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

 GLRX3_HUMAN             Reviewed;         335 AA.
O76003; B3KMP7; B3KMQ5; D3DRG2; Q5JV01; Q96CE0; Q9P1B0; Q9P1B1;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
26-SEP-2003, sequence version 2.
22-NOV-2017, entry version 177.
RecName: Full=Glutaredoxin-3;
AltName: Full=PKC-interacting cousin of thioredoxin {ECO:0000303|PubMed:10636891};
Short=PICOT {ECO:0000303|PubMed:10636891};
AltName: Full=PKC-theta-interacting protein;
Short=PKCq-interacting protein;
AltName: Full=Thioredoxin-like protein 2;
Name=GLRX3; Synonyms=PICOT {ECO:0000303|PubMed:10636891}, TXNL2;
ORFNames=HUSSY-22;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH
PRKCQ, AND VARIANTS HIS-21 AND SER-123.
TISSUE=Liver, Spleen, and T-cell lymphoma;
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 [MRNA].
TISSUE=Melanocyte;
PubMed=11124703;
DOI=10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H;
Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B.,
Cannata N., Zimbello R., Lanfranchi G., Valle G.;
"Characterization of 16 novel human genes showing high similarity to
yeast sequences.";
Yeast 18:69-80(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-21 AND
SER-123.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-21 AND
SER-123.
TISSUE=Bone marrow, and Urinary bladder;
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).
[7]
PROTEIN SEQUENCE OF 59-79; 115-130; 218-231; 246-253; 309-319 AND
323-332.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
SUBUNIT, MUTAGENESIS OF CYS-159 AND CYS-261, AND METAL.
PubMed=20226171; DOI=10.1016/j.bbrc.2010.03.016;
Haunhorst P., Berndt C., Eitner S., Godoy J.R., Lillig C.H.;
"Characterization of the human monothiol glutaredoxin 3 (PICOT) as
iron-sulfur protein.";
Biochem. Biophys. Res. Commun. 394:372-376(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INTERACTION WITH BOLA2.
PubMed=22309771; DOI=10.1021/bi2019089;
Li H., Mapolelo D.T., Randeniya S., Johnson M.K., Outten C.E.;
"Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human
BolA2.";
Biochemistry 51:1687-1696(2012).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-120, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
FUNCTION.
PubMed=23615448; DOI=10.1091/mbc.E12-09-0648;
Haunhorst P., Hanschmann E.M., Brautigam L., Stehling O., Hoffmann B.,
Muhlenhoff U., Lill R., Berndt C., Lillig C.H.;
"Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron
homeostasis and hemoglobin maturation.";
Mol. Biol. Cell 24:1895-1903(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
FUNCTION, AND INTERACTION WITH BOLA2.
PubMed=26613676; DOI=10.1021/jacs.5b10592;
Banci L., Camponeschi F., Ciofi-Baffoni S., Muzzioli R.;
"Elucidating the molecular function of human BOLA2 in GRX3-dependent
anamorsin maturation pathway.";
J. Am. Chem. Soc. 137:16133-16143(2015).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH BOLA2, AND
MUTAGENESIS OF CYS-159; 159-TRP-PRO-160; CYS-261 AND 299-TRP-PRO-300.
PubMed=27519415; DOI=10.1074/jbc.M116.744946;
Frey A.G., Palenchar D.J., Wildemann J.D., Philpott C.C.;
"A glutaredoxin-BolA complex serves as an iron-sulfur cluster
chaperone for the cytosolic cluster assembly machinery.";
J. Biol. Chem. 291:22344-22356(2016).
[19]
STRUCTURE BY NMR OF 1-119.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the thioredoxin domain of human
thioredoxin-like protein 2.";
Submitted (APR-2007) 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 (PubMed:26613676,
PubMed:27519415). Acts as a critical negative regulator of cardiac
hypertrophy and a positive inotropic regulator (By similarity).
Required for hemoglobin maturation (PubMed:23615448). Does not
possess any thyoredoxin activity since it lacks the conserved
motif that is essential for catalytic activity.
