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Glutaredoxin-2, mitochondrial

 GLRX2_RAT               Reviewed;         157 AA.
Q6AXW1;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 2.
12-SEP-2018, entry version 113.
RecName: Full=Glutaredoxin-2, mitochondrial;
Flags: Precursor;
Name=Glrx2; Synonyms=Grx2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[3]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
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).
-!- 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 (By similarity).
{ECO:0000250}.
-!- ACTIVITY 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 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The
homodimer is probably linked by 1 2Fe-2S cluster (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6AXW1-1; Sequence=Displayed;
Name=2;
IsoId=Q6AXW1-2; Sequence=VSP_015223;
-!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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EMBL; AABR03084863; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC079292; AAH79292.1; -; mRNA.
RefSeq; NP_001013052.1; NM_001013034.1. [Q6AXW1-2]
RefSeq; XP_006250017.1; XM_006249955.2. [Q6AXW1-1]
RefSeq; XP_006250019.1; XM_006249957.3. [Q6AXW1-2]
RefSeq; XP_008767748.1; XM_008769526.2. [Q6AXW1-2]
UniGene; Rn.17175; -.
ProteinModelPortal; Q6AXW1; -.
SMR; Q6AXW1; -.
STRING; 10116.ENSRNOP00000056811; -.
PaxDb; Q6AXW1; -.
PRIDE; Q6AXW1; -.
Ensembl; ENSRNOT00000060062; ENSRNOP00000056811; ENSRNOG00000003385. [Q6AXW1-1]
GeneID; 114022; -.
KEGG; rno:114022; -.
UCSC; RGD:1307950; rat. [Q6AXW1-1]
CTD; 51022; -.
RGD; 1307950; Glrx2.
eggNOG; KOG1752; Eukaryota.
eggNOG; COG0695; LUCA.
GeneTree; ENSGT00900000141123; -.
HOGENOM; HOG000095204; -.
HOVERGEN; HBG096801; -.
InParanoid; Q6AXW1; -.
KO; K03676; -.
OMA; DMLEYGS; -.
OrthoDB; EOG091G0WLY; -.
PRO; PR:Q6AXW1; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000003385; Expressed in 10 organ(s), highest expression level in testis.
Genevisible; Q6AXW1; RN.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0071451; P:cellular response to superoxide; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
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.
2: Evidence at transcript level;
2Fe-2S; Alternative splicing; Complete proteome; Disulfide bond;
Electron transport; Glutathionylation; Iron; Iron-sulfur;
Metal-binding; Mitochondrion; Nucleus; Redox-active center;
Reference proteome; Transit peptide; Transport.
TRANSIT 1 19 Mitochondrion. {ECO:0000255}.
CHAIN 20 157 Glutaredoxin-2, mitochondrial.
/FTId=PRO_0000011631.
DOMAIN 50 150 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
METAL 61 61 Iron-sulfur (2Fe-2S); shared with dimeric
partner; in inactive form. {ECO:0000250}.
METAL 146 146 Iron-sulfur (2Fe-2S); shared with dimeric
partner; in inactive form. {ECO:0000250}.
BINDING 67 67 Glutathione. {ECO:0000250}.
BINDING 102 102 Glutathione. {ECO:0000250}.
BINDING 114 114 Glutathione; via amide nitrogen and
carbonyl oxygen. {ECO:0000250}.
MOD_RES 70 70 S-glutathionyl cysteine; alternate.
{ECO:0000250}.
DISULFID 70 73 Redox-active; alternate. {ECO:0000250}.
VAR_SEQ 1 33 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015223.
SEQUENCE 157 AA; 17275 MW; 0CA4BEB5C9D7A572 CRC64;
MSWYRAASVG RRLVASGRIL AGRRGAAGAA GSGMGNSTSS FWGKSATTPV NQIQETISNN
CVVIFSKSSC SYCSMAKKIF HDMNVNYKVV ELDMVEYGSQ FQEALYKMTG ERTVPRIFVN
GIFIGGAADT HRLHKEGKLL PLVHQCYLNK SKRKDVE


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