MSRB9_ARATH
ID MSRB9_ARATH Reviewed; 143 AA.
AC Q84JT6; O49708; Q8LCW5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Peptide methionine sulfoxide reductase B9;
DE Short=AtMSRB9;
DE EC=1.8.4.12;
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase;
GN Name=MSRB9; OrderedLocusNames=At4g21850; ORFNames=T8O5.60;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17031545; DOI=10.1007/s11120-006-9097-1;
RA Rouhier N., Vieira Dos Santos C., Tarrago L., Rey P.;
RT "Plant methionine sulfoxide reductase A and B multigenic families.";
RL Photosyn. Res. 89:247-262(2006).
CC -!- FUNCTION: Catalyzes the reduction of methionine sulfoxide (MetSO) to
CC methionine in proteins. Plays a protective role against oxidative
CC stress by restoring activity to proteins that have been inactivated by
CC methionine oxidation. MSRB family specifically reduces the MetSO R-
CC enantiomer (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84JT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84JT6-2; Sequence=VSP_039513, VSP_039514;
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79140.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021890; CAA17152.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161556; CAB79140.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84511.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84512.1; -; Genomic_DNA.
DR EMBL; BT004230; AAO42245.1; -; mRNA.
DR EMBL; BT005691; AAO64111.1; -; mRNA.
DR EMBL; AY086368; AAM64435.1; -; mRNA.
DR PIR; T05467; T05467.
DR RefSeq; NP_567638.1; NM_118305.3. [Q84JT6-1]
DR RefSeq; NP_849418.1; NM_179087.1. [Q84JT6-2]
DR AlphaFoldDB; Q84JT6; -.
DR SMR; Q84JT6; -.
DR STRING; 3702.AT4G21850.1; -.
DR PaxDb; Q84JT6; -.
DR PRIDE; Q84JT6; -.
DR ProteomicsDB; 239014; -. [Q84JT6-1]
DR EnsemblPlants; AT4G21850.1; AT4G21850.1; AT4G21850. [Q84JT6-1]
DR EnsemblPlants; AT4G21850.2; AT4G21850.2; AT4G21850. [Q84JT6-2]
DR GeneID; 828273; -.
DR Gramene; AT4G21850.1; AT4G21850.1; AT4G21850. [Q84JT6-1]
DR Gramene; AT4G21850.2; AT4G21850.2; AT4G21850. [Q84JT6-2]
DR KEGG; ath:AT4G21850; -.
DR Araport; AT4G21850; -.
DR TAIR; locus:2141692; AT4G21850.
DR eggNOG; KOG0856; Eukaryota.
DR HOGENOM; CLU_031040_8_1_1; -.
DR InParanoid; Q84JT6; -.
DR OMA; ATNERHC; -.
DR PhylomeDB; Q84JT6; -.
DR PRO; PR:Q84JT6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84JT6; baseline and differential.
DR Genevisible; Q84JT6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR PANTHER; PTHR46081; PTHR46081; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Disulfide bond; Electron transport;
KW Metal-binding; Oxidoreductase; Redox-active center; Reference proteome;
KW Transport; Zinc.
FT CHAIN 1..143
FT /note="Peptide methionine sulfoxide reductase B9"
FT /id="PRO_0000395527"
FT DOMAIN 19..140
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 129
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT DISULFID 76..129
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT VAR_SEQ 93..121
FT /note="PEAGGRRMEITCAACDGHLGHVVKGEGFP -> VIDIFFFFSFMTHNYFSDK
FT DCCIKQVLCL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039513"
FT VAR_SEQ 122..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039514"
FT CONFLICT 6
FT /note="T -> R (in Ref. 4; AAM64435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 143 AA; 15412 MW; 6BF25765DF8F854E CRC64;
MPTSATAVAP STGSVQKKDQ DWRAILSPEQ FRVLREKGTE NRGKGEYTKL FDDGIYSCAG
CATPLYKSTT KFDSGCGWPS FFDAIPGAIK QTPEAGGRRM EITCAACDGH LGHVVKGEGF
PTATDERHCV NSVSLKFSEI SSQ
