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Glutaredoxin-2, mitochondrial

 GLRX2_HUMAN             Reviewed;         164 AA.
Q9NS18; Q3LR69; Q7L1N7; Q96JC0; Q9Y3D4;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=Glutaredoxin-2, mitochondrial;
Flags: Precursor;
Name=GLRX2; Synonyms=GRX2; ORFNames=CGI-133;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Colon, and Testis;
PubMed=11297543; DOI=10.1074/jbc.M011605200;
Lundberg M., Johansson C., Chandra J., Enoksson M., Jacobsson G.,
Ljung J., Johansson M., Holmgren A.;
"Cloning and expression of a novel human glutaredoxin (Grx2) with
mitochondrial and nuclear isoforms.";
J. Biol. Chem. 276:26269-26275(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11397793; DOI=10.1074/jbc.M100020200;
Gladyshev V.N., Liu A., Novoselov S.V., Krysan K., Sun Q.-A.,
Kryukov V.M., Kryukov G.V., Lou M.F.;
"Identification and characterization of a new mammalian glutaredoxin
(thioltransferase), Grx2.";
J. Biol. Chem. 276:30374-30380(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-95.
NIEHS SNPs program;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-164 (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-164 (ISOFORM 1).
TISSUE=Mammary gland;
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).
[7]
TISSUE SPECIFICITY.
PubMed=15184054; DOI=10.1016/j.bbrc.2004.04.199;
Lundberg M., Fernandes A.P., Kumar S., Holmgren A.;
"Cellular and plasma levels of human glutaredoxin 1 and 2 detected by
sensitive ELISA systems.";
Biochem. Biophys. Res. Commun. 319:801-809(2004).
[8]
TISSUE SPECIFICITY.
PubMed=15297967; DOI=10.1016/j.humpath.2004.04.009;
Peltoniemi M., Kaarteenaho-Wiik R., Saily M., Sormunen R., Paakko P.,
Holmgren A., Soini Y., Kinnula V.L.;
"Expression of glutaredoxin is highly cell specific in human lung and
is decreased by transforming growth factor-beta in vitro and in
interstitial lung diseases in vivo.";
Hum. Pathol. 35:1000-1007(2004).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF SER-78 AND
CYS-80.
PubMed=14676218; DOI=10.1074/jbc.M312719200;
Johansson C., Lillig C.H., Holmgren A.;
"Human mitochondrial glutaredoxin reduces S-glutathionylated proteins
with high affinity accepting electrons from either glutathione or
thioredoxin reductase.";
J. Biol. Chem. 279:7537-7543(2004).
[10]
FUNCTION.
PubMed=15328416; DOI=10.1073/pnas.0401896101;
Lillig C.H., Loenn M.E., Enoksson M., Fernandes A.P., Holmgren A.;
"Short interfering RNA-mediated silencing of glutaredoxin 2 increases
the sensitivity of HeLa cells toward doxorubicin and phenylarsine
oxide.";
Proc. Natl. Acad. Sci. U.S.A. 101:13227-13232(2004).
[11]
FUNCTION.
PubMed=15649413; DOI=10.1016/j.bbrc.2004.12.067;
Enoksson M., Fernandes A.P., Prast S., Lillig C.H., Holmgren A.,
Orrenius S.;
"Overexpression of glutaredoxin 2 attenuates apoptosis by preventing
cytochrome c release.";
Biochem. Biophys. Res. Commun. 327:774-779(2005).
[12]
SUBUNIT, ENZYME REGULATION, METAL-BINDING, AND MUTAGENESIS OF CYS-68
AND CYS-153.
PubMed=15917333; DOI=10.1073/pnas.0500735102;
Lillig C.H., Berndt C., Vergnolle O., Loenn M.E., Hudemann C.,
Bill E., Holmgren A.;
"Characterization of human glutaredoxin 2 as iron-sulfur protein: a
possible role as redox sensor.";
Proc. Natl. Acad. Sci. U.S.A. 102:8168-8173(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
STRUCTURE BY NMR OF 48-164.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-044, an N-terminal 2 domain of
glutaredoxin 2 from human cDNA.";
Submitted (NOV-2005) to the PDB data bank.
[15]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 50-164 IN COMPLEX WITH
GLUTATHIONE, GLUTATHIONYLATION AT CYS-77, AND DISULFIDE BOND.
PubMed=17121859; DOI=10.1074/jbc.M608179200;
Johansson C., Kavanagh K.L., Gileadi O., Oppermann U.;
"Reversible sequestration of active site cysteines in a 2Fe-2S-bridged
dimer provides a mechanism for glutaredoxin 2 regulation in human
mitochondria.";
J. Biol. Chem. 282:3077-3082(2007).
-!- FUNCTION: Glutathione-dependent oxidoreductase that facilitates
the maintenance of mitochondrial redox homeostasis upon induction
of apoptosis by oxidative stress. Involved in response to hydrogen
peroxide and regulation of apoptosis caused by oxidative stress.
