MSRB_DROME
ID MSRB_DROME Reviewed; 208 AA.
AC Q8INK9; A4V2P1; B7Z0V7; Q53XF3; Q8IGC0; Q8IGS8; Q8INK8; Q8INL0; Q8STJ0;
AC Q9VGV4;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Methionine-R-sulfoxide reductase B1;
DE EC=1.8.4.12 {ECO:0000269|PubMed:11929995, ECO:0000269|PubMed:24212093};
DE AltName: Full=Selenoprotein R;
GN Name=SelR; Synonyms=MsrB, MsrB1; ORFNames=CG6584;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAN13491.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), ENZYME ACTIVITY, ACTIVE SITE, AND
RP ZINC-BINDING.
RX PubMed=11929995; DOI=10.1073/pnas.072603099;
RA Kryukov G.V., Kumar R.A., Koc A., Sun Z., Gladyshev V.N.;
RT "Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide
RT reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4245-4250(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; G AND H).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ZINC-BINDING, DISULFIDE BOND, MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-93;
RP CYS-96; CYS-111; CYS-154; CYS-157; HIS-160; HIS-163; CYS-177 AND SER-180.
RX PubMed=12145281; DOI=10.1074/jbc.m203496200;
RA Kumar R.A., Koc A., Cerny R.L., Gladyshev V.N.;
RT "Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila
RT methionine-R-sulfoxide reductase.";
RL J. Biol. Chem. 277:37527-37535(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=24212093; DOI=10.1038/ncb2871;
RA Hung R.J., Spaeth C.S., Yesilyurt H.G., Terman J.R.;
RT "SelR reverses Mical-mediated oxidation of actin to regulate F-actin
RT dynamics.";
RL Nat. Cell Biol. 15:1445-1454(2013).
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 residues. Acts as a regulator
CC of actin assembly by reducing methionine (R)-sulfoxide mediated by
CC Mical on actin thereby promoting filament repolymerization.
CC {ECO:0000269|PubMed:24212093}.
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:0000269|PubMed:11929995, ECO:0000269|PubMed:24212093};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11929995};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11929995};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9JLC3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=E {ECO:0000303|PubMed:12537572};
CC IsoId=Q8INK9-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:11929995}; Synonyms=I;
CC IsoId=Q8INK9-2; Sequence=VSP_008300, VSP_008301;
CC Name=B {ECO:0000303|PubMed:12537572};
CC IsoId=Q8INK9-3; Sequence=VSP_008300;
CC Name=C {ECO:0000303|PubMed:12537572};
CC IsoId=Q8INK9-4; Sequence=VSP_008301;
CC Name=G;
CC IsoId=Q8INK9-6; Sequence=VSP_008300, VSP_035868;
CC Name=H;
CC IsoId=Q8INK9-7; Sequence=VSP_008300, VSP_035869;
CC -!- TISSUE SPECIFICITY: Present in the embryonic nervous system (brain and
CC cord) in neuronal cell bodies, along axons. Also present in embryonic
CC muscles in motor axons. Localizes to growing bristle tips where it is
CC distributed in small puntae. Present at and at sites of actin
CC localization. {ECO:0000269|PubMed:24212093}.
CC -!- MASS SPECTROMETRY: [Isoform A]: Mass=19439.6; Method=Electrospray;
CC Note=The measured range is 1-155.;
CC Evidence={ECO:0000269|PubMed:12145281};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AF486578; AAM10931.1; -; mRNA.
DR EMBL; AE014297; AAF54569.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13490.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13491.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13492.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13493.2; -; Genomic_DNA.
DR EMBL; AE014297; AAS65138.1; -; Genomic_DNA.
DR EMBL; AE014297; ACL83495.1; -; Genomic_DNA.
DR EMBL; AY070627; AAL48098.1; -; mRNA.
DR EMBL; BT001621; AAN71376.1; -; mRNA.
DR EMBL; BT001854; AAN71615.1; -; mRNA.
DR EMBL; BT011487; AAR99145.1; -; mRNA.
DR RefSeq; NP_001138036.1; NM_001144564.3. [Q8INK9-6]
DR RefSeq; NP_650030.1; NM_141773.4. [Q8INK9-2]
DR RefSeq; NP_731522.1; NM_169368.3. [Q8INK9-4]
DR RefSeq; NP_731523.1; NM_169369.3. [Q8INK9-1]
DR RefSeq; NP_731524.1; NM_169370.4. [Q8INK9-3]
DR RefSeq; NP_731525.2; NM_169371.4. [Q8INK9-7]
DR RefSeq; NP_996195.1; NM_206473.4. [Q8INK9-2]
DR AlphaFoldDB; Q8INK9; -.
DR SMR; Q8INK9; -.
DR BioGRID; 66453; 3.
DR DIP; DIP-61754N; -.
DR IntAct; Q8INK9; 3.
