MSRB3_MOUSE
ID MSRB3_MOUSE Reviewed; 253 AA.
AC Q8BU85;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Methionine-R-sulfoxide reductase B3, mitochondrial;
DE Short=MsrB3;
DE EC=1.8.4.12 {ECO:0000250|UniProtKB:Q9JLC3};
DE EC=1.8.4.14 {ECO:0000250|UniProtKB:Q9JLC3};
DE Flags: Precursor;
GN Name=Msrb3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-253.
RC STRAIN=C57BL/6J; TISSUE=Lung, and Urinary bladder;
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] OF 48-253.
RC TISSUE=Olfactory epithelium;
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 IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=15249228; DOI=10.1016/j.bbrc.2004.06.078;
RA Kim H.Y., Gladyshev V.N.;
RT "Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide
RT reductase.";
RL Biochem. Biophys. Res. Commun. 320:1277-1283(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21185009; DOI=10.1016/j.ajhg.2010.11.010;
RA Ahmed Z.M., Yousaf R., Lee B.C., Khan S.N., Lee S., Lee K., Husnain T.,
RA Rehman A.U., Bonneux S., Ansar M., Ahmad W., Leal S.M., Gladyshev V.N.,
RA Belyantseva I.A., Van Camp G., Riazuddin S., Friedman T.B., Riazuddin S.;
RT "Functional null mutations of MSRB3 encoding methionine sulfoxide reductase
RT are associated with human deafness DFNB74.";
RL Am. J. Hum. Genet. 88:19-29(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the reduction of free and protein-bound methionine
CC sulfoxide to methionine. {ECO:0000250|UniProtKB:Q8IXL7}.
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:0000250|UniProtKB:Q9JLC3};
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:0000250|UniProtKB:Q9JLC3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:15249228}. Note=Not detected in the mitochondrion.
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in the sensory epithelia
CC of the organ of Corti and vestibular end organs as early as P2 up to
CC adulthood (at protein level). In the organ of Corti, present in inner
CC and outer hair cells and, to a lesser extent, in supporting cells (at
CC protein level). In hair cells, distributed throughout the cell body.
CC Barely detectable level in stereocilia. Also observed in spiral
CC ganglion neurons, but not in the stria vascularis. In the vestibular
CC end organs, found throughout the sensory epithelium, but more intense
CC expression in hair cells than in supporting cells (at protein level).
CC In vestibular hair cells, present within cell bodies and to a lesser
CC extent in kinocilia. Barely detectable in stereocilia.
CC {ECO:0000269|PubMed:21185009}.
CC -!- DEVELOPMENTAL STAGE: Expressed in temporal bones at 15 dpc through
CC postnatal 30, levels decrease thereafter, but is still present in the
CC inner ear at P180.
CC -!- MISCELLANEOUS: Contains a signal peptide followed by a mitochondrial
CC transit peptide within a single transcript. However, the protein is
CC detected exclusively within the endoplasmic reticulum. This contasts
CC with other species, including Homo sapiens, where the signal and
CC transit peptides are encoded on 2 mutually exclusive exons
CC (PubMed:15249228), and where alternative splicing leads to the
CC synthesis of either the endoplasmic reticulum resident form or the
CC mitochondrial form. {ECO:0000305|PubMed:15249228}.
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH96447.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC39776.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE23258.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC138388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK086975; BAC39776.1; ALT_INIT; mRNA.
DR EMBL; AK137163; BAE23258.1; ALT_INIT; mRNA.
DR EMBL; BC096447; AAH96447.1; ALT_INIT; mRNA.
DR RefSeq; NP_796066.1; NM_177092.4.
DR RefSeq; XP_006513827.1; XM_006513764.3.
DR AlphaFoldDB; Q8BU85; -.
DR SMR; Q8BU85; -.
DR IntAct; Q8BU85; 1.
DR MINT; Q8BU85; -.
DR STRING; 10090.ENSMUSP00000089781; -.
DR iPTMnet; Q8BU85; -.
DR PhosphoSitePlus; Q8BU85; -.
DR jPOST; Q8BU85; -.
DR MaxQB; Q8BU85; -.
DR PaxDb; Q8BU85; -.
DR PeptideAtlas; Q8BU85; -.
DR PRIDE; Q8BU85; -.
DR ProteomicsDB; 286070; -.
DR DNASU; 320183; -.
DR GeneID; 320183; -.
DR KEGG; mmu:320183; -.
DR UCSC; uc007hfh.2; mouse.
DR CTD; 253827; -.
DR MGI; MGI:2443538; Msrb3.
DR eggNOG; KOG0856; Eukaryota.
DR InParanoid; Q8BU85; -.
DR OrthoDB; 1549489at2759; -.
DR PhylomeDB; Q8BU85; -.
DR TreeFam; TF329147; -.
DR BRENDA; 1.8.4.12; 3474.
DR Reactome; R-MMU-5676934; Protein repair.
DR BioGRID-ORCS; 320183; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Msrb3; mouse.
DR PRO; PR:Q8BU85; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BU85; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; ISS:HGNC-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:HGNC-UCL.
DR GO; GO:0030091; P:protein repair; ISS:HGNC-UCL.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR HAMAP; MF_01400; MsrB; 1.
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 Acetylation; Endoplasmic reticulum; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Signal; Zinc.
FT SIGNAL 1..56
FT /evidence="ECO:0000255"
FT CHAIN 57..253
FT /note="Methionine-R-sulfoxide reductase B3, mitochondrial"
FT /id="PRO_0000327241"
FT DOMAIN 107..229
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 227..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 250..253
FT /note="Endoplasmic reticulum retention signal"
FT ACT_SITE 218
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 253 AA; 26832 MW; 361264F3C605ADB5 CRC64;
MPPAAPSVAR SREGGGIGQR RLVFPKSARR TLPCPIALCL GLCLAAAAAT TTRASAAAFA
SAGDTTAMSA FNLLHLVTKS QPVAPRACGL PSGSCRDKKN CKVVFSQQEL RKRLTPLQYH
VTQEKGTESA FEGEYTHHKD PGIYKCVVCG TPLFKSETKF DSGSGWPAFH DVISSEAIEF
TDDFSYGMHR VETSCSQCGA HLGHIFDDGP RPTGKRYCIN SASLSFTPAD SSEAEGSGIK
ESGSPAAADR AEL
