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MSRA_BRANA
ID   MSRA_BRANA              Reviewed;         257 AA.
AC   P54151;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Peptide methionine sulfoxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
DE   AltName: Full=Protein-methionine-S-oxide reductase;
GN   Name=PMSR;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jet neuf;
RX   PubMed=8111035; DOI=10.1007/bf00020171;
RA   Keddie J.S., Tsiantis M., Piffanelli P., Cella R., Hatzopoulos P.,
RA   Murphy D.J.;
RT   "A seed-specific Brassica napus oleosin promoter interacts with a G-box-
RT   specific protein and may be bi-directional.";
RL   Plant Mol. Biol. 24:327-340(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-4; ALA-14; SER-24; ALA-75 AND
RP   SER-129.
RC   TISSUE=Leaf;
RX   PubMed=8771781; DOI=10.1046/j.1365-313x.1996.10020235.x;
RA   Sadanandom A.C., Piffanelli P., Knott T., Robinson C., Sharpe A.,
RA   Lydiate D., Murphy D.J., Fairbairn D.J.;
RT   "Identification of a peptide methionine sulphoxide reductase gene in an
RT   oleosin promoter from Brassica napus.";
RL   Plant J. 10:235-242(1996).
CC   -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC       that have been inactivated by oxidation. Catalyzes the reversible
CC       oxidation-reduction of methionine sulfoxide in proteins to methionine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58772; EC=1.8.4.11;
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000305}.
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DR   EMBL; X94225; CAA63919.1; -; Genomic_DNA.
DR   EMBL; Z48619; CAA88538.1; -; mRNA.
DR   EMBL; X91486; CAA62760.1; -; mRNA.
DR   PIR; S55365; S55365.
DR   PIR; T47215; T47215.
DR   RefSeq; NP_001302774.1; NM_001315845.1.
DR   RefSeq; NP_001302784.1; NM_001315855.1.
DR   AlphaFoldDB; P54151; -.
DR   SMR; P54151; -.
DR   GeneID; 106346565; -.
DR   GeneID; 106442570; -.
DR   KEGG; bna:106346565; -.
DR   KEGG; bna:106442570; -.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Phosphoprotein.
FT   CHAIN           1..257
FT                   /note="Peptide methionine sulfoxide reductase"
FT                   /id="PRO_0000138633"
FT   REGION          61..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LY15"
FT   VARIANT         4
FT                   /note="I -> L"
FT                   /evidence="ECO:0000269|PubMed:8771781"
FT   VARIANT         14
FT                   /note="V -> A"
FT                   /evidence="ECO:0000269|PubMed:8771781"
FT   VARIANT         24
FT                   /note="A -> S"
FT                   /evidence="ECO:0000269|PubMed:8771781"
FT   VARIANT         75
FT                   /note="S -> A"
FT                   /evidence="ECO:0000269|PubMed:8771781"
FT   VARIANT         129
FT                   /note="T -> S"
FT                   /evidence="ECO:0000269|PubMed:8771781"
SQ   SEQUENCE   257 AA;  28466 MW;  41F4440E41772788 CRC64;
     MLSIVASPPV ISAVSLSKPL QSLAKAALSL SKRAKPTSPF PKTARSISVY KSPMNNLFTR
     LGFGSRPQPD PAASSAIAQG PDDDVPSPGQ QFAQFGAGCF WGAELAYQRV PGVTKTEVGY
     SHGFVDNPTY EDVCSETTGH NEIVRVQYDP KEVSFESLLD VFWKRHDPTT LNRQGNDVGT
     RYRSGIYFYT DEQEKLAREA MEKQQKILNR KIVTEILPAT KFYRAENYHQ QYLAKGGRMG
     LSQSAEKGCN DPIRCYG
 
 
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