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Protein

Glutaredoxin-1

Gene

GLRX

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

ReactomeiR-SSC-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:GRX
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 106105Glutaredoxin-1PRO_0000141602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei9 – 91N6-succinyllysineBy similarity
Disulfide bondi23 ↔ 26Redox-active
Disulfide bondi79 ↔ 831 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP12309.
PeptideAtlasiP12309.

Expressioni

Gene expression databases

ExpressionAtlasiP12309. differential.
GenevisibleiP12309. SS.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015066.

Structurei

Secondary structure

1
106
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97Combined sources
Beta strandi15 – 195Combined sources
Helixi24 – 3512Combined sources
Beta strandi42 – 476Combined sources
Helixi48 – 503Combined sources
Helixi54 – 6512Combined sources
Beta strandi72 – 754Combined sources
Beta strandi78 – 825Combined sources
Helixi83 – 919Combined sources
Helixi94 – 1029Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTEX-ray2.20A2-106[»]
ProteinModelPortaliP12309.
SMRiP12309. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12309.

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.
InParanoidiP12309.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
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.

P12309-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQAFVNSKI QPGKVVVFIK PTCPFCRKTQ ELLSQLPFKE GLLEFVDITA
60 70 80 90 100
TSDTNEIQDY LQQLTGARTV PRVFIGKECI GGCTDLESMH KRGELLTRLQ

QIGALK
Length:106
Mass (Da):11,828
Last modified:January 23, 2007 - v2
Checksum:iFEA9B18376E1D5B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AQ → QA AA sequence (PubMed:3571278).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31453 mRNA. Translation: AAA31132.1.
PIRiJQ0117. GDPG.
RefSeqiNP_999398.1. NM_214233.1.
XP_005655046.1. XM_005654989.2.
UniGeneiSsc.54096.

Genome annotation databases

EnsembliENSSSCT00000015476; ENSSSCP00000015066; ENSSSCG00000014167.
GeneIDi397463.
KEGGissc:397463.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31453 mRNA. Translation: AAA31132.1.
PIRiJQ0117. GDPG.
RefSeqiNP_999398.1. NM_214233.1.
XP_005655046.1. XM_005654989.2.
UniGeneiSsc.54096.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KTEX-ray2.20A2-106[»]
ProteinModelPortaliP12309.
SMRiP12309. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015066.

Proteomic databases

PaxDbiP12309.
PeptideAtlasiP12309.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000015476; ENSSSCP00000015066; ENSSSCG00000014167.
GeneIDi397463.
KEGGissc:397463.

Organism-specific databases

CTDi2745.

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
COG0695. LUCA.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG000283.
InParanoidiP12309.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
TreeFamiTF326994.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP12309.

Gene expression databases

ExpressionAtlasiP12309. differential.
GenevisibleiP12309. SS.

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

  1. "Cloning and sequencing the cDNA encoding pig liver thioltransferase."
    Yang Y., Gan Z.-R., Wells W.W.
    Gene 83:339-346(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Cloning and sequencing of the cDNA for pig liver thioltransferase (glutaredoxin)."
    Yang Y., Wells W.W.
    J. Cell Biol. 107:747A-747A(1988)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The primary structure of pig liver thioltransferase."
    Gan Z.-R., Wells W.W.
    J. Biol. Chem. 262:6699-6703(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-106.
    Tissue: Liver.
  4. "Crystal structure of thioltransferase at 2.2-A resolution."
    Katti S.K., Robbins A.R., Yang Y., Wells W.W.
    Protein Sci. 4:1998-2005(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiGLRX1_PIG
AccessioniPrimary (citable) accession number: P12309
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 119 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.