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Protein

Glutaredoxin-3

Gene

Glrx3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Crucial regulator of cellular iron homeostasis and hemoglobin maturation (By similarity). Critical negative regulator of cardiac hypertrophy and a positive inotropic regulator. May play a role in regulating the function of the thioredoxin system. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity
Metal bindingi263 – 2631Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-3
Alternative name(s):
PKC-interacting cousin of thioredoxin
Short name:
PICOT
PKC-theta-interacting protein
Short name:
PKCq-interacting protein
Thioredoxin-like protein 2
Gene namesi
Name:Glrx3
Synonyms:Picot, Txnl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi69414. Glrx3.

Subcellular locationi

  • Cytoplasmcell cortex By similarity
  • CytoplasmmyofibrilsarcomereZ line By similarity

  • Note: Under the plasma membrane. After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (By similarity). In the Z line, found associated with CSRP3.By similarity

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • dendrite Source: RGD
  • extracellular exosome Source: Ensembl
  • nucleus Source: RGD
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 337336Glutaredoxin-3PRO_0000120021Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9JLZ1.
PRIDEiQ9JLZ1.

PTM databases

iPTMnetiQ9JLZ1.
PhosphoSiteiQ9JLZ1.

Expressioni

Inductioni

In neonatal cardiomyocytes after exposure to the hypertrophic agonists EDN1 (ET-1) or phenylephrine (PE). In transverse aortic constriction (TAC) induced cardiac hypertrophy in adult hearts.1 Publication

Gene expression databases

ExpressionAtlasiQ9JLZ1. baseline and differential.
GenevisibleiQ9JLZ1. RN.

Interactioni

Subunit structurei

Monomer and homodimer; the homodimer is probably linked by 2 2Fe-2S clusters that may serve as a redox sensor. The monomer interacts with other proteins. Interacts (via N-terminus) with PRKCQ/PKC-theta. Interacts with CSRP2 (By similarity). Interacts (via C-terminus) with CSRP3.By similarity1 Publication

GO - Molecular functioni

  • protein kinase C binding Source: RGD

Protein-protein interaction databases

IntActiQ9JLZ1. 1 interaction.
STRINGi10116.ENSRNOP00000022406.

Structurei

3D structure databases

ProteinModelPortaliQ9JLZ1.
SMRiQ9JLZ1. Positions 20-121, 139-227, 241-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 119118ThioredoxinPROSITE-ProRule annotationAdd
BLAST
Domaini144 – 23895Glutaredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini239 – 33799Glutaredoxin 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The thioredoxin domain lacks the two redox-active cysteines. This strongly suggests that it lacks thioredoxin activity.

Sequence similaritiesi

Contains 2 glutaredoxin domains.PROSITE-ProRule annotation
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0911. Eukaryota.
COG0278. LUCA.
GeneTreeiENSGT00550000075030.
HOGENOMiHOG000165751.
HOVERGENiHBG054719.
InParanoidiQ9JLZ1.
OMAiWAPQCTQ.
OrthoDBiEOG7B5WX3.
PhylomeDBiQ9JLZ1.
TreeFamiTF314151.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 2 hits.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
TIGRFAMsiTIGR00365. TIGR00365. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 2 hits.
PS51352. THIOREDOXIN_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: Q9JLZ1-1) [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
MAAGAAEAAE AAVAVVEVGS ARQFEELLRL KTKSLLVVHF WAPWAPQCVQ
60 70 80 90 100
MNDVMAELAK EHPHVSFVKL EAEAVPEVSE KYEISSVPTF LFFKNSQKVD
110 120 130 140 150
RLDGAHAPEL TKKVQRHVSS GSFPPSTNEH VKEDLNLRLK KLTHAAPCML
160 170 180 190 200
FMKGTPQEPR CGFSKQMVEI LHKHNIQFSS FDIFSDEEVR QGLKTYSNWP
210 220 230 240 250
TYPQLYVSGE LIGGLDIIKE LEASEELDTI CPKAPKLEER LKVLTNKASV
260 270 280 290 300
MLFMKGNKQE AKCGFSKQIL EILNSTGVEY ETFDILEDEE VRQGLKTFSN
310 320 330
WPTYPQLYVR GDLVGGLDIV KELKDNGELL PILKGEN
Length:337
Mass (Da):37,849
Last modified:March 1, 2005 - v2
Checksum:iDA1E3DA9C0DBC22C
GO
Isoform 2 (identifier: Q9JLZ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     94-151: Missing.

