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Q923X4

- GLRX2_MOUSE

UniProt

Q923X4 - GLRX2_MOUSE

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Protein
Glutaredoxin-2, mitochondrial
Gene
Glrx2, Grx2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Enzyme regulationi

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.

Kineticsi

  1. KM=1.68 mM for HEDS1 Publication
  2. KM=1.77 mM for S-sulfocysteine
  3. KM=0.3 mM for L-cystine

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
Binding sitei67 – 671Glutathione By similarity
Binding sitei102 – 1021Glutathione By similarity
Binding sitei114 – 1141Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Metal bindingi146 – 1461Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. protein disulfide oxidoreductase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. response to hydrogen peroxide Source: UniProtKB
  3. response to organic substance Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-2, mitochondrial
Gene namesi
Name:Glrx2
Synonyms:Grx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1916617. Glrx2.

Subcellular locationi

Isoform 1 : Mitochondrion 1 Publication
Isoform 2 : Nucleus 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919Mitochondrion Reviewed prediction
Add
BLAST
Chaini20 – 156137Glutaredoxin-2, mitochondrial
PRO_0000011629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 73Redox-active; alternate By similarity
Modified residuei70 – 701S-glutathionyl cysteine; alternate By similarity

Keywords - PTMi

Disulfide bond, Glutathionylation

Proteomic databases

MaxQBiQ923X4.
PaxDbiQ923X4.
PRIDEiQ923X4.

PTM databases

PhosphoSiteiQ923X4.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in testis, and at much lower level in kidney and brain.1 Publication

Developmental stagei

During development, it is expressed at highest level at E11.1 Publication

Gene expression databases

ArrayExpressiQ923X4.
BgeeiQ923X4.
CleanExiMM_GLRX2.
GenevestigatoriQ923X4.

Interactioni

Subunit structurei

Monomer; active form. Homodimer; inactive form. The homodimer is probably linked by 1 2Fe-2S cluster By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ923X4.
SMRiQ923X4. Positions 49-148.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 150101Glutaredoxin
Add
BLAST

Sequence similaritiesi

Belongs to the glutaredoxin family.

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG1752.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG096801.
InParanoidiQ923X4.
KOiK03676.
OMAiGMESNTS.
OrthoDBiEOG7QRQWZ.
PhylomeDBiQ923X4.
TreeFamiTF319627.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q923X4-1) [UniParc]FASTAAdd to Basket

Also known as: Grx2a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSWRRAASVG RRLVASGRIL AGRRGAAGAA GSGMGNSTSS FWGKSTTTPV    50
NQIQETISNN CVVIFSKTSC SYCSMAKKIF HDMNVNYKAV ELDMLEYGNQ 100
FQDALHKMTG ERTVPRIFVN GRFIGGAADT HRLHKEGKLL PLVHQCYLKK 150
KQEERH 156
Length:156
Mass (Da):17,307
Last modified:December 1, 2001 - v1
Checksum:i605BA5C62A139C3E
GO
Isoform 2 (identifier: Q923X4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Show »
Length:123
Mass (Da):14,042
Checksum:i803375159539AECD
GO

Sequence cautioni

The sequence AAF86465.1 differs from that shown. Reason: Frameshift at position 128.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform 2.
VSP_015222Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF380337 mRNA. Translation: AAK85319.1.
AF276918 mRNA. Translation: AAF86465.1. Frameshift.
AK005853 mRNA. Translation: BAB24276.1.
CCDSiCCDS15343.1. [Q923X4-1]
CCDS15344.1. [Q923X4-2]
RefSeqiNP_001033681.1. NM_001038592.1. [Q923X4-1]
NP_001033682.1. NM_001038593.1. [Q923X4-2]
NP_001033683.1. NM_001038594.1. [Q923X4-2]
NP_075994.2. NM_023505.2. [Q923X4-2]
XP_006529919.1. XM_006529856.1. [Q923X4-2]
UniGeneiMm.272727.

Genome annotation databases

EnsembliENSMUST00000050491; ENSMUSP00000053443; ENSMUSG00000018196. [Q923X4-1]
ENSMUST00000111957; ENSMUSP00000107588; ENSMUSG00000018196. [Q923X4-2]
ENSMUST00000129653; ENSMUSP00000121010; ENSMUSG00000018196. [Q923X4-2]
ENSMUST00000145969; ENSMUSP00000121665; ENSMUSG00000018196. [Q923X4-2]
GeneIDi69367.
KEGGimmu:69367.
UCSCiuc007cwz.1. mouse. [Q923X4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF380337 mRNA. Translation: AAK85319.1 .
AF276918 mRNA. Translation: AAF86465.1 . Frameshift.
AK005853 mRNA. Translation: BAB24276.1 .
CCDSi CCDS15343.1. [Q923X4-1 ]
CCDS15344.1. [Q923X4-2 ]
RefSeqi NP_001033681.1. NM_001038592.1. [Q923X4-1 ]
NP_001033682.1. NM_001038593.1. [Q923X4-2 ]
NP_001033683.1. NM_001038594.1. [Q923X4-2 ]
NP_075994.2. NM_023505.2. [Q923X4-2 ]
XP_006529919.1. XM_006529856.1. [Q923X4-2 ]
UniGenei Mm.272727.

3D structure databases

ProteinModelPortali Q923X4.
SMRi Q923X4. Positions 49-148.
ModBasei Search...

PTM databases

PhosphoSitei Q923X4.

Proteomic databases

MaxQBi Q923X4.
PaxDbi Q923X4.
PRIDEi Q923X4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000050491 ; ENSMUSP00000053443 ; ENSMUSG00000018196 . [Q923X4-1 ]
ENSMUST00000111957 ; ENSMUSP00000107588 ; ENSMUSG00000018196 . [Q923X4-2 ]
ENSMUST00000129653 ; ENSMUSP00000121010 ; ENSMUSG00000018196 . [Q923X4-2 ]
ENSMUST00000145969 ; ENSMUSP00000121665 ; ENSMUSG00000018196 . [Q923X4-2 ]
GeneIDi 69367.
KEGGi mmu:69367.
UCSCi uc007cwz.1. mouse. [Q923X4-1 ]

Organism-specific databases

CTDi 51022.
MGIi MGI:1916617. Glrx2.

Phylogenomic databases

eggNOGi KOG1752.
GeneTreei ENSGT00390000003677.
HOGENOMi HOG000095204.
HOVERGENi HBG096801.
InParanoidi Q923X4.
KOi K03676.
OMAi GMESNTS.
OrthoDBi EOG7QRQWZ.
PhylomeDBi Q923X4.
TreeFami TF319627.

Miscellaneous databases

NextBioi 329240.
PROi Q923X4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q923X4.
Bgeei Q923X4.
CleanExi MM_GLRX2.
Genevestigatori Q923X4.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00462. Glutaredoxin. 1 hit.
[Graphical view ]
PRINTSi PR00160. GLUTAREDOXIN.
SUPFAMi SSF52833. SSF52833. 1 hit.
TIGRFAMsi TIGR02180. GRX_euk. 1 hit.
PROSITEi PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2."
    Gladyshev V.N., Liu A., Novoselov S.V., Krysan K., Sun Q.-A., Kryukov V.M., Kryukov G.V., Lou M.F.
    J. Biol. Chem. 276:30374-30380(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
  2. Reddy P.G., Bhuyan D.K., Bhuyan K.C.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: CFW.
    Tissue: Lens.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  4. "Absolute gene expression patterns of thioredoxin and glutaredoxin redox systems in mouse."
    Jurado J., Prieto-Alamo M.-J., Madrid-Risquez J., Pueyo C.
    J. Biol. Chem. 278:45546-45554(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defense."
    Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., Murphy M.P.
    J. Biol. Chem. 279:47939-47951(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGLRX2_MOUSE
AccessioniPrimary (citable) accession number: Q923X4
Secondary accession number(s): Q9DAG8, Q9JHY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi