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Mitochondrial peptide methionine sulfoxide reductase (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (PMSR)

 MSRA_HUMAN              Reviewed;         235 AA.
Q9UJ68; E9PAS8; Q52TC4; Q549N4; Q66MI7;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 147.
RecName: Full=Mitochondrial peptide methionine sulfoxide reductase;
EC=1.8.4.11;
AltName: Full=Peptide-methionine (S)-S-oxide reductase;
Short=Peptide Met(O) reductase;
AltName: Full=Protein-methionine-S-oxide reductase;
Short=PMSR;
Flags: Precursor;
Name=MSRA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=10452521; DOI=10.1016/S0014-5793(99)00917-5;
Kuschel L., Hansel A., Schoenherr R., Weissbach H., Brot N., Hoshi T.,
Heinemann S.H.;
"Molecular cloning and functional expression of a human peptide
methionine sulfoxide reductase (hMsrA).";
FEBS Lett. 456:17-21(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, AND
SUBCELLULAR LOCATION.
PubMed=15680232; DOI=10.1016/j.bbapap.2004.09.010;
Hansel A., Heinemann S.H., Hoshi T.;
"Heterogeneity and function of mammalian MSRs: enzymes for repair,
protection and regulation.";
Biochim. Biophys. Acta 1703:239-247(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), NUCLEOTIDE SEQUENCE
[GENOMIC DNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE PROMOTER USAGE, AND
SUBCELLULAR LOCATION.
PubMed=16364291; DOI=10.1016/j.exer.2005.10.003;
Lee J.W., Gordiyenko N.V., Marchetti M., Tserentsoodol N., Sagher D.,
Alam S., Weissbach H., Kantorow M., Rodriguez I.R.;
"Gene structure, localization and role in oxidative stress of
methionine sulfoxide reductase A (MSRA) in the monkey retina.";
Exp. Eye Res. 82:816-827(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
[GENOMIC DNA] (ISOFORM 1).
Zhao Y., Yu L., Tu Q., Yue P., Zhang M., Zhao S.Y.;
"Cloning of a novel human cDNA which shows great homology to Bos
taurus methionine sulfoxide reductase (msrA) mRNA.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hypothalamus;
Peng Y., Huang C., Gu Y., Xu S., Han Z., Fu G., Chen Z.;
"A novel gene expressed in human hypothalamus.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-6; ARG-7; ARG-22 AND
11-LEU--LEU-14.
PubMed=12039877; DOI=10.1096/fj.01-0737fje;
Hansel A., Kuschel L., Hehl S., Lemke C., Agricola H.J., Hoshi T.,
Heinemann S.H.;
"Mitochondrial targeting of the human peptide methionine sulfoxide
reductase (MSRA), an enzyme involved in the repair of oxidized
proteins.";
FASEB J. 16:911-913(2002).
[11]
MYRISTOYLATION AT GLY-2 (ISOFORM 5), AND ALTERNATIVE INITIATION.
PubMed=20368336; DOI=10.1074/jbc.M110.119701;
Kim G., Cole N.B., Lim J.C., Zhao H., Levine R.L.;
"Dual sites of protein initiation control the localization and
myristoylation of methionine sulfoxide reductase A.";
J. Biol. Chem. 285:18085-18094(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
MYRISTOYLATION AT GLY-2 (ISOFORM 5), CLEAVAGE OF INITIATOR METHIONINE
(ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
-!- FUNCTION: Has an important function as a repair enzyme for
proteins that have been inactivated by oxidation. Catalyzes the
reversible oxidation-reduction of methionine sulfoxide in proteins
to methionine.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
-!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
L-methionine (S)-S-oxide + thioredoxin.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm. Membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=5;
Comment=Only about 25% of mRNAs are initiated at the
mitochondrial isoform 1 codon.;
Name=1; Synonyms=MsrA1, mitoMSRA, a;
IsoId=Q9UJ68-1; Sequence=Displayed;
Note=Mitochondrial. Produced by alternative splicing.;
Name=2; Synonyms=MsrA2, d;
IsoId=Q9UJ68-2; Sequence=VSP_041405;
Note=Cytoplasmic. Produced by alternative promoter usage.;
Name=3; Synonyms=MsrA3, cytoMSRA, c;
IsoId=Q9UJ68-3; Sequence=VSP_041406;
Note=Cytoplasmic and nuclear. Produced by alternative promoter
usage.;
Name=4; Synonyms=b;
IsoId=Q9UJ68-4; Sequence=VSP_041407;
Note=Produced by alternative splicing.;
Name=5;
IsoId=Q9UJ68-5; Sequence=VSP_042132;
Note=Cytoplasmic. Contains a N-myristoyl glycine at position 2.