Show »
Length:279
Mass (Da):31,361
Checksum:iDD56FE9EB5D1DA76
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei94 – 15158Missing in isoform 2. 1 PublicationVSP_012927Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118651 mRNA. Translation: AAF28843.1.
BC086381 mRNA. Translation: AAH86381.1.
RefSeqiNP_116003.2. NM_032614.2. [Q9JLZ1-1]
UniGeneiRn.3578.

Genome annotation databases

EnsembliENSRNOT00000022406; ENSRNOP00000022406; ENSRNOG00000016227. [Q9JLZ1-1]
GeneIDi58815.
KEGGirno:58815.
UCSCiRGD:69414. rat. [Q9JLZ1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118651 mRNA. Translation: AAF28843.1.
BC086381 mRNA. Translation: AAH86381.1.
RefSeqiNP_116003.2. NM_032614.2. [Q9JLZ1-1]
UniGeneiRn.3578.

3D structure databases

ProteinModelPortaliQ9JLZ1.
SMRiQ9JLZ1. Positions 20-121, 139-227, 241-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JLZ1. 1 interaction.
STRINGi10116.ENSRNOP00000022406.

PTM databases

iPTMnetiQ9JLZ1.
PhosphoSiteiQ9JLZ1.

Proteomic databases

PaxDbiQ9JLZ1.
PRIDEiQ9JLZ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022406; ENSRNOP00000022406; ENSRNOG00000016227. [Q9JLZ1-1]
GeneIDi58815.
KEGGirno:58815.
UCSCiRGD:69414. rat. [Q9JLZ1-1]

Organism-specific databases

CTDi10539.
RGDi69414. Glrx3.

Phylogenomic databases

eggNOGiKOG0911. Eukaryota.
COG0278. LUCA.
GeneTreeiENSGT00550000075030.
HOGENOMiHOG000165751.
HOVERGENiHBG054719.
InParanoidiQ9JLZ1.
OMAiWAPQCTQ.
OrthoDBiEOG7B5WX3.
PhylomeDBiQ9JLZ1.
TreeFamiTF314151.

Miscellaneous databases

NextBioi611350.
PROiQ9JLZ1.

Gene expression databases

ExpressionAtlasiQ9JLZ1. baseline and differential.
GenevisibleiQ9JLZ1. RN.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 2 hits.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
TIGRFAMsiTIGR00365. TIGR00365. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 2 hits.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain."
    Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A.
    J. Biol. Chem. 275:1902-1909(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: Sprague-Dawley.
  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 1).
    Tissue: Ovary.
  3. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-29; 82-94; 102-112; 133-138; 174-190; 311-321 AND 325-334, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. Lubec G., Chen W.-Q.
    Submitted (FEB-2007) to UniProtKB
    Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "PICOT inhibits cardiac hypertrophy and enhances ventricular function and cardiomyocyte contractility."
    Jeong D., Cha H., Kim E., Kang M., Yang D.K., Kim J.M., Yoon P.O., Oh J.G., Bernecker O.Y., Sakata S., Le T.T., Cui L., Lee Y.H., Kim do H., Woo S.H., Liao R., Hajjar R.J., Park W.J.
    Circ. Res. 99:307-314(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  6. "PICOT, protein kinase C theta-interacting protein, is a novel regulator of FcepsilonRI-mediated mast cell activation."
    Kato N., Motohashi S., Okada T., Ozawa T., Mashima K.
    Cell. Immunol. 251:62-67(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: OVEREXPRESSION.
  7. "PICOT attenuates cardiac hypertrophy by disrupting calcineurin-NFAT signaling."
    Jeong D., Kim J.M., Cha H., Oh J.G., Park J., Yun S.H., Ju E.S., Jeon E.S., Hajjar R.J., Park W.J.
    Circ. Res. 102:711-719(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CSRP3.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiGLRX3_RAT
AccessioniPrimary (citable) accession number: Q9JLZ1
Secondary accession number(s): Q5RK11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: March 1, 2005
Last modified: May 11, 2016
This is version 122 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, Direct protein sequencing, 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.