ID   H0YFW5_HUMAN            Unreviewed;       174 AA.
AC   H0YFW5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   16-JAN-2019, entry version 45.
DE   RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|RuleBase:RU365044};
DE            EC=1.8.4.12 {ECO:0000256|RuleBase:RU365044};
DE   Flags: Fragment;
GN   Name=MSRB3 {ECO:0000313|Ensembl:ENSP00000440722};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000440722, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000440722, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RG   Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A., null.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000440722}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2012) 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-
CC       translational modification that takes place on specific residues.
CC       {ECO:0000256|RuleBase:RU365044}.
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-
CC         COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:45764, 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.
CC       {ECO:0000256|RuleBase:RU365044};
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|RuleBase:RU365044}.
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DR   EMBL; AC025419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; H0YFW5; -.
DR   jPOST; H0YFW5; -.
DR   MaxQB; H0YFW5; -.
DR   PeptideAtlas; H0YFW5; -.
DR   PRIDE; H0YFW5; -.
DR   Ensembl; ENST00000541189; ENSP00000440722; ENSG00000174099.
DR   UCSC; uc058qlh.1; human.
DR   EuPathDB; HostDB:ENSG00000174099.10; -.
DR   HGNC; HGNC:27375; MSRB3.
DR   OpenTargets; ENSG00000174099; -.
DR   eggNOG; KOG0856; Eukaryota.
DR   eggNOG; COG0229; LUCA.
DR   GeneTree; ENSGT00940000155240; -.
DR   ChiTaRS; MSRB3; human.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000174099; Expressed in 199 organ(s), highest expression level in myometrium.
DR   ExpressionAtlas; H0YFW5; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR028427; Met_Sox_Rdtase.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   PANTHER; PTHR10173; PTHR10173; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Metal-binding {ECO:0000256|RuleBase:RU365044};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU365044};
KW   Proteomics identification {ECO:0000213|EPD:H0YFW5,
KW   ECO:0000213|MaxQB:H0YFW5, ECO:0000213|PeptideAtlas:H0YFW5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU365044}.
FT   SIGNAL        1     39       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        40    174       Peptide-methionine (R)-S-oxide reductase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003546460.
FT   DOMAIN       56    174       MsrB. {ECO:0000259|PROSITE:PS51790}.
FT   NON_TER       1      1       {ECO:0000313|Ensembl:ENSP00000440722}.
SQ   SEQUENCE   174 AA;  19480 MW;  DF21B8D23E95DF18 CRC64;
     XRRRLPGLSM SPRRTLPRPL SLCLSLCLCL CLAAALGSAQ SGSCRDKKNC KVVFSQQELR
     KRLTPLQYHV TQEKGTESAF EGEYTHHKDP GIYKCVVCGT PLFKSETKFD SGSGWPSFHD
     VINSEAITFT DDFSYGMHRV ETSCSQQEGP HQMLPLNLGF PGLQNCEPIN FYSF
//