Produced by alternative initiation.
{ECO:0000269|PubMed:20368336, ECO:0000269|PubMed:25807930};
-!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in adult kidney
and cerebellum, followed by liver, heart ventricles, bone marrow
and hippocampus.
-!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
{ECO:0000305}.
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EMBL; AJ242973; CAB59628.1; -; mRNA.
EMBL; AY690665; AAU11088.1; -; mRNA.
EMBL; AY958429; AAY17426.1; -; mRNA.
EMBL; AY958430; AAY17427.1; -; mRNA.
EMBL; AY958431; AAY17428.1; -; mRNA.
EMBL; AY958432; AAY17429.1; -; Genomic_DNA.
EMBL; AY958432; AAY17430.1; -; Genomic_DNA.
EMBL; AY958432; AAY17431.1; -; Genomic_DNA.
EMBL; AK293488; BAH11521.1; -; mRNA.
EMBL; AF086925; AAP97154.1; -; mRNA.
EMBL; AF183420; AAG09689.1; -; mRNA.
EMBL; AC023385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC034111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471157; EAW65584.1; -; Genomic_DNA.
EMBL; CH471157; EAW65585.1; -; Genomic_DNA.
EMBL; BC054033; AAH54033.1; -; mRNA.
CCDS; CCDS47798.1; -. [Q9UJ68-4]
CCDS; CCDS47799.1; -. [Q9UJ68-3]
CCDS; CCDS56522.1; -. [Q9UJ68-2]
CCDS; CCDS5975.1; -. [Q9UJ68-1]
RefSeq; NP_001129142.1; NM_001135670.2. [Q9UJ68-4]
RefSeq; NP_001129143.1; NM_001135671.2. [Q9UJ68-3]
RefSeq; NP_001186658.1; NM_001199729.2. [Q9UJ68-2]
RefSeq; NP_036463.1; NM_012331.4. [Q9UJ68-1]
RefSeq; XP_016868938.1; XM_017013449.1. [Q9UJ68-2]
RefSeq; XP_016868939.1; XM_017013450.1. [Q9UJ68-2]
UniGene; Hs.490981; -.
ProteinModelPortal; Q9UJ68; -.
SMR; Q9UJ68; -.
BioGrid; 110588; 9.
IntAct; Q9UJ68; 6.
STRING; 9606.ENSP00000313921; -.
DrugBank; DB00134; L-Methionine.
iPTMnet; Q9UJ68; -.
PhosphoSitePlus; Q9UJ68; -.
BioMuta; MSRA; -.
DMDM; 12230350; -.
EPD; Q9UJ68; -.
PaxDb; Q9UJ68; -.
PeptideAtlas; Q9UJ68; -.
PRIDE; Q9UJ68; -.
ProteomicsDB; 84588; -.
ProteomicsDB; 84589; -. [Q9UJ68-2]
ProteomicsDB; 84590; -. [Q9UJ68-3]
ProteomicsDB; 84591; -. [Q9UJ68-4]
ProteomicsDB; 84592; -. [Q9UJ68-5]
DNASU; 4482; -.
Ensembl; ENST00000317173; ENSP00000313921; ENSG00000175806. [Q9UJ68-1]
Ensembl; ENST00000382490; ENSP00000371930; ENSG00000175806. [Q9UJ68-3]
Ensembl; ENST00000441698; ENSP00000410912; ENSG00000175806. [Q9UJ68-4]
Ensembl; ENST00000528246; ENSP00000436839; ENSG00000175806. [Q9UJ68-2]
Ensembl; ENST00000643047; ENSP00000493922; ENSG00000285250. [Q9UJ68-3]
Ensembl; ENST00000643332; ENSP00000495223; ENSG00000285250. [Q9UJ68-4]
Ensembl; ENST00000645254; ENSP00000496174; ENSG00000285250. [Q9UJ68-2]
Ensembl; ENST00000645318; ENSP00000493848; ENSG00000285250. [Q9UJ68-1]
GeneID; 4482; -.
KEGG; hsa:4482; -.
UCSC; uc003wsx.4; human. [Q9UJ68-1]
CTD; 4482; -.
DisGeNET; 4482; -.
EuPathDB; HostDB:ENSG00000175806.14; -.
GeneCards; MSRA; -.
H-InvDB; HIX0168875; -.
HGNC; HGNC:7377; MSRA.
HPA; HPA023804; -.
HPA; HPA053069; -.
MIM; 601250; gene.
neXtProt; NX_Q9UJ68; -.
OpenTargets; ENSG00000175806; -.
PharmGKB; PA31182; -.
eggNOG; KOG1635; Eukaryota.
eggNOG; COG0225; LUCA.
GeneTree; ENSGT00390000003823; -.
HOGENOM; HOG000263862; -.
HOVERGEN; HBG006401; -.
InParanoid; Q9UJ68; -.
KO; K07304; -.
OMA; MRQGGDI; -.
OrthoDB; EOG091G0MD8; -.
PhylomeDB; Q9UJ68; -.
TreeFam; TF353884; -.
BRENDA; 1.8.4.11; 2681.
Reactome; R-HSA-5676934; Protein repair.
ChiTaRS; MSRA; human.
GeneWiki; MSRA_(gene); -.
GenomeRNAi; 4482; -.
PRO; PR:Q9UJ68; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000175806; -.
CleanEx; HS_MSRA; -.
ExpressionAtlas; Q9UJ68; baseline and differential.
Genevisible; Q9UJ68; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; TAS:Reactome.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0006555; P:methionine metabolic process; TAS:ProtInc.
GO; GO:0030091; P:protein repair; TAS:Reactome.
GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
Gene3D; 3.30.1060.10; -; 1.
HAMAP; MF_01401; MsrA; 1.
InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
Pfam; PF01625; PMSR; 1.
SUPFAM; SSF55068; SSF55068; 1.
TIGRFAMs; TIGR00401; msrA; 1.
1: Evidence at protein level;
Acetylation; Alternative initiation; Alternative promoter usage;
Alternative splicing; Complete proteome; Cytoplasm; Lipoprotein;
Membrane; Mitochondrion; Myristate; Nucleus; Oxidoreductase;
Reference proteome; Transit peptide.
TRANSIT 1 23 Mitochondrion.
CHAIN 24 235 Mitochondrial peptide methionine
sulfoxide reductase.
/FTId=PRO_0000138626.
MOD_RES 106 106 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9D6Y7}.
MOD_RES 106 106 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9D6Y7}.
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16364291}.
/FTId=VSP_041405.
VAR_SEQ 1 48 MLSATRRACQLLLLHSLFPVPRMGNSASNIVSPQEALPGRK
EQTPVAA -> MCSEP (in isoform 3).
{ECO:0000303|PubMed:15680232,
ECO:0000303|PubMed:16364291}.
/FTId=VSP_041406.
VAR_SEQ 1 22 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_042132.
VAR_SEQ 71 110 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_041407.
MUTAGEN 6 6 R->A: Impaired subcellular location.
{ECO:0000269|PubMed:12039877}.
MUTAGEN 7 7 R->A: Impaired subcellular location.
{ECO:0000269|PubMed:12039877}.
MUTAGEN 11 13 Missing: Impaired subcellular location.
MUTAGEN 22 22 R->A: Impaired subcellular location.
{ECO:0000269|PubMed:12039877}.
CONFLICT 12 14 Missing (in Ref. 6; AAG09689).
{ECO:0000305}.
CONFLICT 134 137 LKVF -> SRL (in Ref. 6; AAG09689).
{ECO:0000305}.
SEQUENCE 235 AA; 26132 MW; B89A9BBBE4D58D90 CRC64;
MLSATRRACQ LLLLHSLFPV PRMGNSASNI VSPQEALPGR KEQTPVAAKH HVNGNRTVEP
FPEGTQMAVF GMGCFWGAER KFWVLKGVYS TQVGFAGGYT SNPTYKEVCS EKTGHAEVVR
VVYQPEHMSF EELLKVFWEN HDPTQGMRQG NDHGTQYRSA IYPTSAKQME AALSSKENYQ
KVLSEHGFGP ITTDIREGQT FYYAEDYHQQ YLSKNPNGYC GLGGTGVSCP VGIKK


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