MSB1A_DANRE
ID MSB1A_DANRE Reviewed; 110 AA.
AC Q802G6; Q6NWX6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Methionine-R-sulfoxide reductase B1-A;
DE Short=MsrB;
DE Short=MsrB1-A;
DE EC=1.8.4.12 {ECO:0000250|UniProtKB:Q9JLC3};
DE EC=1.8.4.14 {ECO:0000250|UniProtKB:Q9JLC3};
DE AltName: Full=Selenoprotein X-A;
DE Short=SePR;
DE Short=SelX-A;
GN Name=msrb1; Synonyms=sepx1, sepx1a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=12915322; DOI=10.1016/s1567-133x(03)00054-1;
RA Thisse C., Degrave A., Kryukov G.V., Gladyshev V.N., Obrecht-Pflumio S.,
RA Krol A., Thisse B., Lescure A.;
RT "Spatial and temporal expression patterns of selenoprotein genes during
RT embryogenesis in zebrafish.";
RL Gene Expr. Patterns 3:525-532(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 residue. Acts as a regulator
CC of actin assembly by reducing methionine (R)-sulfoxide mediated by
CC MICALs (mical1, mical2 or mical3) on actin, thereby promoting filament
CC repolymerization. Plays a role in innate immunity by reducing oxidized
CC actin, leading to actin repolymerization in macrophages.
CC {ECO:0000250|UniProtKB:Q9JLC3}.
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:0000250|UniProtKB:Q9JLC3};
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:0000250|UniProtKB:Q9JLC3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9JLC3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9JLC3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9JLC3}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in the polster, paraxial
CC mesoderm, tectum, otic vesicle and liver.
CC {ECO:0000269|PubMed:12915322}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AY216585; AAO86699.1; -; mRNA.
DR EMBL; BC067380; AAH67380.1; -; mRNA.
DR RefSeq; NP_840073.2; NM_178288.5.
DR STRING; 7955.ENSDARP00000115071; -.
DR PaxDb; Q802G6; -.
DR Ensembl; ENSDART00000131758; ENSDARP00000122736; ENSDARG00000025436.
DR GeneID; 352916; -.
DR KEGG; dre:352916; -.
DR CTD; 352916; -.
DR ZFIN; ZDB-GENE-030411-3; msrb1a.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00510000047678; -.
DR HOGENOM; CLU_147472_1_0_1; -.
DR InParanoid; Q802G6; -.
DR OMA; NDGPAKG; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q802G6; -.
DR Reactome; R-DRE-5676934; Protein repair.
DR PRO; PR:Q802G6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000025436; Expressed in head kidney and 39 other tissues.
DR ExpressionAtlas; Q802G6; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; IBA:GO_Central.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0030091; P:protein repair; IBA:GO_Central.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Immunity; Innate immunity; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Selenocysteine; Zinc.
FT CHAIN 1..110
FT /note="Methionine-R-sulfoxide reductase B1-A"
FT /id="PRO_0000318636"
FT DOMAIN 1..104
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT NON_STD 93
FT /note="Selenocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZV6"
FT CONFLICT 52
FT /note="E -> K (in Ref. 1; AAO86699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12553 MW; 0639C892C7861174 CRC64;
MSFCSFSGGE IYKDHFESGM YVCAQCGYEL FSSRSKYEHS SPWPAFTETI HEDSVSKQEE
RWGAYKVRCG KCGNGLGHEF VNDGPKHGLS RFUIFSSSLK FIPKVKNEQQ