{ECO:0000250|UniProtKB:Q9CQM9, ECO:0000269|PubMed:23615448,
ECO:0000269|PubMed:26613676, ECO:0000269|PubMed:27519415}.
-!- SUBUNIT: Homodimer; the homodimer is independent of 2Fe-2S
clusters (PubMed:27519415). Heterotrimer; forms a heterotrimeric
complex composed by two BOLA2 molecules and one GLRX3 molecule;
linked by [2Fe-2S] clusters (PubMed:22309771, PubMed:26613676,
PubMed:27519415). Interacts (via N-terminus) with PRKCQ/PKC-theta
(PubMed:10636891). Interacts (via C-terminus) with CSRP3 (By
similarity). Interacts with CSRP2 (By similarity).
{ECO:0000250|UniProtKB:Q9CQM9, ECO:0000269|PubMed:10636891,
ECO:0000269|PubMed:22309771, ECO:0000269|PubMed:26613676,
ECO:0000269|PubMed:27519415}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-374781, EBI-374781;
Q96Q83:ALKBH3; NbExp=3; IntAct=EBI-374781, EBI-6658697;
Q9Y3E2:BOLA1; NbExp=9; IntAct=EBI-374781, EBI-1049556;
Q13191:CBLB; NbExp=3; IntAct=EBI-374781, EBI-744027;
Q9UFW8:CGGBP1; NbExp=3; IntAct=EBI-374781, EBI-723153;
Q6FI81:CIAPIN1; NbExp=13; IntAct=EBI-374781, EBI-750511;
Q6FI81-1:CIAPIN1; NbExp=2; IntAct=EBI-374781, EBI-16172762;
Q9NWS6:FAM118A; NbExp=3; IntAct=EBI-374781, EBI-8638992;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-374781, EBI-10172181;
P28799:GRN; NbExp=7; IntAct=EBI-374781, EBI-747754;
Q13422:IKZF1; NbExp=3; IntAct=EBI-374781, EBI-745305;
Q15323:KRT31; NbExp=3; IntAct=EBI-374781, EBI-948001;
O76015:KRT38; NbExp=3; IntAct=EBI-374781, EBI-1047263;
P60412:KRTAP10-11; NbExp=4; IntAct=EBI-374781, EBI-10217483;
P60370:KRTAP10-5; NbExp=5; IntAct=EBI-374781, EBI-10172150;
P60410:KRTAP10-8; NbExp=7; IntAct=EBI-374781, EBI-10171774;
P60411:KRTAP10-9; NbExp=5; IntAct=EBI-374781, EBI-10172052;
Q9BYQ6:KRTAP4-11; NbExp=5; IntAct=EBI-374781, EBI-10302392;
Q9BQ66:KRTAP4-12; NbExp=6; IntAct=EBI-374781, EBI-739863;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-374781, EBI-10172511;
Q9BYR0:KRTAP4-7; NbExp=3; IntAct=EBI-374781, EBI-10302547;
Q6L8H2:KRTAP5-3; NbExp=4; IntAct=EBI-374781, EBI-11974251;
Q6L8G9:KRTAP5-6; NbExp=3; IntAct=EBI-374781, EBI-10250562;
P26371:KRTAP5-9; NbExp=7; IntAct=EBI-374781, EBI-3958099;
Q9BYQ4:KRTAP9-2; NbExp=5; IntAct=EBI-374781, EBI-1044640;
Q5TA82:LCE2D; NbExp=3; IntAct=EBI-374781, EBI-10246750;
O60336:MAPKBP1; NbExp=5; IntAct=EBI-374781, EBI-947402;
Q6UVY6:MOXD1; NbExp=5; IntAct=EBI-374781, EBI-7134667;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-374781, EBI-945833;
Q96PB7:OLFM3; NbExp=3; IntAct=EBI-374781, EBI-10292253;
Q92824:PCSK5; NbExp=3; IntAct=EBI-374781, EBI-751290;
Q99471:PFDN5; NbExp=3; IntAct=EBI-374781, EBI-357275;
O15162:PLSCR1; NbExp=4; IntAct=EBI-374781, EBI-740019;
