MSRA_RAT
ID MSRA_RAT Reviewed; 233 AA.
AC Q923M1; A9LAT3; A9LAT4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Mitochondrial peptide methionine sulfoxide reductase;
DE EC=1.8.4.11 {ECO:0000250|UniProtKB:Q9D6Y7};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE AltName: Full=Protein-methionine-S-oxide reductase;
DE Short=PMSR;
DE Flags: Precursor;
GN Name=Msra;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11311146; DOI=10.1042/bj3550819;
RA Petropoulos I., Mary J., Perichon M., Friguet B.;
RT "Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and
RT down-regulation of gene expression and enzyme activity during aging.";
RL Biochem. J. 355:819-825(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-233 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 20-233 (ISOFORM 3), TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Smooth muscle;
RX PubMed=17907003; DOI=10.1080/10715760701642096;
RA Haenold R., Wassef R., Hansel A., Heinemann S.H., Hoshi T.;
RT "Identification of a new functional splice variant of the enzyme methionine
RT sulphoxide reductase A (MSRA) expressed in rat vascular smooth muscle
RT cells.";
RL Free Radic. Res. 41:1233-1245(2007).
RN [4]
RP PROTEIN SEQUENCE OF 28-47, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=12693988; DOI=10.1042/bj20030443;
RA Vougier S., Mary J., Friguet B.;
RT "Subcellular localization of methionine sulphoxide reductase A (MsrA):
RT evidence for mitochondrial and cytosolic isoforms in rat liver cells.";
RL Biochem. J. 373:531-537(2003).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC Evidence={ECO:0000250|UniProtKB:Q9D6Y7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, 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:58772; EC=1.8.4.11;
CC Evidence={ECO:0000250|UniProtKB:Q9D6Y7};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=mito-MSRA;
CC IsoId=Q923M1-1; Sequence=Displayed;
CC Name=2; Synonyms=MSRA2a;
CC IsoId=Q923M1-3; Sequence=VSP_041410;
CC Name=3; Synonyms=MSRA2b1, MSRA2b2;
CC IsoId=Q923M1-4; Sequence=VSP_041411, VSP_041412;
CC Name=4; Synonyms=cyto-MSRA;
CC IsoId=Q923M1-2; Sequence=VSP_041413;
CC -!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed.
CC {ECO:0000269|PubMed:17907003}.
CC -!- MISCELLANEOUS: [Isoform 1]: Mitochondrial.
CC -!- MISCELLANEOUS: [Isoform 2]: Mitochondrial. Enzymatically active.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Mitochondrial. No enzymatic activity.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Cytoplasmic. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AY005464; AAF99392.1; -; mRNA.
DR EMBL; BC087009; AAH87009.1; -; mRNA.
DR EMBL; DQ989019; ABL73891.1; -; mRNA.
DR EMBL; DQ989020; ABL73892.1; -; mRNA.
DR EMBL; DQ989021; ABL73893.1; -; mRNA.
DR RefSeq; NP_445759.1; NM_053307.2. [Q923M1-1]
DR RefSeq; XP_008768967.2; XM_008770745.2. [Q923M1-1]
DR AlphaFoldDB; Q923M1; -.
DR SMR; Q923M1; -.
DR STRING; 10116.ENSRNOP00000067242; -.
DR ChEMBL; CHEMBL3509605; -.
DR iPTMnet; Q923M1; -.
DR PhosphoSitePlus; Q923M1; -.
DR PRIDE; Q923M1; -.
DR Ensembl; ENSRNOT00000102126; ENSRNOP00000097940; ENSRNOG00000012440. [Q923M1-1]
DR GeneID; 29447; -.
DR KEGG; rno:29447; -.
DR UCSC; RGD:70979; rat. [Q923M1-1]
DR CTD; 4482; -.
DR RGD; 70979; Msra.
DR GeneTree; ENSGT00390000003823; -.
DR InParanoid; Q923M1; -.
DR OrthoDB; 1383773at2759; -.
DR BRENDA; 1.8.4.11; 5301.
DR Reactome; R-RNO-5676934; Protein repair.
DR PRO; PR:Q923M1; -.
DR Proteomes; UP000002494; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Mitochondrion; Oxidoreductase; Redox-active center;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 21..233
FT /note="Mitochondrial peptide methionine sulfoxide
FT reductase"
FT /id="PRO_0000138628"
FT ACT_SITE 72
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D6Y7"
FT MOD_RES 104
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D6Y7"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D6Y7"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D6Y7"
FT DISULFID 72..218
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT DISULFID 218..227
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT VAR_SEQ 1..46
FT /note="MLSASRRTLQLLSSSIPVRMMGDSSSKVISAEEALPGRTESIPVAA -> ME
FT QQPQA (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_041413"
FT VAR_SEQ 46
FT /note="A -> AALPTPSLSPNQKLNYFVWKEVPGKHSWP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17907003"
FT /id="VSP_041410"
FT VAR_SEQ 47..56
FT /note="KHHVSGNRTV -> SCHPKLHPSN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17907003"
FT /id="VSP_041411"
FT VAR_SEQ 57..233
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17907003"
FT /id="VSP_041412"
SQ SEQUENCE 233 AA; 25851 MW; 6F895BD4FEBCB18C CRC64;
MLSASRRTLQ LLSSSIPVRM MGDSSSKVIS AEEALPGRTE SIPVAAKHHV SGNRTVEPFP
EGTQMAVFGM GCFWGAERKF WLLKGVYSTQ VGFAGGYTRN PTYKEVCSEK TGHAEVVRVV
YRPEHVSFEE LLKVFWENHD PTQGMRQGND CGTQYRSAVY PTSAVQMEAA LKSKEEYQKV
LSKHGFGPIT TDIREGQVFY YAEDYHQQYL SKNPDGYCGL GGTGVSCPTA IKK
