ID Q3UQ95_MOUSE Unreviewed; 123 AA.
AC Q3UQ95;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Glutaredoxin-2, mitochondrial {ECO:0000256|ARBA:ARBA00039819};
GN Name=Glrx2 {ECO:0000313|MGI:MGI:1916617};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE25147.1};
RN [1] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [5] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [6] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000313|EMBL:BAE25147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE25147.1};
RC TISSUE=Mammary gland {ECO:0000313|EMBL:BAE25147.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
CC -!- FUNCTION: Glutathione-dependent oxidoreductase that facilitates the
CC maintenance of mitochondrial redox homeostasis upon induction of
CC apoptosis by oxidative stress. Involved in response to hydrogen
CC peroxide and regulation of apoptosis caused by oxidative stress. Acts
CC as a very efficient catalyst of monothiol reactions because of its high
CC affinity for protein glutathione-mixed disulfides. Can receive
CC electrons not only from glutathione (GSH), but also from thioredoxin
CC reductase supporting both monothiol and dithiol reactions. Efficiently
CC catalyzes both glutathionylation and deglutathionylation of
CC mitochondrial complex I, which in turn regulates the superoxide
CC production by the complex. Overexpression decreases the susceptibility
CC to apoptosis and prevents loss of cardiolipin and cytochrome c release.
CC {ECO:0000256|ARBA:ARBA00037470}.
CC -!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The homodimer
CC is probably linked by 1 2Fe-2S cluster.
CC {ECO:0000256|ARBA:ARBA00038558}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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DR EMBL; AK142654; BAE25147.1; -; mRNA.
DR RefSeq; NP_001033682.1; NM_001038593.1.
DR RefSeq; NP_001033683.1; NM_001038594.1.
DR RefSeq; NP_075994.2; NM_023505.2.
DR RefSeq; XP_006529919.1; XM_006529856.2.
DR AlphaFoldDB; Q3UQ95; -.
DR SMR; Q3UQ95; -.
DR PeptideAtlas; Q3UQ95; -.
DR DNASU; 69367; -.
DR GeneID; 69367; -.
DR AGR; MGI:1916617; -.
DR CTD; 51022; -.
DR MGI; MGI:1916617; Glrx2.
DR VEuPathDB; HostDB:ENSMUSG00000018196; -.
DR HOGENOM; CLU_026126_7_2_1; -.
DR OMA; INGNCVG; -.
DR OrthoDB; 203654at2759; -.
DR BioGRID-ORCS; 69367; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Glrx2; mouse.
DR ExpressionAtlas; Q3UQ95; baseline and differential.
DR Genevisible; Q3UQ95; MM.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR PANTHER; PTHR46679; -; 1.
DR PANTHER; PTHR46679:SF1; GLUTAREDOXIN-2, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Glutathionylation {ECO:0000256|ARBA:ARBA00023206};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 29..91
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 123 AA; 14042 MW; 803375159539AECD CRC64;
MGNSTSSFWG KSTTTPVNQI QETISNNCVV IFSKTSCSYC SMAKKIFHDM NVNYKAVELD
MLEYGNQFQD ALHKMTGERT VPRIFVNGRF IGGAADTHRL HKEGKLLPLV HQCYLKKKQE
ERH
//
