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Protein

Glutaredoxin-1

Gene

Glrx

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • cell redox homeostasis Source: InterPro
  • cellular response to estradiol stimulus Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • negative regulation of hydrogen peroxide-mediated programmed cell death Source: RGD
  • negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: RGD
  • ovulation cycle process Source: RGD
  • positive regulation of cell adhesion molecule production Source: RGD
  • positive regulation of exocytosis Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • positive regulation of NIK/NF-kappaB signaling Source: RGD
  • response to ischemia Source: RGD
  • response to nutrient Source: RGD
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-1
Alternative name(s):
Thioltransferase-1
Short name:
TTase-1
Gene namesi
Name:Glrx
Synonyms:Glrx1, Grx
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi70951. Glrx.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • dendrite Source: RGD
  • mitochondrial intermembrane space Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 107106Glutaredoxin-1PRO_0000141604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei9 – 91N6-succinyllysineBy similarity
Disulfide bondi23 ↔ 26Redox-activeBy similarity
Disulfide bondi79 ↔ 83By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiQ9ESH6.
PRIDEiQ9ESH6.

PTM databases

iPTMnetiQ9ESH6.
PhosphoSiteiQ9ESH6.

Expressioni

Gene expression databases

GenevisibleiQ9ESH6. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4575322.
STRINGi10116.ENSRNOP00000016372.

Structurei

3D structure databases

ProteinModelPortaliQ9ESH6.
SMRiQ9ESH6. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 106104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
COG0695. LUCA.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG000283.
InParanoidiQ9ESH6.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
PhylomeDBiQ9ESH6.
TreeFamiTF326994.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. 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.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9ESH6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQEFVNCKI QSGKVVVFIK PTCPYCRKTQ EILSQLPFKR GLLEFVDITA
60 70 80 90 100
TNNTNAIQDY LQQLTGARTV PRVFIGKDCI GGCSDLLSMQ QNGELTARLK

QIGALQL
Length:107
Mass (Da):11,879
Last modified:January 23, 2007 - v3
Checksum:iC46C67042138E9E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91K → R in AAK07419 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF167981 mRNA. Translation: AAF89637.3.
AF319950 mRNA. Translation: AAK07419.1.
BC061555 mRNA. Translation: AAH61555.1.
RefSeqiNP_071614.1. NM_022278.1.
UniGeneiRn.1484.

Genome annotation databases

EnsembliENSRNOT00000016372; ENSRNOP00000016372; ENSRNOG00000012183.
GeneIDi64045.
KEGGirno:64045.
UCSCiRGD:70951. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF167981 mRNA. Translation: AAF89637.3.
AF319950 mRNA. Translation: AAK07419.1.
BC061555 mRNA. Translation: AAH61555.1.
RefSeqiNP_071614.1. NM_022278.1.
UniGeneiRn.1484.

3D structure databases

ProteinModelPortaliQ9ESH6.
SMRiQ9ESH6. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4575322.
STRINGi10116.ENSRNOP00000016372.

PTM databases

iPTMnetiQ9ESH6.
PhosphoSiteiQ9ESH6.

Proteomic databases

PaxDbiQ9ESH6.
PRIDEiQ9ESH6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016372; ENSRNOP00000016372; ENSRNOG00000012183.
GeneIDi64045.
KEGGirno:64045.
UCSCiRGD:70951. rat.

Organism-specific databases

CTDi2745.
RGDi70951. Glrx.

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
COG0695. LUCA.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG000283.
InParanoidiQ9ESH6.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
PhylomeDBiQ9ESH6.
TreeFamiTF326994.

Enzyme and pathway databases

ReactomeiR-RNO-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

NextBioi612705.
PROiQ9ESH6.

Gene expression databases

GenevisibleiQ9ESH6. RN.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. 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.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of rat glutaredoxin."
    Miranda-Vizuete A.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and expression of glutaredoxin cDNA gene from PC12 cell line in E.coli."
    Liu C.Z., Xie Z.H., He Y.H., Wang A.M., Ma C.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Tissue: Pituitary.

Entry informationi

Entry nameiGLRX1_RAT
AccessioniPrimary (citable) accession number: Q9ESH6
Secondary accession number(s): Q99PB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 107 of the entry and version 3 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.