorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025170"
FT PEPTIDE 230..234
FT /note="Met-enkephalin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025171"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 153
FT /note="Valine amide"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
SQ SEQUENCE 260 AA; 29917 MW; A7FD70D9197CB99F CRC64;
MFRPTGGCSL AILGVFIFHI GEVQSQCWES SRCADLSSED GILECIKACK MDLSAESPVF
PGNGHLQPLS ESIRKYVMTH FRWNKFGRRN NTGNDGSSGG YKREDISNYP VLNLFPSSDN
QNAQGDNMEE EPMDRQENKR AYSMEHFRWG KPVGRKRRPI KVYPNGVEEE SAESFPMELR
RELSLELDYP EIDLDEDIED NEVERALTKK NGNYRMHHFR WGSPPKDKRY GGFMTPERSQ
TPLMTLFKNA IIKNTHKKGL
