MSRB1_MOUSE
ID MSRB1_MOUSE Reviewed; 116 AA.
AC Q9JLC3; Q545U8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Methionine-R-sulfoxide reductase B1;
DE Short=MsrB1;
DE EC=1.8.4.12 {ECO:0000269|PubMed:11929995, ECO:0000269|PubMed:23911929};
DE EC=1.8.4.14 {ECO:0000269|PubMed:11929995, ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:20605785, ECO:0000269|PubMed:23911929};
DE AltName: Full=Selenoprotein R;
DE Short=SelR;
DE AltName: Full=Selenoprotein X;
DE Short=SelX;
GN Name=Msrb1; Synonyms=Sepr, Sepx1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10567350; DOI=10.1074/jbc.274.48.33888;
RA Kryukov G.V., Kryukov V.M., Gladyshev V.N.;
RT "New mammalian selenocysteine-containing proteins identified with an
RT algorithm that searches for selenocysteine insertion sequence elements.";
RL J. Biol. Chem. 274:33888-33897(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=14699060; DOI=10.1091/mbc.e03-08-0629;
RA Kim H.-Y., Gladyshev V.N.;
RT "Methionine sulfoxide reduction in mammals: characterization of methionine-
RT R-sulfoxide reductases.";
RL Mol. Biol. Cell 15:1055-1064(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
RA Gladyshev V.N.;
RT "MsrB1 and MICALs regulate actin assembly and macrophage function via
RT reversible stereoselective methionine oxidation.";
RL Mol. Cell 51:397-404(2013).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=19636847; DOI=10.1007/s12104-007-9039-7;
RA Sal L.S., Aachmann F.L., Kim H.Y., Gladyshev V.N., Dikiy A.;
RT "NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide
RT reductase B1 from Mus musculus.";
RL Biomol. NMR. Assign. 1:131-133(2007).
RN [8] {ECO:0007744|PDB:2KV1}
RP STRUCTURE BY NMR OF MUTANT SEL-95 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND MUTAGENESIS OF SEC-95.
RX PubMed=20605785; DOI=10.1074/jbc.m110.132308;
RA Aachmann F.L., Sal L.S., Kim H.Y., Marino S.M., Gladyshev V.N., Dikiy A.;
RT "Insights into function, catalytic mechanism, and fold evolution of
RT selenoprotein methionine sulfoxide reductase B1 through structural
RT analysis.";
RL J. Biol. Chem. 285:33315-33323(2010).
CC -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces
CC methionine (R)-sulfoxide back to methionine (PubMed:11929995,
CC PubMed:14699060, PubMed:23911929, PubMed:20605785). While in many
CC cases, 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 residue (PubMed:14699060,
CC PubMed:20605785). Acts as a regulator of actin assembly by reducing
CC methionine (R)-sulfoxide mediated by MICALs (MICAL1, MICAL2 or MICAL3)
CC on actin, thereby promoting filament repolymerization
CC (PubMed:23911929). Plays a role in innate immunity by reducing oxidized
CC actin, leading to actin repolymerization in macrophages
CC (PubMed:23911929). {ECO:0000269|PubMed:11929995,
CC ECO:0000269|PubMed:14699060, ECO:0000269|PubMed:20605785,
CC ECO:0000269|PubMed:23911929}.
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:23911929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58773; EC=1.8.4.14;
CC Evidence={ECO:0000269|PubMed:11929995, ECO:0000269|PubMed:14699060,
CC ECO:0000269|PubMed:20605785, ECO:0000269|PubMed:23911929};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:14699060};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14699060,
CC ECO:0000269|PubMed:20605785};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14699060}. Nucleus
CC {ECO:0000269|PubMed:14699060}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23911929}.
CC -!- PTM: Truncated MSRB1/SEPX1 proteins produced by failed UGA/Sec decoding
CC are ubiquitinated by the CRL2(FEM1C) E3 ubiquitin-protein ligase
CC complex. {ECO:0000250|UniProtKB:Q9NZV6}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AF195142; AAF13697.1; -; mRNA.
