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Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2)

 GLRX3_MOUSE             Reviewed;         337 AA.
Q9CQM9; Q5I0V8; Q9JLZ2;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
07-NOV-2018, entry version 152.
RecName: Full=Glutaredoxin-3;
AltName: Full=PKC-interacting cousin of thioredoxin;
Short=PICOT;
AltName: Full=PKC-theta-interacting protein;
Short=PKCq-interacting protein;
AltName: Full=Thioredoxin-like protein 2;
Name=Glrx3; Synonyms=Picot, Txnl2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=10636891; DOI=10.1074/jbc.275.3.1902;
Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A.;
"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.";
J. Biol. Chem. 275:1902-1909(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Head;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Kidney, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 82-94.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[5]
FUNCTION, AND OVEREXPRESSION.
PubMed=16809552; DOI=10.1161/01.RES.0000234780.06115.2c;
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.;
"PICOT inhibits cardiac hypertrophy and enhances ventricular function
and cardiomyocyte contractility.";
Circ. Res. 99:307-314(2006).
[6]
FUNCTION, SUBCELLULAR LOCATION, OVEREXPRESSION, AND INTERACTION WITH
CSRP2 AND CSRP3.
PubMed=18258855; DOI=10.1161/CIRCRESAHA.107.165985;
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.;
"PICOT attenuates cardiac hypertrophy by disrupting calcineurin-NFAT
signaling.";
Circ. Res. 102:711-719(2008).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18929570; DOI=10.1016/j.yjmcc.2008.09.124;
Cha H., Kim J.M., Oh J.G., Jeong M.H., Park C.S., Park J., Jeong H.J.,
Park B.K., Lee Y.-H., Jeong D., Yang D.K., Bernecker O.Y., Kim do H.,
Hajjar R.J., Park W.J.;
"PICOT is a critical regulator of cardiac hypertrophy and
cardiomyocyte contractility.";
J. Mol. Cell. Cardiol. 45:796-803(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
STRUCTURE BY NMR OF 241-336.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the picot homology 2 domain of the mouse pkc-
interacting cousin of thioredoxin protein.";
Submitted (NOV-2004) to the PDB data bank.
-!- FUNCTION: Together with BOLA2, acts as a cytosolic iron-sulfur
(Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster
insertion into a subset of cytosolic proteins (By similarity).
Acts as a critical negative regulator of cardiac hypertrophy and a
positive inotropic regulator (PubMed:16809552, PubMed:18258855,
PubMed:18929570). Required for hemoglobin maturation. Does not
possess any thyoredoxin activity since it lacks the conserved
motif that is essential for catalytic activity (By similarity).
{ECO:0000250|UniProtKB:O76003, ECO:0000269|PubMed:16809552,
ECO:0000269|PubMed:18258855, ECO:0000269|PubMed:18929570}.
-!- SUBUNIT: Homodimer; the homodimer is independent of 2Fe-2S
clusters. Heterotrimer; forms a heterotrimeric complex composed by
two BOLA2 molecules and one GLRX3 molecule; linked by [2Fe-2S]
clusters. Interacts (via N-terminus) with PRKCQ/PKC-theta (By
similarity). Interacts (via C-terminus) with CSRP3
(PubMed:18258855). Interacts with CSRP2 (PubMed:18258855).
{ECO:0000250|UniProtKB:O76003, ECO:0000269|PubMed:18258855}.
-!- INTERACTION:
Q8WTY4:Ciapin1; NbExp=4; IntAct=EBI-4319195, EBI-2943068;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:O76003}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:18258855}. Cytoplasm, myofibril, sarcomere, Z
line {ECO:0000269|PubMed:18258855}. Note=Under the plasma membrane
(PubMed:18258855). After PMA stimulation, GLRX3 and PRKCQ/PKC-
theta translocate to a more extended submembrane area
(PubMed:18258855). In the Z line, found associated with CSRP3
(PubMed:18258855). {ECO:0000269|PubMed:18258855}.
-!- DOMAIN: The thioredoxin domain lacks the two redox-active
cysteines. This strongly suggests that it lacks thioredoxin
activity. {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:18929570}.
-!- 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.
{ECO:0000269|PubMed:16809552, ECO:0000269|PubMed:18258855,
ECO:0000269|PubMed:18929570}.
-----------------------------------------------------------------------
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EMBL; AF118650; AAF28842.1; -; mRNA.
EMBL; AK010354; BAB26874.1; -; mRNA.
EMBL; AK017371; BAB30712.1; -; mRNA.
EMBL; AK147158; BAE27724.1; -; mRNA.
EMBL; AK152446; BAE31225.1; -; mRNA.
EMBL; AK152634; BAE31376.1; -; mRNA.
EMBL; AK155190; BAE33105.1; -; mRNA.
EMBL; AK167672; BAE39721.1; -; mRNA.