Acts as a very efficient catalyst of monothiol reactions because
of its high affinity for protein glutathione-mixed disulfides. Can
receive electrons not only from glutathione (GSH), but also from
thioredoxin reductase supporting both monothiol and dithiol
reactions. Efficiently catalyzes both glutathionylation and
deglutathionylation of mitochondrial complex I, which in turn
regulates the superoxide production by the complex. Overexpression
decreases the susceptibility to apoptosis and prevents loss of
cardiolipin and cytochrome c release.
{ECO:0000269|PubMed:11297543, ECO:0000269|PubMed:14676218,
ECO:0000269|PubMed:15328416, ECO:0000269|PubMed:15649413}.
-!- ENZYME REGULATION: The 2Fe-2S present in the homodimer leads to
inactivation of the enzyme. The 2Fe-2S may serve as a redox
sensor: the presence of one-electron oxidants or reductants
leading to the loss of the 2Fe-2S cluster, subsequent
monomerization and activation of the enzyme. Unlike other
glutaredoxins, it is not inhibited by oxidation of structural Cys
residues. {ECO:0000269|PubMed:15917333}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.9 mM for GSH {ECO:0000269|PubMed:14676218};
KM=0.77 mM for glutathionylated ribonuclease A
{ECO:0000269|PubMed:14676218};
KM=4.3 mM for glutathionylated BSA
{ECO:0000269|PubMed:14676218};
KM=0.11 mM for glutathionylated beta-mercaptoethanol
{ECO:0000269|PubMed:14676218};
-!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The
homodimer is probably linked by 1 2Fe-2S cluster.
{ECO:0000269|PubMed:15917333, ECO:0000269|PubMed:17121859}.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Grx2a;
IsoId=Q9NS18-1; Sequence=Displayed;
Name=2; Synonyms=Grx2b;
IsoId=Q9NS18-2; Sequence=VSP_015221;
Note=Variant in position: 40:R->W.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
skeletal muscle, colon, thymus, spleen, kidney, liver, small
intestine, placenta and lung. Not expressed in peripheral blood
leukocytes. {ECO:0000269|PubMed:11297543,
ECO:0000269|PubMed:15184054, ECO:0000269|PubMed:15297967}.
-!- MISCELLANEOUS: The absence of GLRX2 dramatically sensitizes cells
to cell death induced by doxorubicin/adriamycin and phenylarsine
oxide.
-!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD34128.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAH28113.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/glrx2/";
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EMBL; AF132495; AAF37320.2; -; mRNA.
EMBL; AF290514; AAK83089.1; -; mRNA.
EMBL; AY038988; AAK72499.1; -; mRNA.
EMBL; DQ194815; ABA03170.1; -; Genomic_DNA.
EMBL; AL136370; CAI10820.1; -; Genomic_DNA.
EMBL; AL136370; CAI10821.1; -; Genomic_DNA.
EMBL; AF151891; AAD34128.1; ALT_FRAME; mRNA.
EMBL; BC028113; AAH28113.1; ALT_INIT; mRNA.
CCDS; CCDS1380.1; -. [Q9NS18-2]
CCDS; CCDS1381.1; -. [Q9NS18-1]
RefSeq; NP_001230328.1; NM_001243399.1.
RefSeq; NP_001306220.1; NM_001319291.1.
RefSeq; NP_057150.2; NM_016066.4. [Q9NS18-2]
RefSeq; NP_932066.1; NM_197962.2. [Q9NS18-1]
RefSeq; XP_016856886.1; XM_017001397.1.
UniGene; Hs.458283; -.
PDB; 2CQ9; NMR; -; A=48-164.
PDB; 2FLS; X-ray; 2.05 A; A=56-164.
PDB; 2HT9; X-ray; 1.90 A; A/B=41-164.
PDBsum; 2CQ9; -.
PDBsum; 2FLS; -.
PDBsum; 2HT9; -.
ProteinModelPortal; Q9NS18; -.
SMR; Q9NS18; -.
BioGrid; 119228; 6.
IntAct; Q9NS18; 2.
DrugBank; DB00143; Glutathione.
iPTMnet; Q9NS18; -.
PhosphoSitePlus; Q9NS18; -.
BioMuta; GLRX2; -.
DMDM; 73919686; -.
EPD; Q9NS18; -.
MaxQB; Q9NS18; -.
PeptideAtlas; Q9NS18; -.
PRIDE; Q9NS18; -.
Ensembl; ENST00000367439; ENSP00000356409; ENSG00000023572. [Q9NS18-1]
Ensembl; ENST00000367440; ENSP00000356410; ENSG00000023572. [Q9NS18-2]
GeneID; 51022; -.
KEGG; hsa:51022; -.
UCSC; uc001gsz.3; human. [Q9NS18-1]
CTD; 51022; -.
DisGeNET; 51022; -.
EuPathDB; HostDB:ENSG00000023572.8; -.
GeneCards; GLRX2; -.
HGNC; HGNC:16065; GLRX2.
HPA; HPA023087; -.
HPA; HPA057224; -.
MIM; 606820; gene.
neXtProt; NX_Q9NS18; -.
OpenTargets; ENSG00000023572; -.
PharmGKB; PA28732; -.
GeneTree; ENSGT00900000141123; -.
HOGENOM; HOG000095204; -.
