ID K7AJ99_PANTR Unreviewed; 182 AA.
AC K7AJ99; A0A2J8MNN3; H2R7R7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|RuleBase:RU365044};
DE EC=1.8.4.12 {ECO:0000256|RuleBase:RU365044};
GN Name=MSRB2 {ECO:0000313|EMBL:JAA18101.1,
GN ECO:0000313|Ensembl:ENSPTRP00000050733.5,
GN ECO:0000313|VGNC:VGNC:53395};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA18101.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000050733.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA18101.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02904.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA43024.1}, Skin {ECO:0000313|EMBL:JAA28745.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA18101.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000050733.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces
CC methionine (R)-sulfoxide back to methionine. While in many cases
CC methionine oxidation is the result of random oxidation following
CC oxidative stress, methionine oxidation is also a post-translational
CC modification that takes place on specific residues.
CC {ECO:0000256|RuleBase:RU365044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, 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:58773; EC=1.8.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000502};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC Evidence={ECO:0000256|RuleBase:RU365044};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU365044};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU365044};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000256|ARBA:ARBA00007174, ECO:0000256|RuleBase:RU365044}.
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DR EMBL; AACZ04070765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01008434; JAA02904.1; -; mRNA.
DR EMBL; GABF01004044; JAA18101.1; -; mRNA.
DR EMBL; GABD01004355; JAA28745.1; -; mRNA.
DR EMBL; GABE01001715; JAA43024.1; -; mRNA.
DR STRING; 9598.ENSPTRP00000050733; -.
DR PaxDb; 9598-ENSPTRP00000050733; -.
DR Ensembl; ENSPTRT00000057797.5; ENSPTRP00000050733.5; ENSPTRG00000029920.5.
DR VGNC; VGNC:53395; MSRB2.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00940000161673; -.
DR OMA; CDVPLFS; -.
DR TreeFam; TF329147; -.
DR Proteomes; UP000002277; Chromosome 10.
DR Bgee; ENSPTRG00000029920; Expressed in heart and 21 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl.
DR GO; GO:0030091; P:protein repair; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR10173:SF37; METHIONINE-R-SULFOXIDE REDUCTASE B2, MITOCHONDRIAL; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|RuleBase:RU365044};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365044};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Signal {ECO:0000256|RuleBase:RU365044};
KW Zinc {ECO:0000256|RuleBase:RU365044}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU365044"
FT CHAIN 17..182
FT /note="Peptide-methionine (R)-S-oxide reductase"
FT /evidence="ECO:0000256|RuleBase:RU365044"
FT /id="PRO_5015095792"
FT DOMAIN 51..180
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 182 AA; 19509 MW; D77341063463A550 CRC64;
MARLLWLLRG LTLGTAPRRA VRGQAGGGGP GTGPGLGEAG SLATCELPLA KSEWQKKLTP
EQFYVTREKG TEPPFSGIYL NSKEAGMYHC VCCDSPLFSS EKKYCSGTGW PSFSEAHGTS
GSDESHTGIL RRLDTSLGSA RTEVVCKQCE AHLGHVFPDG PGPNGQRFCI NSVALKFKPR
KH
//