DR EMBL; AK002339; BAC55245.1; -; mRNA.
DR EMBL; AK002652; BAE43148.1; -; mRNA.
DR EMBL; AK003112; BAC55248.1; -; mRNA.
DR EMBL; AK003624; BAC55249.1; -; mRNA.
DR EMBL; BC090646; AAH90646.1; -; mRNA.
DR CCDS; CCDS28495.1; -.
DR RefSeq; NP_001333597.1; NM_001346668.1.
DR RefSeq; NP_038787.1; NM_013759.3.
DR PDB; 2KV1; NMR; -; A=1-116.
DR PDBsum; 2KV1; -.
DR BMRB; Q9JLC3; -.
DR SMR; Q9JLC3; -.
DR BioGRID; 205170; 1.
DR IntAct; Q9JLC3; 1.
DR STRING; 10090.ENSMUSP00000110917; -.
DR iPTMnet; Q9JLC3; -.
DR PhosphoSitePlus; Q9JLC3; -.
DR MaxQB; Q9JLC3; -.
DR PaxDb; Q9JLC3; -.
DR PRIDE; Q9JLC3; -.
DR ProteomicsDB; 291525; -.
DR Antibodypedia; 58024; 128 antibodies from 24 providers.
DR DNASU; 27361; -.
DR Ensembl; ENSMUST00000101800; ENSMUSP00000099300; ENSMUSG00000075705.
DR Ensembl; ENSMUST00000115262; ENSMUSP00000110917; ENSMUSG00000075705.
DR GeneID; 27361; -.
DR KEGG; mmu:27361; -.
DR UCSC; uc008ayh.1; mouse.
DR CTD; 51734; -.
DR MGI; MGI:1351642; Msrb1.
DR VEuPathDB; HostDB:ENSMUSG00000075705; -.
DR eggNOG; KOG0856; Eukaryota.
DR GeneTree; ENSGT00510000047678; -.
DR HOGENOM; CLU_147472_1_0_1; -.
DR InParanoid; Q9JLC3; -.
DR OMA; NDGPAKG; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q9JLC3; -.
DR TreeFam; TF329147; -.
DR BRENDA; 1.8.4.12; 3474.
DR Reactome; R-MMU-5676934; Protein repair.
DR BioGRID-ORCS; 27361; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Msrb1; mouse.
DR EvolutionaryTrace; Q9JLC3; -.
DR PRO; PR:Q9JLC3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JLC3; protein.
DR Bgee; ENSMUSG00000075705; Expressed in granulocyte and 257 other tissues.
DR Genevisible; Q9JLC3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; IDA:MGI.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC-UCL.
DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0030091; P:protein repair; IDA:HGNC-UCL.
DR DisProt; DP02258; -.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Selenocysteine;
KW Ubl conjugation; Zinc.
FT CHAIN 1..116
FT /note="Methionine-R-sulfoxide reductase B1"
FT /id="PRO_0000140322"
FT DOMAIN 1..106
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:20605785, ECO:0000312|PDB:2KV1"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:20605785, ECO:0000312|PDB:2KV1"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:20605785, ECO:0000312|PDB:2KV1"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126,
FT ECO:0000269|PubMed:20605785, ECO:0000312|PDB:2KV1"
FT NON_STD 95
FT /note="Selenocysteine"
FT /evidence="ECO:0000305|PubMed:10567350"
FT MUTAGEN 95
FT /note="U->C: Optimum pH 7.5."
FT /evidence="ECO:0000269|PubMed:20605785"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2KV1"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2KV1"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2KV1"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:2KV1"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2KV1"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2KV1"
SQ SEQUENCE 116 AA; 12788 MW; 7DE4E5EE86CAA333 CRC64;
MSFCSFFGGE VFQNHFEPGV YVCAKCSYEL FSSHSKYAHS SPWPAFTETI HPDSVTKCPE
KNRPEALKVS CGKCGNGLGH EFLNDGPKRG QSRFUIFSSS LKFVPKGKEA AASQGH