DR STRING; 7227.FBpp0081772; -.
DR PaxDb; Q8INK9; -.
DR DNASU; 41309; -.
DR EnsemblMetazoa; FBtr0082291; FBpp0081768; FBgn0267376. [Q8INK9-3]
DR EnsemblMetazoa; FBtr0082292; FBpp0081769; FBgn0267376. [Q8INK9-2]
DR EnsemblMetazoa; FBtr0082294; FBpp0081771; FBgn0267376. [Q8INK9-4]
DR EnsemblMetazoa; FBtr0082295; FBpp0081772; FBgn0267376. [Q8INK9-1]
DR EnsemblMetazoa; FBtr0273345; FBpp0271853; FBgn0267376. [Q8INK9-6]
DR EnsemblMetazoa; FBtr0273346; FBpp0271854; FBgn0267376. [Q8INK9-7]
DR EnsemblMetazoa; FBtr0273347; FBpp0271855; FBgn0267376. [Q8INK9-2]
DR GeneID; 41309; -.
DR KEGG; dme:Dmel_CG6584; -.
DR CTD; 41309; -.
DR FlyBase; FBgn0267376; SelR.
DR VEuPathDB; VectorBase:FBgn0267376; -.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00940000155240; -.
DR InParanoid; Q8INK9; -.
DR PhylomeDB; Q8INK9; -.
DR BRENDA; 1.8.4.12; 1994.
DR Reactome; R-DME-5676934; Protein repair.
DR BioGRID-ORCS; 41309; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41309; -.
DR PRO; PR:Q8INK9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0267376; Expressed in adult Malpighian tubule (Drosophila) and 39 other tissues.
DR ExpressionAtlas; Q8INK9; baseline and differential.
DR Genevisible; Q8INK9; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030041; P:actin filament polymerization; IGI:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:FlyBase.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
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 Alternative splicing; Cytoplasm; Cytoskeleton; Disulfide bond;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..208
FT /note="Methionine-R-sulfoxide reductase B1"
FT /id="PRO_0000140323"
FT DOMAIN 54..188
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:11929995"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:11929995"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:11929995"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:11929995"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:11929995"
FT DISULFID 111..177
FT /evidence="ECO:0000269|PubMed:12145281"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform A, isoform B, isoform G and
FT isoform H)"
FT /evidence="ECO:0000303|PubMed:11929995,
FT ECO:0000303|PubMed:12537569, ECO:0000303|Ref.5"
FT /id="VSP_008300"
FT VAR_SEQ 134..144
FT /note="Missing (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:11929995,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_008301"
FT VAR_SEQ 135..208
FT /note="GGNILLLIAHPERIRTEVRCARCNAHMGHVFEDGPKPTRKRYCINSASIEFV
FT NADPATSSPPVATPTAAPIAQQ -> VVISKTLGMVRTEVRCSRCSAHMGHVFDDGPPP
FT KHRRFCINSASIDFVKSATPSKADPSTASSKK (in isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_035868"
FT VAR_SEQ 136..208
FT /note="GNILLLIAHPERIRTEVRCARCNAHMGHVFEDGPKPTRKRYCINSASIEFVN
FT ADPATSSPPVATPTAAPIAQQ -> MVRTEVRCSRCSAHMGHVFDDGPPPKHRRFCINS
FT ASIDFVKSATPSKADPSTASSKK (in isoform H)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_035869"
FT MUTAGEN 93
FT /note="C->G: Loss of activity and zinc binding."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 96
FT /note="C->G,S: Loss of activity and zinc binding."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 111
FT /note="C->S: Thioredoxin-dependent activity reduced, but no
FT change in DTT-dependent activity."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 154
FT /note="C->G,S: Loss of activity and zinc binding."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 157
FT /note="C->S: Loss of activity and zinc binding."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 160
FT /note="H->G: Loss of thioredoxin-dependent activity, 81%
FT DTT-dependent activity."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 163
FT /note="H->G: Loss of thioredoxin-dependent activity, 80%
FT DTT-dependent activity."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 177
FT /note="C->K,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12145281"
FT MUTAGEN 180
FT /note="S->G: Loss of thioredoxin-dependent activity, 85%
FT DTT-dependent activity."
FT /evidence="ECO:0000269|PubMed:12145281"
SQ SEQUENCE 208 AA; 23299 MW; A8193586F60C1DCF CRC64;
MFALSARHAL RRTRIFAIPR FFADSRQDSD NPDKRYSGPA ATMDNKSEKV TVNKEELRKR
LTPVQYQVTQ EAGTERPFTG CYNKHYEKGV YQCIVCHQDL FSSETKYDSG CGWPAFNDVL
DKGKVTLHRD ASIPGGNILL LIAHPERIRT EVRCARCNAH MGHVFEDGPK PTRKRYCINS
ASIEFVNADP ATSSPPVATP TAAPIAQQ
