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Methionine-R-sulfoxide reductase B1 (EC 1.8.4.12) (Selenoprotein R)

 MSRB_DROME              Reviewed;         208 AA.
Q8INK9; A4V2P1; B7Z0V7; Q53XF3; Q8IGC0; Q8IGS8; Q8INK8; Q8INL0;
Q8STJ0; Q9VGV4;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 142.
RecName: Full=Methionine-R-sulfoxide reductase B1;
EC=1.8.4.12 {ECO:0000269|PubMed:11929995, ECO:0000269|PubMed:24212093};
AltName: Full=Selenoprotein R;
Name=SelR; Synonyms=MsrB, MsrB1; ORFNames=CG6584;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|EMBL:AAN13491.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), ENZYME ACTIVITY, ACTIVE SITE,
AND ZINC-BINDING.
PubMed=11929995; DOI=10.1073/pnas.072603099;
Kryukov G.V., Kumar R.A., Koc A., Sun Z., Gladyshev V.N.;
"Selenoprotein R is a zinc-containing stereo-specific methionine
sulfoxide reductase.";
Proc. Natl. Acad. Sci. U.S.A. 99:4245-4250(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; G AND H).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
ZINC-BINDING, DISULFIDE BOND, MASS SPECTROMETRY, AND MUTAGENESIS OF
CYS-93; CYS-96; CYS-111; CYS-154; CYS-157; HIS-160; HIS-163; CYS-177
AND SER-180.
PubMed=12145281; DOI=10.1074/jbc.M203496200;
Kumar R.A., Koc A., Cerny R.L., Gladyshev V.N.;
"Reaction mechanism, evolutionary analysis, and role of zinc in
Drosophila methionine-R-sulfoxide reductase.";
J. Biol. Chem. 277:37527-37535(2002).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=24212093; DOI=10.1038/ncb2871;
Hung R.J., Spaeth C.S., Yesilyurt H.G., Terman J.R.;
"SelR reverses Mical-mediated oxidation of actin to regulate F-actin
dynamics.";
Nat. Cell Biol. 15:1445-1454(2013).
-!- 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 residues.
Acts as a regulator of actin assembly by reducing methionine (R)-
sulfoxide mediated by Mical on actin thereby promoting filament
repolymerization. {ECO:0000269|PubMed:24212093}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
{ECO:0000269|PubMed:11929995, ECO:0000269|PubMed:24212093}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11929995};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11929995};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}.
Nucleus {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9JLC3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=E {ECO:0000303|PubMed:12537572};
IsoId=Q8INK9-1; Sequence=Displayed;
Note=No experimental confirmation available.
{ECO:0000303|PubMed:12537572};
Name=A {ECO:0000269|PubMed:11929995}; Synonyms=I;
IsoId=Q8INK9-2; Sequence=VSP_008300, VSP_008301;
Name=B {ECO:0000303|PubMed:12537572};
IsoId=Q8INK9-3; Sequence=VSP_008300;
Note=No experimental confirmation available.
{ECO:0000303|PubMed:12537572};
Name=C {ECO:0000303|PubMed:12537572};
IsoId=Q8INK9-4; Sequence=VSP_008301;
Note=No experimental confirmation available.
{ECO:0000303|PubMed:12537572};
Name=G;
IsoId=Q8INK9-6; Sequence=VSP_008300, VSP_035868;
Note=No experimental confirmation available.;
Name=H;
IsoId=Q8INK9-7; Sequence=VSP_008300, VSP_035869;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Present in the embryonic nervous system (brain
and cord) in neuronal cell bodies, along axons. Also present in
embryonic muscles in motor axons. Localizes to growing bristle
tips where it is distributed in small puntae. Present at and at
sites of actin localization. {ECO:0000269|PubMed:24212093}.
-!- MASS SPECTROMETRY: Mass=19439.6; Method=Electrospray; Range=2-156
(Q8INK9-2); Evidence={ECO:0000269|PubMed:12145281};
-!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF486578; AAM10931.1; -; mRNA.
EMBL; AE014297; AAF54569.1; -; Genomic_DNA.
EMBL; AE014297; AAN13490.1; -; Genomic_DNA.
EMBL; AE014297; AAN13491.1; -; Genomic_DNA.
EMBL; AE014297; AAN13492.1; -; Genomic_DNA.
EMBL; AE014297; AAN13493.2; -; Genomic_DNA.
EMBL; AE014297; AAS65138.1; -; Genomic_DNA.
EMBL; AE014297; ACL83495.1; -; Genomic_DNA.
EMBL; AY070627; AAL48098.1; -; mRNA.
EMBL; BT001621; AAN71376.1; -; mRNA.
EMBL; BT001854; AAN71615.1; -; mRNA.
EMBL; BT011487; AAR99145.1; -; mRNA.
RefSeq; NP_001138036.1; NM_001144564.3. [Q8INK9-6]
RefSeq; NP_650030.1; NM_141773.4. [Q8INK9-2]
RefSeq; NP_731522.1; NM_169368.3. [Q8INK9-4]
RefSeq; NP_731523.1; NM_169369.3. [Q8INK9-1]
RefSeq; NP_731524.1; NM_169370.4. [Q8INK9-3]
RefSeq; NP_731525.2; NM_169371.4. [Q8INK9-7]
RefSeq; NP_996195.1; NM_206473.4. [Q8INK9-2]
UniGene; Dm.1144; -.
ProteinModelPortal; Q8INK9; -.