HOVERGEN; HBG096801; -.
InParanoid; Q9NS18; -.
KO; K03676; -.
OMA; DMLEYGS; -.
OrthoDB; EOG091G0WLY; -.
PhylomeDB; Q9NS18; -.
TreeFam; TF319627; -.
SABIO-RK; Q9NS18; -.
EvolutionaryTrace; Q9NS18; -.
GeneWiki; GLRX2; -.
GenomeRNAi; 51022; -.
PRO; PR:Q9NS18; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000023572; -.
CleanEx; HS_GLRX2; -.
Genevisible; Q9NS18; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; TAS:UniProtKB.
GO; GO:0009055; F:electron carrier activity; NAS:UniProtKB.
GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003756; F:protein disulfide isomerase activity; TAS:UniProtKB.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
GO; GO:0071451; P:cellular response to superoxide; IEA:Ensembl.
GO; GO:0042262; P:DNA protection; NAS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; TAS:UniProtKB.
GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
GO; GO:0051775; P:response to redox state; TAS:UniProtKB.
GO; GO:0009266; P:response to temperature stimulus; NAS:UniProtKB.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR011899; Glutaredoxin_euk/vir.
InterPro; IPR014025; Glutaredoxin_subgr.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00462; Glutaredoxin; 1.
PRINTS; PR00160; GLUTAREDOXIN.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR02180; GRX_euk; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Alternative splicing; Complete proteome;
Disulfide bond; Electron transport; Glutathionylation; Iron;
Iron-sulfur; Metal-binding; Mitochondrion; Nucleus; Phosphoprotein;
Polymorphism; Redox-active center; Reference proteome;
Transit peptide; Transport.
TRANSIT 1 19 Mitochondrion. {ECO:0000255}.
CHAIN 20 164 Glutaredoxin-2, mitochondrial.
/FTId=PRO_0000011628.
DOMAIN 57 157 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
METAL 68 68 Iron-sulfur (2Fe-2S); shared with dimeric
partner; in inactive form. {ECO:0000305}.
METAL 153 153 Iron-sulfur (2Fe-2S); shared with dimeric
partner; in inactive form. {ECO:0000305}.
BINDING 74 74 Glutathione.
{ECO:0000269|PubMed:17121859}.
BINDING 109 109 Glutathione.
{ECO:0000269|PubMed:17121859}.
BINDING 121 121 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:17121859}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 77 77 S-glutathionyl cysteine; alternate.
{ECO:0000269|PubMed:17121859}.
DISULFID 77 80 Redox-active; alternate. {ECO:0000250}.
VAR_SEQ 1 40 MIWRRAALAGTRLVWSRSGSAGWLDRAAGAAGAAAAAASG
-> MNPRDKQVSRFSPLKDVYTWVALAGIQRSGSPGRTRSA
ARR (in isoform 2).
{ECO:0000303|PubMed:11297543}.
/FTId=VSP_015221.
VARIANT 95 95 K -> E (in dbSNP:rs34237236).
{ECO:0000269|Ref.3}.
/FTId=VAR_025234.
MUTAGEN 68 68 C->S: Abolishes absorption at 320 nm and
420 nm suggesting the loss of 2Fe-2S-
binding. {ECO:0000269|PubMed:15917333}.
MUTAGEN 78 78 S->P: Specifically increases the specific
activity but decreases affinity for
glutathionylated substrates.
{ECO:0000269|PubMed:14676218}.
MUTAGEN 80 80 C->S: Strongly impairs enzymatic
activity. {ECO:0000269|PubMed:14676218}.
MUTAGEN 153 153 C->S: Abolishes absorption at 320 nm and
420 nm suggesting the loss of 2Fe-2S-
binding. {ECO:0000269|PubMed:15917333}.
HELIX 57 66 {ECO:0000244|PDB:2HT9}.
STRAND 68 73 {ECO:0000244|PDB:2HT9}.
HELIX 78 90 {ECO:0000244|PDB:2HT9}.
STRAND 95 98 {ECO:0000244|PDB:2HT9}.
HELIX 99 101 {ECO:0000244|PDB:2HT9}.
HELIX 105 116 {ECO:0000244|PDB:2HT9}.
STRAND 123 126 {ECO:0000244|PDB:2HT9}.
STRAND 129 133 {ECO:0000244|PDB:2HT9}.
HELIX 134 142 {ECO:0000244|PDB:2HT9}.
HELIX 146 152 {ECO:0000244|PDB:2HT9}.
STRAND 154 156 {ECO:0000244|PDB:2CQ9}.
HELIX 160 162 {ECO:0000244|PDB:2HT9}.
SEQUENCE 164 AA; 18052 MW; D9798A01BB532A5D CRC64;
MIWRRAALAG TRLVWSRSGS AGWLDRAAGA AGAAAAAASG MESNTSSSLE NLATAPVNQI
QETISDNCVV IFSKTSCSYC TMAKKLFHDM NVNYKVVELD LLEYGNQFQD ALYKMTGERT
VPRIFVNGTF IGGATDTHRL HKEGKLLPLV HQCYLKKSKR KEFQ


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