EMBL; BC033506; AAH33506.1; -; mRNA.
EMBL; BC087885; AAH87885.1; -; mRNA.
CCDS; CCDS21948.1; -.
RefSeq; NP_075629.2; NM_023140.5.
UniGene; Mm.267692; -.
UniGene; Mm.388932; -.
PDB; 1WIK; NMR; -; A=241-336.
PDBsum; 1WIK; -.
ProteinModelPortal; Q9CQM9; -.
SMR; Q9CQM9; -.
IntAct; Q9CQM9; 5.
MINT; Q9CQM9; -.
STRING; 10090.ENSMUSP00000066621; -.
iPTMnet; Q9CQM9; -.
PhosphoSitePlus; Q9CQM9; -.
SwissPalm; Q9CQM9; -.
REPRODUCTION-2DPAGE; IPI00315550; -.
REPRODUCTION-2DPAGE; Q9CQM9; -.
EPD; Q9CQM9; -.
MaxQB; Q9CQM9; -.
PaxDb; Q9CQM9; -.
PeptideAtlas; Q9CQM9; -.
PRIDE; Q9CQM9; -.
Ensembl; ENSMUST00000064404; ENSMUSP00000066621; ENSMUSG00000031068.
GeneID; 30926; -.
KEGG; mmu:30926; -.
UCSC; uc009kew.1; mouse.
CTD; 10539; -.
MGI; MGI:1353653; Glrx3.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
GeneTree; ENSGT00550000075030; -.
HOGENOM; HOG000165751; -.
HOVERGEN; HBG054719; -.
InParanoid; Q9CQM9; -.
OMA; AKCGFSR; -.
OrthoDB; EOG091G0YN0; -.
PhylomeDB; Q9CQM9; -.
TreeFam; TF314151; -.
ChiTaRS; Glrx3; mouse.
EvolutionaryTrace; Q9CQM9; -.
PRO; PR:Q9CQM9; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000031068; Expressed in 88 organ(s), highest expression level in spleen.
CleanEx; MM_GLRX3; -.
ExpressionAtlas; Q9CQM9; baseline and differential.
Genevisible; Q9CQM9; MM.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0030018; C:Z disc; IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
GO; GO:0044571; P:[2Fe-2S] cluster assembly; ISS:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
GO; GO:0002026; P:regulation of the force of heart contraction; IMP:UniProtKB.
CDD; cd03028; GRX_PICOT_like; 2.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR033658; GRX_PICOT-like.
InterPro; IPR004480; Monothiol_GRX-rel.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10293; PTHR10293; 1.
Pfam; PF00462; Glutaredoxin; 2.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 3.
TIGRFAMs; TIGR00365; TIGR00365; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 2.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O76003}.
CHAIN 2 337 Glutaredoxin-3.
/FTId=PRO_0000120020.
DOMAIN 2 119 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 144 238 Glutaredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
DOMAIN 239 337 Glutaredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
METAL 161 161 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:O76003}.
METAL 263 263 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:O76003}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O76003}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000250|UniProtKB:O76003}.
CONFLICT 76 76 P -> T (in Ref. 1; AAF28842).
{ECO:0000305}.
HELIX 241 245 {ECO:0000244|PDB:1WIK}.
STRAND 248 256 {ECO:0000244|PDB:1WIK}.
TURN 257 259 {ECO:0000244|PDB:1WIK}.
HELIX 266 275 {ECO:0000244|PDB:1WIK}.
STRAND 280 287 {ECO:0000244|PDB:1WIK}.
HELIX 289 299 {ECO:0000244|PDB:1WIK}.
STRAND 306 308 {ECO:0000244|PDB:1WIK}.
STRAND 310 315 {ECO:0000244|PDB:1WIK}.
HELIX 317 326 {ECO:0000244|PDB:1WIK}.
HELIX 330 334 {ECO:0000244|PDB:1WIK}.
SEQUENCE 337 AA; 37778 MW; 74A1C65621B28FA0 CRC64;
MAAGAAEAGE AAVAVVEVGS AQQFEELLRL KTKSLLVVHF WAPWAPQCVQ MNDVMAELAK
EHPHVSFVKL EAEAVPEVSE KYEISSVPTF LFFKNSQKVD RLDGAHAPEL TKKVQRHVSS
GAFPPSTNEH LKEDLSLRLK KLTHAAPCML FMKGTPQEPR CGFSKQMVEI LHKHNIQFSS
FDIFSDEEVR QGLKTYSNWP TYPQLYVSGE LIGGLDIIKE LEASEELDTI CPKAPKLEER
LKVLTNKASV MLFMKGNKQE AKCGFSKQIL EILNSTGVEY ETFDILEDEE VRQGLKTFSN
WPTYPQLYVR GDLVGGLDIV KELKDNGELL PILKGEN


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