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COLI_ONCKE
ID   COLI_ONCKE              Reviewed;         226 AA.
AC   P10000; P01199; P01204; P87470; P87471; P87472; P87473; P87474; P87475;
AC   P87476; P87477; P87478; Q90521; Q92024;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   25-MAY-2022, entry version 90.
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   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3197404; DOI=10.1016/0305-0491(88)90155-1;
RA   Kitahara N., Nishizawa T., Iida K., Okazaki H., Andoh T., Soma G.;
RT   "Absence of a gamma-melanocyte-stimulating hormone sequence in
RT   proopiomelanocortin mRNA of chum salmon Oncorhynchus keta.";
RL   Comp. Biochem. Physiol. 91B:365-370(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-226.
RX   PubMed=6095185; DOI=10.1093/nar/12.21.8029;
RA   Soma G., Kitahara N., Nishizawa T., Nanami H., Kotake C., Okazaki H.,
RA   Andoh T.;
RT   "Nucleotide sequence of a cloned cDNA for proopiomelanocortin precursor of
RT   chum salmon, Onchorynchus keta.";
RL   Nucleic Acids Res. 12:8029-8041(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-226.
RX   PubMed=6087806; DOI=10.1016/s0006-291x(84)80069-8;
RA   Nishizawa T., Kitahara N., Nanami H., Hara N., Kotake C., Okazaki H.,
RA   Andoh T., Soma G.;
RT   "Heterogeneity of 3' nontranslated regions in proopiomelanocortin (POMC)
RT   precursor mRNA of chum salmon Onchorynchus keta: polymorphism of the
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 122:556-562(1984).
RN   [4]
RP   PROTEIN SEQUENCE OF 98-112, AND ACETYLATION AT SER-98.
RX   PubMed=7447938; DOI=10.1016/0006-291x(80)91345-5;
RA   Kawauchi H., Adachi Y., Tsubokawa M.;
RT   "Occurrence of a new melanocyte stimulating hormone in the salmon pituitary
RT   gland.";
RL   Biochem. Biophys. Res. Commun. 96:1508-1517(1980).
RN   [5]
RP   PROTEIN SEQUENCE OF 198-226, AND ACETYLATION AT TYR-198.
RX   PubMed=475783; DOI=10.1016/0006-291x(79)91114-8;
RA   Kawauchi H., Tsubokawa M., Muramoto K.;
RT   "Isolation and primary structure of endorphin from salmon pituitary
RT   glands.";
RL   Biochem. Biophys. Res. Commun. 88:1249-1254(1979).
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=AAA49426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M27692; AAA49426.1; ALT_INIT; mRNA.
DR   EMBL; K02613; AAA49424.1; -; mRNA.
DR   EMBL; K02614; AAA49425.1; -; mRNA.
DR   EMBL; X01122; CAA25591.1; -; mRNA.
DR   PIR; I51080; CTONPK.
DR   AlphaFoldDB; P10000; -.
DR   iPTMnet; P10000; -.
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; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Endorphin; Hormone; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..97
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025083"
FT   PEPTIDE         98..138
FT                   /note="Corticotropin"
FT                   /id="PRO_0000025084"
FT   PEPTIDE         98..112
FT                   /note="Melanocyte-stimulating hormone alpha"
FT                   /evidence="ECO:0000269|PubMed:7447938"
FT                   /id="PRO_0000025085"
FT   PEPTIDE         116..138
FT                   /note="Corticotropin-like intermediary peptide"
FT                   /id="PRO_0000025086"
FT   PEPTIDE         141..226
FT                   /note="Lipotropin beta"
FT                   /id="PRO_0000025087"
FT   PEPTIDE         141..195
FT                   /note="Lipotropin gamma"
FT                   /id="PRO_0000025088"
FT   PEPTIDE         179..195
FT                   /note="Melanocyte-stimulating hormone beta"
FT                   /id="PRO_0000025089"
FT   PEPTIDE         198..226
FT                   /note="Beta-endorphin"
FT                   /evidence="ECO:0000269|PubMed:475783"
FT                   /id="PRO_0000025090"
FT   PEPTIDE         198..202
FT                   /note="Met-enkephalin"
FT                   /evidence="ECO:0000269|PubMed:475783"
FT                   /id="PRO_0000025091"
FT   MOD_RES         98
FT                   /note="N-acetylserine; in Corticotropin"
FT                   /evidence="ECO:0000269|PubMed:7447938"
FT   MOD_RES         198
FT                   /note="N-acetyltyrosine; in Beta-endorphin and Met-
FT                   enkephalin"
FT                   /evidence="ECO:0000269|PubMed:475783"
SQ   SEQUENCE   226 AA;  24982 MW;  327CA785F69B1B24 CRC64;
     MVCAPWLLAV VVVCVCNPGV GGQCWDSSHC KDLPSEDKIL ECTHLFRSGL QDESPEPRSA
     AQQSTEESLS LGILLAALTS GERALDADPE PHSDKRHSYS MEHFRWGKPI GHKRRPIKVY
     ASSLEGGDSS EGTFPLQARR QLGSWEDEMV GALGNQGAKA QTKVVPRTLT VTGLQDKKDG
     SYRMGHFRWG SPTAIKRYGG FMKPYTKQSH KPLITLLKHI TLKNEQ
 
 
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