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Methionine-R-sulfoxide reductase B1 (MsrB1) (EC 1.8.4.-) (Selenoprotein X) (SelX)

 MSRB1_HUMAN             Reviewed;         116 AA.
Q9NZV6; Q96RX6; Q9BTV2; Q9P0B1;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 3.
27-SEP-2017, entry version 142.
RecName: Full=Methionine-R-sulfoxide reductase B1;
Short=MsrB1;
EC=1.8.4.-;
AltName: Full=Selenoprotein X;
Short=SelX;
Name=MSRB1; Synonyms=SEPX1; ORFNames=HSPC270;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10608886; DOI=10.1074/jbc.274.53.38147;
Lescure A., Gautheret D., Carbon P., Krol A.;
"Novel selenoproteins identified in silico and in vivo by using a
conserved RNA structural motif.";
J. Biol. Chem. 274:38147-38154(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Chabot M., de Medicis E.;
"The human methionine sulfoxide reductase mRNA codes for a
selenoprotein.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11157797; DOI=10.1093/hmg/10.4.339;
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2
Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 10-112 IN COMPLEX WITH IRON,
COFACTOR, AND ZINC-BINDING SITES.
Structural genomics consortium (SGC);
"Crystal structure of human methionine-r-sulfoxide reductase b1
(msrb1).";
Submitted (APR-2010) to the PDB data bank.
-!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces
methionine (R)-sulfoxide back to methionine. While in many cases,
methionine oxidation is the result of random oxidation following
oxidative stress, methionine oxidation is also a post-
translational modification that takes place on specific residue.
Acts as a regulator of actin assembly by reducing methionine (R)-
sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3) on actin,
thereby promoting filament repolymerization. Plays a role in
innate immunity by reducing oxidized actin, leading to actin
repolymerization in macrophages (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: L-methionine + oxidized thioredoxin = L-
methionine R-oxide + reduced thioredoxin.
{ECO:0000250|UniProtKB:Q9JLC3}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.7};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9JLC3};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}.
Nucleus {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9JLC3}.
-!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF28948.1; Type=Erroneous termination; Positions=95; Note=Translated as Sec.; Evidence={ECO:0000305};
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EMBL; AF166124; AAF21429.1; -; mRNA.
EMBL; AF187272; AAG17033.1; -; mRNA.
EMBL; AF161388; AAF28948.1; ALT_SEQ; mRNA.
EMBL; AE006640; AAK61300.1; -; Genomic_DNA.
EMBL; AC005363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003127; AAH03127.2; -; mRNA.
CCDS; CCDS42100.1; -.
RefSeq; NP_057416.1; NM_016332.3.
UniGene; Hs.655346; -.
PDB; 3MAO; X-ray; 1.42 A; A=10-112.
PDBsum; 3MAO; -.
ProteinModelPortal; Q9NZV6; -.
SMR; Q9NZV6; -.
BioGrid; 119704; 3.
IntAct; Q9NZV6; 5.
STRING; 9606.ENSP00000355084; -.
DrugBank; DB00134; L-Methionine.
PhosphoSitePlus; Q9NZV6; -.
BioMuta; MSRB1; -.
DMDM; 182676387; -.
EPD; Q9NZV6; -.
PaxDb; Q9NZV6; -.
PeptideAtlas; Q9NZV6; -.
PRIDE; Q9NZV6; -.
Ensembl; ENST00000361871; ENSP00000355084; ENSG00000198736.
GeneID; 51734; -.
KEGG; hsa:51734; -.
UCSC; uc021tam.2; human.
CTD; 51734; -.
DisGeNET; 51734; -.
EuPathDB; HostDB:ENSG00000198736.11; -.
GeneCards; MSRB1; -.
H-InvDB; HIX0012700; -.
HGNC; HGNC:14133; MSRB1.
HPA; CAB008650; -.
MIM; 606216; gene.
neXtProt; NX_Q9NZV6; -.
OpenTargets; ENSG00000198736; -.
PharmGKB; PA37848; -.
eggNOG; KOG0856; Eukaryota.
eggNOG; COG0229; LUCA.
GeneTree; ENSGT00510000047678; -.
HOGENOM; HOG000243424; -.
HOVERGEN; HBG002192; -.
InParanoid; Q9NZV6; -.
KO; K07305; -.
PhylomeDB; Q9NZV6; -.
TreeFam; TF329147; -.
BRENDA; 1.8.4.12; 2681.
Reactome; R-HSA-5676934; Protein repair.
GeneWiki; SEPX1; -.
GenomeRNAi; 51734; -.
PRO; PR:Q9NZV6; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000198736; -.
CleanEx; HS_SEPX1; -.
ExpressionAtlas; Q9NZV6; baseline and differential.
Genevisible; Q9NZV6; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; ISS:UniProtKB.
GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; IEA:Ensembl.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:HGNC.
GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0030091; P:protein repair; ISS:HGNC.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
PROSITE; PS51790; MSRB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoskeleton; Immunity;
Innate immunity; Metal-binding; Nucleus; Oxidoreductase;
Reference proteome; Selenocysteine; Zinc.
CHAIN 1 116 Methionine-R-sulfoxide reductase B1.
/FTId=PRO_0000140321.
DOMAIN 1 106 MsrB. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
ACT_SITE 95 95 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
METAL 23 23 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126, ECO:0000269|Ref.7}.
METAL 26 26 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126, ECO:0000269|Ref.7}.
METAL 71 71 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126, ECO:0000269|Ref.7}.
METAL 74 74 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126, ECO:0000269|Ref.7}.
NON_STD 95 95 Selenocysteine.
STRAND 18 23 {ECO:0000244|PDB:3MAO}.
TURN 24 26 {ECO:0000244|PDB:3MAO}.
STRAND 29 32 {ECO:0000244|PDB:3MAO}.
HELIX 33 35 {ECO:0000244|PDB:3MAO}.
STRAND 40 43 {ECO:0000244|PDB:3MAO}.
STRAND 45 47 {ECO:0000244|PDB:3MAO}.
STRAND 54 59 {ECO:0000244|PDB:3MAO}.
STRAND 66 71 {ECO:0000244|PDB:3MAO}.
TURN 72 74 {ECO:0000244|PDB:3MAO}.
STRAND 77 82 {ECO:0000244|PDB:3MAO}.
STRAND 86 88 {ECO:0000244|PDB:3MAO}.
STRAND 93 96 {ECO:0000244|PDB:3MAO}.
HELIX 98 100 {ECO:0000244|PDB:3MAO}.
STRAND 101 105 {ECO:0000244|PDB:3MAO}.
SEQUENCE 116 AA; 12760 MW; 812B033BE02B7C0E CRC64;
MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE
HNRSEALKVS CGKCGNGLGH EFLNDGPKPG QSRFUIFSSS LKFVPKGKET SASQGH


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