BioGrid; 66453; 3.
DIP; DIP-61754N; -.
IntAct; Q8INK9; 2.
STRING; 7227.FBpp0081772; -.
PaxDb; Q8INK9; -.
PRIDE; Q8INK9; -.
EnsemblMetazoa; FBtr0082291; FBpp0081768; FBgn0267376. [Q8INK9-3]
EnsemblMetazoa; FBtr0082292; FBpp0081769; FBgn0267376. [Q8INK9-2]
EnsemblMetazoa; FBtr0082294; FBpp0081771; FBgn0267376. [Q8INK9-4]
EnsemblMetazoa; FBtr0082295; FBpp0081772; FBgn0267376. [Q8INK9-1]
EnsemblMetazoa; FBtr0273345; FBpp0271853; FBgn0267376. [Q8INK9-6]
EnsemblMetazoa; FBtr0273346; FBpp0271854; FBgn0267376. [Q8INK9-7]
EnsemblMetazoa; FBtr0273347; FBpp0271855; FBgn0267376. [Q8INK9-2]
GeneID; 41309; -.
KEGG; dme:Dmel_CG6584; -.
CTD; 41309; -.
FlyBase; FBgn0267376; SelR.
eggNOG; KOG0856; Eukaryota.
eggNOG; COG0229; LUCA.
GeneTree; ENSGT00510000046802; -.
InParanoid; Q8INK9; -.
KO; K07305; -.
OrthoDB; EOG091G043K; -.
PhylomeDB; Q8INK9; -.
GenomeRNAi; 41309; -.
PRO; PR:Q8INK9; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0267376; -.
ExpressionAtlas; Q8INK9; baseline and differential.
Genevisible; Q8INK9; DM.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; HDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:FlyBase.
GO; GO:0008270; F:zinc ion binding; IDA:FlyBase.
GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
GO; GO:0030041; P:actin filament polymerization; IGI:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
GO; GO:0030091; P:protein repair; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:FlyBase.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like_sf.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
TIGRFAMs; TIGR00357; TIGR00357; 1.
PROSITE; PS51790; MSRB; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Disulfide bond; Metal-binding; Nucleus; Oxidoreductase;
Reference proteome; Zinc.
INIT_MET 1 1 Removed.
CHAIN 2 208 Methionine-R-sulfoxide reductase B1.
/FTId=PRO_0000140323.
DOMAIN 54 188 MsrB. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
ACT_SITE 177 177 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01126,
ECO:0000269|PubMed:11929995}.
METAL 93 93 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126,
ECO:0000269|PubMed:11929995}.
METAL 96 96 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126,
ECO:0000269|PubMed:11929995}.
METAL 154 154 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126,
ECO:0000269|PubMed:11929995}.
METAL 157 157 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01126,
ECO:0000269|PubMed:11929995}.
DISULFID 111 177 {ECO:0000269|PubMed:12145281}.
VAR_SEQ 1 42 Missing (in isoform A, isoform B, isoform
G and isoform H).
{ECO:0000303|PubMed:11929995,
ECO:0000303|PubMed:12537569,
ECO:0000303|Ref.5}.
/FTId=VSP_008300.
VAR_SEQ 134 144 Missing (in isoform A and isoform C).
{ECO:0000303|PubMed:11929995,
ECO:0000303|PubMed:12537569}.
/FTId=VSP_008301.
VAR_SEQ 135 208 GGNILLLIAHPERIRTEVRCARCNAHMGHVFEDGPKPTRKR
YCINSASIEFVNADPATSSPPVATPTAAPIAQQ -> VVIS
KTLGMVRTEVRCSRCSAHMGHVFDDGPPPKHRRFCINSASI
DFVKSATPSKADPSTASSKK (in isoform G).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_035868.
VAR_SEQ 136 208 GNILLLIAHPERIRTEVRCARCNAHMGHVFEDGPKPTRKRY
CINSASIEFVNADPATSSPPVATPTAAPIAQQ -> MVRTE
VRCSRCSAHMGHVFDDGPPPKHRRFCINSASIDFVKSATPS
KADPSTASSKK (in isoform H).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_035869.
MUTAGEN 93 93 C->G: Loss of activity and zinc binding.
{ECO:0000269|PubMed:12145281}.
MUTAGEN 96 96 C->G,S: Loss of activity and zinc
binding. {ECO:0000269|PubMed:12145281}.
MUTAGEN 111 111 C->S: Thioredoxin-dependent activity
reduced, but no change in DTT-dependent
activity. {ECO:0000269|PubMed:12145281}.
MUTAGEN 154 154 C->G,S: Loss of activity and zinc
binding. {ECO:0000269|PubMed:12145281}.
MUTAGEN 157 157 C->S: Loss of activity and zinc binding.
{ECO:0000269|PubMed:12145281}.
MUTAGEN 160 160 H->G: Loss of thioredoxin-dependent
activity, 81% DTT-dependent activity.
{ECO:0000269|PubMed:12145281}.
MUTAGEN 163 163 H->G: Loss of thioredoxin-dependent
activity, 80% DTT-dependent activity.
{ECO:0000269|PubMed:12145281}.
MUTAGEN 177 177 C->K,S: Loss of activity.
{ECO:0000269|PubMed:12145281}.
MUTAGEN 180 180 S->G: Loss of thioredoxin-dependent
activity, 85% DTT-dependent activity.
{ECO:0000269|PubMed:12145281}.
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


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