ID   F5H6G9_HUMAN            Unreviewed;       160 AA.
AC   F5H6G9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   16-JAN-2019, entry version 52.
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=MSRB3 {ECO:0000313|Ensembl:ENSP00000437623};
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:ENSP00000437623, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000437623, 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:ENSP00000437623}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) 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; F5H6G9; -.
DR   jPOST; F5H6G9; -.
DR   PeptideAtlas; F5H6G9; -.
DR   PRIDE; F5H6G9; -.
DR   Ensembl; ENST00000540804; ENSP00000437623; ENSG00000174099.
DR   UCSC; uc058qlg.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; F5H6G9; 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:F5H6G9,
KW   ECO:0000213|MaxQB:F5H6G9, ECO:0000213|PeptideAtlas:F5H6G9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|RuleBase:RU365044};
KW   Zinc {ECO:0000256|RuleBase:RU365044}.
FT   SIGNAL        1     30       {ECO:0000256|RuleBase:RU365044}.
FT   CHAIN        31    160       Peptide-methionine (R)-S-oxide reductase.
FT                                {ECO:0000256|RuleBase:RU365044}.
FT                                /FTId=PRO_5015797399.
FT   DOMAIN       47    160       MsrB. {ECO:0000259|PROSITE:PS51790}.
SQ   SEQUENCE   160 AA;  17810 MW;  0A109BA1A25FA71C CRC64;
     MSPRRTLPRP LSLCLSLCLC LCLAAALGSA QSGSCRDKKN CKVVFSQQEL RKRLTPLQYH
     VTQEKGTESA FEGEYTHHKD PGIYKCVVCG TPLFKSETKF DSGSGWPSFH DVINSEAITF
     TDDFSYGMHR VETSCSQVSS SFLKTQYIAF RTPGCAKYSN
//