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Q9CQM9

- GLRX3_MOUSE

UniProt

Q9CQM9 - GLRX3_MOUSE

Protein

Glutaredoxin-3

Gene

Glrx3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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.By similarity3 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

    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

    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.By similarity

    GO - Cellular componenti

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

    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 – 11RemovedBy similarity
    Chaini2 – 337336Glutaredoxin-3PRO_0000120020Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy 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.By similarity1 Publication

    Binary interactionsi

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

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    337
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CQM9.

    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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761P → T in AAF28842. (PubMed:10636891)Curated

    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

    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: October 1, 2014
    This is version 122 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