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Protein

Glutaredoxin-2, mitochondrial

Gene

Glrx2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

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).By similarity

Sites

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

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • cell redox homeostasis Source: InterPro
  • cellular response to superoxide Source: RGD
  • response to hydrogen peroxide Source: Ensembl
  • response to organic substance Source: Ensembl
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi1307950. Glrx2.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

  • dendrite Source: RGD
  • mitochondrial matrix Source: RGD
  • neuronal cell body Source: RGD
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionSequence analysisAdd
BLAST
Chaini20 – 157138Glutaredoxin-2, mitochondrialPRO_0000011631Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glutathionylation

Proteomic databases

PaxDbiQ6AXW1.
PRIDEiQ6AXW1.

Expressioni

Gene expression databases

GenevisibleiQ6AXW1. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000056811.

Structurei

3D structure databases

ProteinModelPortaliQ6AXW1.
SMRiQ6AXW1. Positions 46-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 150101GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
COG0695. LUCA.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG096801.
InParanoidiQ6AXW1.
KOiK03676.
OMAiFCKMAKN.
OrthoDBiEOG7QRQWZ.

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. AlignAdd to basket

Isoform 1 (identifier: Q6AXW1-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MSWYRAASVG RRLVASGRIL AGRRGAAGAA GSGMGNSTSS FWGKSATTPV
60 70 80 90 100
NQIQETISNN CVVIFSKSSC SYCSMAKKIF HDMNVNYKVV ELDMVEYGSQ
110 120 130 140 150
FQEALYKMTG ERTVPRIFVN GIFIGGAADT HRLHKEGKLL PLVHQCYLNK

SKRKDVE
Length:157
Mass (Da):17,275
Last modified:August 30, 2005 - v2
Checksum:i0CA4BEB5C9D7A572
GO
Isoform 2 (identifier: Q6AXW1-2) [UniParc]FASTAAdd to basket

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

Show »
Length:124
Mass (Da):14,003
Checksum:i626A932FFAD38F4B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform 2. 1 PublicationVSP_015223Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03084863 mRNA. No translation available.
BC079292 mRNA. Translation: AAH79292.1.
RefSeqiNP_001013052.1. NM_001013034.1. [Q6AXW1-2]
XP_006250017.1. XM_006249955.1. [Q6AXW1-1]
XP_006250018.1. XM_006249956.2. [Q6AXW1-2]
XP_006250019.1. XM_006249957.2. [Q6AXW1-2]
XP_006250020.1. XM_006249958.2. [Q6AXW1-2]
XP_008767745.1. XM_008769523.1. [Q6AXW1-2]
XP_008767746.1. XM_008769524.1. [Q6AXW1-2]
XP_008767747.1. XM_008769525.1. [Q6AXW1-2]
XP_008767748.1. XM_008769526.1. [Q6AXW1-2]
UniGeneiRn.17175.

Genome annotation databases

EnsembliENSRNOT00000060062; ENSRNOP00000056811; ENSRNOG00000003385. [Q6AXW1-1]
GeneIDi114022.
KEGGirno:114022.
UCSCiRGD:1307950. rat. [Q6AXW1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03084863 mRNA. No translation available.
BC079292 mRNA. Translation: AAH79292.1.
RefSeqiNP_001013052.1. NM_001013034.1. [Q6AXW1-2]
XP_006250017.1. XM_006249955.1. [Q6AXW1-1]
XP_006250018.1. XM_006249956.2. [Q6AXW1-2]
XP_006250019.1. XM_006249957.2. [Q6AXW1-2]
XP_006250020.1. XM_006249958.2. [Q6AXW1-2]
XP_008767745.1. XM_008769523.1. [Q6AXW1-2]
XP_008767746.1. XM_008769524.1. [Q6AXW1-2]
XP_008767747.1. XM_008769525.1. [Q6AXW1-2]
XP_008767748.1. XM_008769526.1. [Q6AXW1-2]
UniGeneiRn.17175.

3D structure databases

ProteinModelPortaliQ6AXW1.
SMRiQ6AXW1. Positions 46-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000056811.

Proteomic databases

PaxDbiQ6AXW1.
PRIDEiQ6AXW1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000060062; ENSRNOP00000056811; ENSRNOG00000003385. [Q6AXW1-1]
GeneIDi114022.
KEGGirno:114022.
UCSCiRGD:1307950. rat. [Q6AXW1-1]

Organism-specific databases

CTDi51022.
RGDi1307950. Glrx2.

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
COG0695. LUCA.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG096801.
InParanoidiQ6AXW1.
KOiK03676.
OMAiFCKMAKN.
OrthoDBiEOG7QRQWZ.

Miscellaneous databases

NextBioi618171.
PROiQ6AXW1.

Gene expression databases

GenevisibleiQ6AXW1. RN.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    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.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "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: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).

Entry informationi

Entry nameiGLRX2_RAT
AccessioniPrimary (citable) accession number: Q6AXW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: May 11, 2016
This is version 100 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.