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Q923X4 (GLRX2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaredoxin-2, mitochondrial
Gene names
Name:Glrx2
Synonyms:Grx2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.5

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 By similarity.

Subunit structure

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

Subcellular location

Isoform 1: Mitochondrion Ref.1.

Isoform 2: Nucleus Ref.1.

Tissue specificity

Widely expressed. Highly expressed in testis, and at much lower level in kidney and brain. Ref.4

Developmental stage

During development, it is expressed at highest level at E11. Ref.4

Sequence similarities

Belongs to the glutaredoxin family.

Contains 1 glutaredoxin domain.

Biophysicochemical properties

Kinetic parameters:

KM=1.68 mM for HEDS Ref.1

KM=1.77 mM for S-sulfocysteine

KM=0.3 mM for L-cystine

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q923X4-1)

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.
Isoform 2 (identifier: Q923X4-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1919Mitochondrion Potential
Chain20 – 156137Glutaredoxin-2, mitochondrial
PRO_0000011629

Regions

Domain50 – 150101Glutaredoxin

Sites

Metal binding611Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
Metal binding1461Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
Binding site671Glutathione By similarity
Binding site1021Glutathione By similarity
Binding site1141Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue701S-glutathionyl cysteine; alternate By similarity
Disulfide bond70 ↔ 73Redox-active; alternate By similarity

Natural variations

Alternative sequence1 – 3333Missing in isoform 2.
VSP_015222

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Grx2a) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 605BA5C62A139C3E

FASTA15617,307
        10         20         30         40         50         60 
MSWRRAASVG RRLVASGRIL AGRRGAAGAA GSGMGNSTSS FWGKSTTTPV NQIQETISNN 

        70         80         90        100        110        120 
CVVIFSKTSC SYCSMAKKIF HDMNVNYKAV ELDMLEYGNQ FQDALHKMTG ERTVPRIFVN 

       130        140        150 
GRFIGGAADT HRLHKEGKLL PLVHQCYLKK KQEERH 

« Hide

Isoform 2 [UniParc].

Checksum: 803375159539AECD
Show »

FASTA12314,042

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF380337 mRNA. Translation: AAK85319.1.
AF276918 mRNA. Translation: AAF86465.1. Frameshift.
AK005853 mRNA. Translation: BAB24276.1.
CCDSCCDS15343.1. [Q923X4-1]
CCDS15344.1. [Q923X4-2]
RefSeqNP_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]
UniGeneMm.272727.

3D structure databases

ProteinModelPortalQ923X4.
SMRQ923X4. Positions 49-148.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ923X4.

Proteomic databases

MaxQBQ923X4.
PaxDbQ923X4.
PRIDEQ923X4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050491; ENSMUSP00000053443; ENSMUSG00000018196. [Q923X4-1]
ENSMUST00000111957; ENSMUSP00000107588; ENSMUSG00000018196. [Q923X4-2]
ENSMUST00000129653; ENSMUSP00000121010; ENSMUSG00000018196. [Q923X4-2]
ENSMUST00000145969; ENSMUSP00000121665; ENSMUSG00000018196. [Q923X4-2]
GeneID69367.
KEGGmmu:69367.
UCSCuc007cwz.1. mouse. [Q923X4-1]

Organism-specific databases

CTD51022.
MGIMGI:1916617. Glrx2.

Phylogenomic databases

eggNOGKOG1752.
GeneTreeENSGT00390000003677.
HOGENOMHOG000095204.
HOVERGENHBG096801.
InParanoidQ923X4.
KOK03676.
OMAGMESNTS.
OrthoDBEOG7QRQWZ.
PhylomeDBQ923X4.
TreeFamTF319627.

Gene expression databases

ArrayExpressQ923X4.
BgeeQ923X4.
CleanExMM_GLRX2.
GenevestigatorQ923X4.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSPR00160. GLUTAREDOXIN.
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR02180. GRX_euk. 1 hit.
PROSITEPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio329240.
PROQ923X4.
SOURCESearch...

Entry information

Entry nameGLRX2_MOUSE
AccessionPrimary (citable) accession number: Q923X4
Secondary accession number(s): Q9DAG8, Q9JHY6
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot