MSRA_BOVIN
ID MSRA_BOVIN Reviewed; 233 AA.
AC P54149; Q3ZC16; Q5E976;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
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 Flags: Precursor;
GN Name=MSRA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RX PubMed=8700890; DOI=10.1073/pnas.93.5.2095;
RA Moskovitz J., Weissbach H., Brot N.;
RT "Cloning the expression of a mammalian gene involved in the reduction of
RT methionine sulfoxide residues in proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2095-2099(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=11063566; DOI=10.1021/bi0020269;
RA Lowther W.T., Brot N., Weissbach H., Matthews B.W.;
RT "Structure and mechanism of peptide methionine sulfoxide reductase, an
RT 'anti-oxidation' enzyme.";
RL Biochemistry 39:13307-13312(2000).
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 -!- 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: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; U37150; AAC48539.1; -; mRNA.
DR EMBL; BT021044; AAX09061.1; -; mRNA.
DR EMBL; BC102980; AAI02981.1; -; mRNA.
DR RefSeq; NP_776539.1; NM_174114.2.
DR PDB; 1FVA; X-ray; 1.70 A; A/B=13-229.
DR PDB; 1FVG; X-ray; 1.60 A; A=21-219.
DR PDBsum; 1FVA; -.
DR PDBsum; 1FVG; -.
DR AlphaFoldDB; P54149; -.
DR SMR; P54149; -.
DR BioGRID; 158665; 1.
DR STRING; 9913.ENSBTAP00000028825; -.
DR BindingDB; P54149; -.
DR ChEMBL; CHEMBL2007622; -.
DR PaxDb; P54149; -.
DR PeptideAtlas; P54149; -.
DR PRIDE; P54149; -.
DR Ensembl; ENSBTAT00000028825; ENSBTAP00000028825; ENSBTAG00000021632.
DR GeneID; 281312; -.
DR KEGG; bta:281312; -.
DR CTD; 4482; -.
DR VEuPathDB; HostDB:ENSBTAG00000021632; -.
DR VGNC; VGNC:31705; MSRA.
DR eggNOG; KOG1635; Eukaryota.
DR GeneTree; ENSGT00390000003823; -.
DR HOGENOM; CLU_031040_10_3_1; -.
DR InParanoid; P54149; -.
DR OMA; AGPFYYA; -.
DR OrthoDB; 1383773at2759; -.
DR TreeFam; TF353884; -.
DR BRENDA; 1.8.4.11; 908.
DR EvolutionaryTrace; P54149; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000021632; Expressed in metanephros cortex and 105 other tissues.
DR ExpressionAtlas; P54149; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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 3D-structure; Acetylation; Disulfide bond; Mitochondrion; Oxidoreductase;
KW Redox-active center; 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_0000138625"
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 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 CONFLICT 4
FT /note="A -> V (in Ref. 1; AAC48539)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="H -> R (in Ref. 2; AAX09061)"
FT /evidence="ECO:0000305"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1FVG"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1FVG"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1FVG"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:1FVG"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:1FVG"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:1FVG"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:1FVG"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1FVG"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1FVG"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:1FVG"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1FVG"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1FVG"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1FVG"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1FVG"
FT HELIX 164..183
FT /evidence="ECO:0007829|PDB:1FVG"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1FVG"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1FVG"
SQ SEQUENCE 233 AA; 25818 MW; DA09151E42FB6C08 CRC64;
MLSATRRALQ LFHSLFPIPR MGDSAAKIVS PQEALPGRKE PLVVAAKHHV NGNRTVEPFP
EGTQMAVFGM GCFWGAERKF WTLKGVYSTQ VGFAGGYTPN PTYKEVCSGK TGHAEVVRVV
FQPEHISFEE LLKVFWENHD PTQGMRQGND HGSQYRSAIY PTSAEHVGAA LKSKEDYQKV
LSEHGFGLIT TDIREGQTFY YAEDYHQQYL SKDPDGYCGL GGTGVSCPLG IKK
