MSRB1_HUMAN
ID MSRB1_HUMAN Reviewed; 116 AA.
AC Q9NZV6; Q96RX6; Q9BTV2; Q9P0B1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Methionine-R-sulfoxide reductase B1;
DE Short=MsrB1;
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;
DE Short=SelX;
GN Name=MSRB1; Synonyms=SEPX1; ORFNames=HSPC270;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10608886; DOI=10.1074/jbc.274.53.38147;
RA Lescure A., Gautheret D., Carbon P., Krol A.;
RT "Novel selenoproteins identified in silico and in vivo by using a conserved
RT RNA structural motif.";
RL J. Biol. Chem. 274:38147-38154(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chabot M., de Medicis E.;
RT "The human methionine sulfoxide reductase mRNA codes for a selenoprotein.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP UBIQUITINATION.
RX PubMed=26138980; DOI=10.1126/science.aab0515;
RA Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.;
RT "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced
RT by failed UGA/Sec decoding.";
RL Science 349:91-95(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 10-112 IN COMPLEX WITH IRON,
RP COFACTOR, AND ZINC-BINDING SITES.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human methionine-r-sulfoxide reductase b1 (msrb1).";
RL Submitted (APR-2010) to the PDB data bank.
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; Evidence={ECO:0000269|Ref.8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9JLC3};
CC -!- INTERACTION:
CC Q9NZV6; PRO_0000000092 [P05067]: APP; NbExp=4; IntAct=EBI-12330065, EBI-821758;
CC Q9NZV6; P10909-5: CLU; NbExp=10; IntAct=EBI-12330065, EBI-10961636;
CC Q9NZV6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12330065, EBI-3867333;
CC Q9NZV6; Q13099: IFT88; NbExp=3; IntAct=EBI-12330065, EBI-347427;
CC Q9NZV6; Q0VD86: INCA1; NbExp=3; IntAct=EBI-12330065, EBI-6509505;
CC Q9NZV6; P14373: TRIM27; NbExp=3; IntAct=EBI-12330065, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9JLC3}.
CC -!- PTM: Truncated MSRB1/SEPX1 proteins produced by failed UGA/Sec decoding
CC are ubiquitinated by some Cul2-RING E3 ubiquitin-protein ligase
CC complexes (containing either PRAME, PRAMF6, PRAMF9 or FEM1C as
CC substrate-recognition component). {ECO:0000269|PubMed:26138980}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28948.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF166124; AAF21429.1; -; mRNA.
DR EMBL; AF187272; AAG17033.1; -; mRNA.
DR EMBL; AF161388; AAF28948.1; ALT_SEQ; mRNA.
DR EMBL; AE006640; AAK61300.1; -; Genomic_DNA.
DR EMBL; AC005363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003127; AAH03127.2; -; mRNA.
DR CCDS; CCDS42100.1; -.
DR RefSeq; NP_057416.1; NM_016332.3.
DR PDB; 3MAO; X-ray; 1.42 A; A=10-112.
DR PDBsum; 3MAO; -.
DR SMR; Q9NZV6; -.
DR BioGRID; 119704; 10.
DR IntAct; Q9NZV6; 11.
DR MINT; Q9NZV6; -.
DR STRING; 9606.ENSP00000355084; -.
DR DrugBank; DB00134; Methionine.
DR iPTMnet; Q9NZV6; -.
DR PhosphoSitePlus; Q9NZV6; -.
DR BioMuta; MSRB1; -.
DR DMDM; 182676387; -.
DR EPD; Q9NZV6; -.
DR jPOST; Q9NZV6; -.
DR MassIVE; Q9NZV6; -.
DR PaxDb; Q9NZV6; -.
DR PeptideAtlas; Q9NZV6; -.
DR PRIDE; Q9NZV6; -.
DR ProteomicsDB; 83519; -.
DR Antibodypedia; 58024; 128 antibodies from 24 providers.
DR DNASU; 51734; -.
DR Ensembl; ENST00000361871.8; ENSP00000355084.3; ENSG00000198736.13.
DR GeneID; 51734; -.
DR KEGG; hsa:51734; -.
DR MANE-Select; ENST00000361871.8; ENSP00000355084.3; NM_016332.4; NP_057416.1.
DR UCSC; uc021tam.2; human.
DR CTD; 51734; -.
DR DisGeNET; 51734; -.
DR GeneCards; MSRB1; -.
DR HGNC; HGNC:14133; MSRB1.
DR HPA; ENSG00000198736; Tissue enhanced (liver).
DR MIM; 606216; gene.
DR neXtProt; NX_Q9NZV6; -.
DR OpenTargets; ENSG00000198736; -.
DR PharmGKB; PA37848; -.
DR VEuPathDB; HostDB:ENSG00000198736; -.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00510000047678; -.
DR HOGENOM; CLU_147472_1_0_1; -.
DR InParanoid; Q9NZV6; -.
DR OMA; NDGPAKG; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q9NZV6; -.
DR TreeFam; TF329147; -.
DR BRENDA; 1.8.4.12; 2681.
DR PathwayCommons; Q9NZV6; -.
DR Reactome; R-HSA-5676934; Protein repair.
DR SignaLink; Q9NZV6; -.
DR BioGRID-ORCS; 51734; 69 hits in 1081 CRISPR screens.
DR ChiTaRS; MSRB1; human.
DR GeneWiki; SEPX1; -.
DR GenomeRNAi; 51734; -.
DR Pharos; Q9NZV6; Tbio.
DR PRO; PR:Q9NZV6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NZV6; protein.
DR Bgee; ENSG00000198736; Expressed in blood and 191 other tissues.
DR ExpressionAtlas; Q9NZV6; baseline and differential.
DR Genevisible; Q9NZV6; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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: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:0008270; F:zinc ion binding; ISS:HGNC-UCL.
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; ISS:HGNC-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Selenocysteine;
KW Ubl conjugation; Zinc.
FT CHAIN 1..116
FT /note="Methionine-R-sulfoxide reductase B1"
FT /id="PRO_0000140321"
FT DOMAIN 1..106
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 95
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 ECO:0000269|Ref.8"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|Ref.8"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|Ref.8"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|Ref.8"
FT NON_STD 95
FT /note="Selenocysteine"
FT /evidence="ECO:0000305|PubMed:10608886"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:3MAO"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3MAO"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3MAO"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3MAO"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3MAO"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3MAO"
SQ SEQUENCE 116 AA; 12760 MW; 812B033BE02B7C0E CRC64;
MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE
HNRSEALKVS CGKCGNGLGH EFLNDGPKPG QSRFUIFSSS LKFVPKGKET SASQGH
