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

 GLRX3_RAT               Reviewed;         337 AA.
Q9JLZ1; Q5RK11;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 2.
22-NOV-2017, entry version 135.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley;
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] (ISOFORM 1).
TISSUE=Ovary;
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).
[3]
PROTEIN SEQUENCE OF 23-29; 82-94; 102-112; 133-138; 174-190; 311-321
AND 325-334, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[4]
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
Lubec G., Chen W.-Q.;
Submitted (FEB-2007) to UniProtKB.
[5]
FUNCTION, AND INDUCTION.
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]
OVEREXPRESSION.
PubMed=18479680; DOI=10.1016/j.cellimm.2008.04.005;
Kato N., Motohashi S., Okada T., Ozawa T., Mashima K.;
"PICOT, protein kinase C theta-interacting protein, is a novel
regulator of FcepsilonRI-mediated mast cell activation.";
Cell. Immunol. 251:62-67(2008).
[7]
FUNCTION, AND INTERACTION WITH CSRP3.
STRAIN=Sprague-Dawley;
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).
-!- 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).
Required for hemoglobin maturation (By similarity). 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:0000250|UniProtKB:Q9CQM9,
ECO:0000269|PubMed:16809552, ECO:0000269|PubMed:18258855}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:O76003, ECO:0000250|UniProtKB:Q9CQM9,
ECO:0000269|PubMed:18258855}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:O76003}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:O76003}. Cytoplasm, myofibril, sarcomere, Z
line {ECO:0000250|UniProtKB:Q9CQM9}. Note=Under the plasma
membrane (By similarity). 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). {ECO:0000250|UniProtKB:Q9CQM9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JLZ1-1; Sequence=Displayed;
Name=2;
IsoId=Q9JLZ1-2; Sequence=VSP_012927;
-!- INDUCTION: 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. {ECO:0000269|PubMed:16809552}.
-!- DOMAIN: The thioredoxin domain lacks the two redox-active
cysteines. This strongly suggests that it lacks thioredoxin
activity.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF118651; AAF28843.1; -; mRNA.
EMBL; BC086381; AAH86381.1; -; mRNA.
RefSeq; NP_116003.2; NM_032614.2. [Q9JLZ1-1]
UniGene; Rn.3578; -.
ProteinModelPortal; Q9JLZ1; -.
SMR; Q9JLZ1; -.
IntAct; Q9JLZ1; 1.
STRING; 10116.ENSRNOP00000022406; -.
iPTMnet; Q9JLZ1; -.
PhosphoSitePlus; Q9JLZ1; -.
PaxDb; Q9JLZ1; -.
PRIDE; Q9JLZ1; -.
Ensembl; ENSRNOT00000022406; ENSRNOP00000022406; ENSRNOG00000016227. [Q9JLZ1-1]
GeneID; 58815; -.
KEGG; rno:58815; -.
UCSC; RGD:69414; rat. [Q9JLZ1-1]
CTD; 10539; -.
RGD; 69414; Glrx3.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
GeneTree; ENSGT00550000075030; -.
HOGENOM; HOG000165751; -.
HOVERGEN; HBG054719; -.
InParanoid; Q9JLZ1; -.
OMA; NNWPTFP; -.
OrthoDB; EOG091G0YN0; -.
PhylomeDB; Q9JLZ1; -.
TreeFam; TF314151; -.
PRO; PR:Q9JLZ1; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000016227; -.
ExpressionAtlas; Q9JLZ1; baseline and differential.
Genevisible; Q9JLZ1; RN.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0030018; C:Z disc; ISO:RGD.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IDA:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0044571; P:[2Fe-2S] cluster assembly; ISS:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:RGD.
GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
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;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.4}.
CHAIN 2 337 Glutaredoxin-3.
/FTId=PRO_0000120021.
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:0000269|Ref.4}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000250|UniProtKB:O76003}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:O76003}.
VAR_SEQ 94 151 Missing (in isoform 2).
{ECO:0000303|PubMed:10636891}.
/FTId=VSP_012927.
SEQUENCE 337 AA; 37849 MW; DA1E3DA9C0DBC22C CRC64;
MAAGAAEAAE AAVAVVEVGS ARQFEELLRL KTKSLLVVHF WAPWAPQCVQ MNDVMAELAK
EHPHVSFVKL EAEAVPEVSE KYEISSVPTF LFFKNSQKVD RLDGAHAPEL TKKVQRHVSS
GSFPPSTNEH VKEDLNLRLK KLTHAAPCML FMKGTPQEPR CGFSKQMVEI LHKHNIQFSS
FDIFSDEEVR QGLKTYSNWP TYPQLYVSGE LIGGLDIIKE LEASEELDTI CPKAPKLEER
LKVLTNKASV MLFMKGNKQE AKCGFSKQIL EILNSTGVEY ETFDILEDEE VRQGLKTFSN
WPTYPQLYVR GDLVGGLDIV KELKDNGELL PILKGEN


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