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Q9CQM9

- GLRX3_MOUSE

UniProt

Q9CQM9 - GLRX3_MOUSE

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Protein
Glutaredoxin-3
Gene
Glrx3, Picot, Txnl2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. Has an essential function in embryogenesis.

Sites

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

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. iron-sulfur cluster binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB
  5. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. negative regulation of cardiac muscle hypertrophy Source: UniProtKB
  3. regulation of the force of heart contraction Source: UniProtKB
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1353653. 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.

GO - Cellular componenti

  1. Z disc Source: UniProtKB
  2. cell cortex Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Homozygous null mutants die in utero sometime between E12.5 and E14.5. E12.5 embryos have a smaller body size and hemorrhage in the head. Heterozygous mutants are fertile and show no abnormalities in growth and development, cardiomyocytes exhibit significantly reduced contractility.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 337336Glutaredoxin-3
PRO_0000120020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CQM9.
PaxDbiQ9CQM9.
PRIDEiQ9CQM9.

2D gel databases

REPRODUCTION-2DPAGEIPI00315550.
Q9CQM9.

PTM databases

PhosphoSiteiQ9CQM9.

Expressioni

Gene expression databases

BgeeiQ9CQM9.
CleanExiMM_GLRX3.
GenevestigatoriQ9CQM9.

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 By similarity. Interacts (via C-terminus) with CSRP3. Interacts with CSRP2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Ciapin1Q8WTY44EBI-4319195,EBI-2943068

Protein-protein interaction databases

IntActiQ9CQM9. 4 interactions.
MINTiMINT-4138889.
STRINGi10090.ENSMUSP00000066621.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi241 – 2455
Beta strandi248 – 2569
Turni257 – 2593
Helixi266 – 27510
Beta strandi280 – 2878
Helixi289 – 29911
Beta strandi306 – 3083
Beta strandi310 – 3156
Helixi317 – 32610
Helixi330 – 3345

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WIKNMR-A241-336[»]
ProteinModelPortaliQ9CQM9.
SMRiQ9CQM9. Positions 20-121, 134-234, 241-337.

Miscellaneous databases

EvolutionaryTraceiQ9CQM9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 119118Thioredoxin
Add
BLAST
Domaini144 – 23895Glutaredoxin 1
Add
BLAST
Domaini239 – 33799Glutaredoxin 2
Add
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.
Contains 1 thioredoxin domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00550000075030.
HOGENOMiHOG000165751.
HOVERGENiHBG054719.
InParanoidiQ9CQM9.
OMAiYPQLYLD.
OrthoDBiEOG7B5WX3.
PhylomeDBiQ9CQM9.
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]

Sequencei

Sequence statusi: Complete.

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

Q9CQM9-1 [UniParc]FASTAAdd to Basket

« Hide

MAAGAAEAGE AAVAVVEVGS AQQFEELLRL KTKSLLVVHF WAPWAPQCVQ    50
MNDVMAELAK EHPHVSFVKL EAEAVPEVSE KYEISSVPTF LFFKNSQKVD 100
RLDGAHAPEL TKKVQRHVSS GAFPPSTNEH LKEDLSLRLK KLTHAAPCML 150
FMKGTPQEPR CGFSKQMVEI LHKHNIQFSS FDIFSDEEVR QGLKTYSNWP 200
TYPQLYVSGE LIGGLDIIKE LEASEELDTI CPKAPKLEER LKVLTNKASV 250
MLFMKGNKQE AKCGFSKQIL EILNSTGVEY ETFDILEDEE VRQGLKTFSN 300
WPTYPQLYVR GDLVGGLDIV KELKDNGELL PILKGEN 337
Length:337
Mass (Da):37,778
Last modified:June 1, 2001 - v1
Checksum:i74A1C65621B28FA0
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761P → T in AAF28842. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF118650 mRNA. Translation: AAF28842.1.
AK010354 mRNA. Translation: BAB26874.1.
AK017371 mRNA. Translation: BAB30712.1.
AK147158 mRNA. Translation: BAE27724.1.
AK152446 mRNA. Translation: BAE31225.1.
AK152634 mRNA. Translation: BAE31376.1.
AK155190 mRNA. Translation: BAE33105.1.
AK167672 mRNA. Translation: BAE39721.1.
BC033506 mRNA. Translation: AAH33506.1.
BC087885 mRNA. Translation: AAH87885.1.
CCDSiCCDS21948.1.
RefSeqiNP_075629.2. NM_023140.4.
UniGeneiMm.267692.

Genome annotation databases

EnsembliENSMUST00000064404; ENSMUSP00000066621; ENSMUSG00000031068.
GeneIDi30926.
KEGGimmu:30926.
UCSCiuc009kew.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF118650 mRNA. Translation: AAF28842.1 .
AK010354 mRNA. Translation: BAB26874.1 .
AK017371 mRNA. Translation: BAB30712.1 .
AK147158 mRNA. Translation: BAE27724.1 .
AK152446 mRNA. Translation: BAE31225.1 .
AK152634 mRNA. Translation: BAE31376.1 .
AK155190 mRNA. Translation: BAE33105.1 .
AK167672 mRNA. Translation: BAE39721.1 .
BC033506 mRNA. Translation: AAH33506.1 .
BC087885 mRNA. Translation: AAH87885.1 .
CCDSi CCDS21948.1.
RefSeqi NP_075629.2. NM_023140.4.
UniGenei Mm.267692.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WIK NMR - A 241-336 [» ]
ProteinModelPortali Q9CQM9.
SMRi Q9CQM9. Positions 20-121, 134-234, 241-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9CQM9. 4 interactions.
MINTi MINT-4138889.
STRINGi 10090.ENSMUSP00000066621.

PTM databases

PhosphoSitei Q9CQM9.

2D gel databases

REPRODUCTION-2DPAGE IPI00315550.
Q9CQM9.

Proteomic databases

MaxQBi Q9CQM9.
PaxDbi Q9CQM9.
PRIDEi Q9CQM9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064404 ; ENSMUSP00000066621 ; ENSMUSG00000031068 .
GeneIDi 30926.
KEGGi mmu:30926.
UCSCi uc009kew.1. mouse.

Organism-specific databases

CTDi 10539.
MGIi MGI:1353653. Glrx3.

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00550000075030.
HOGENOMi HOG000165751.
HOVERGENi HBG054719.
InParanoidi Q9CQM9.
OMAi YPQLYLD.
OrthoDBi EOG7B5WX3.
PhylomeDBi Q9CQM9.
TreeFami TF314151.

Miscellaneous databases

EvolutionaryTracei Q9CQM9.
NextBioi 307324.
PROi Q9CQM9.
SOURCEi Search...

Gene expression databases

Bgeei Q9CQM9.
CleanExi MM_GLRX3.
Genevestigatori Q9CQM9.

Family and domain databases

Gene3Di 3.40.30.10. 3 hits.
InterProi IPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view ]
PANTHERi PTHR10293. PTHR10293. 1 hit.
Pfami PF00462. Glutaredoxin. 2 hits.
PF00085. Thioredoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 3 hits.
TIGRFAMsi TIGR00365. TIGR00365. 1 hit.
PROSITEi PS51354. GLUTAREDOXIN_2. 2 hits.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. "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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell and Head.
  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].
    Strain: Czech II.
    Tissue: Kidney and Mammary tumor.
  4. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 82-94.
    Tissue: Brain.
  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, OVEREXPRESSION.
  6. "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, OVEREXPRESSION, INTERACTION WITH CSRP2 AND CSRP3.
  7. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Solution structure of the picot homology 2 domain of the mouse pkc-interacting cousin of thioredoxin protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 241-336.

Entry informationi

Entry nameiGLRX3_MOUSE
AccessioniPrimary (citable) accession number: Q9CQM9
Secondary accession number(s): Q5I0V8, Q9JLZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Transgenic mice with cardiac-specific Glrx3 overexpression show that it is a potent inhibitor of cardiac hypertrophy induced by pressure overload (transverse aortic constriction). In addition, overexpression dramatically increases the ventricular function and cardiomyocyte contractility.

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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