Q04759:PRKCQ; NbExp=5; IntAct=EBI-374781, EBI-374762;
Q9P2K3-2:RCOR3; NbExp=4; IntAct=EBI-374781, EBI-1504830;
O76081:RGS20; NbExp=3; IntAct=EBI-374781, EBI-1052678;
O76081-6:RGS20; NbExp=3; IntAct=EBI-374781, EBI-10178530;
Q9BT81:SOX7; NbExp=3; IntAct=EBI-374781, EBI-7239117;
O95793:STAU1; NbExp=3; IntAct=EBI-374781, EBI-358174;
Q9BX79-6:STRA6; NbExp=4; IntAct=EBI-374781, EBI-12140683;
P15884:TCF4; NbExp=3; IntAct=EBI-374781, EBI-533224;
Q86YD3:TMEM25; NbExp=3; IntAct=EBI-374781, EBI-10260688;
Q13077:TRAF1; NbExp=5; IntAct=EBI-374781, EBI-359224;
Q9NQ86:TRIM36; NbExp=5; IntAct=EBI-374781, EBI-2341518;
Q8IWZ5:TRIM42; NbExp=6; IntAct=EBI-374781, EBI-5235829;
Q16851:UGP2; NbExp=3; IntAct=EBI-374781, EBI-743729;
Q8NCP5:ZBTB44; NbExp=3; IntAct=EBI-374781, EBI-5658292;
Q9UQR1:ZNF148; NbExp=3; IntAct=EBI-374781, EBI-2688184;
P17027:ZNF23; NbExp=3; IntAct=EBI-374781, EBI-5657766;
Q9BUY5:ZNF426; NbExp=3; IntAct=EBI-374781, EBI-743265;
Q6NX49:ZNF544; NbExp=3; IntAct=EBI-374781, EBI-2841978;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000305|PubMed:27519415}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:10636891}. 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}.
-!- TISSUE SPECIFICITY: Expressed in heart, spleen, testis and, to a
lower extent, in thymus and peripheral blood leukocytes. Weakly
expressed in lung, placenta, colon and small intestine.
-!- DOMAIN: The thioredoxin domain lacks the two redox-active
cysteines. This strongly suggests that it lacks thioredoxin
activity. {ECO:0000305}.
-!- MISCELLANEOUS: Silencing of Grx3 in HeLa cells decreases the
activities of several cytosolic Fe/S proteins, such as ACO1, a
major component of post-transcriptional iron regulation. As a
consequence, Grx3-depleted cells show decreased levels of ferritin
and increased levels of transferrin receptor, features
characteristic of cellular iron starvation (PubMed:23615448).
{ECO:0000305|PubMed:23615448}.
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EMBL; AF118649; AAF28841.1; -; mRNA.
EMBL; AF118652; AAF28844.1; -; mRNA.
EMBL; AJ010841; CAA09375.1; -; mRNA.
EMBL; AK022131; BAG51067.1; -; mRNA.
EMBL; AK021926; BAG51059.1; -; mRNA.
EMBL; AL139123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49152.1; -; Genomic_DNA.
EMBL; CH471066; EAW49154.1; -; Genomic_DNA.
EMBL; CH471066; EAW49155.1; -; Genomic_DNA.
EMBL; BC005289; AAH05289.1; -; mRNA.
EMBL; BC014372; AAH14372.2; -; mRNA.
CCDS; CCDS7661.1; -.
RefSeq; NP_001186797.1; NM_001199868.1.
RefSeq; NP_006532.2; NM_006541.4.
UniGene; Hs.42644; -.
PDB; 2DIY; NMR; -; A=1-117.
PDB; 2WZ9; X-ray; 1.55 A; A=1-125.
PDB; 2YAN; X-ray; 1.90 A; A/B=232-334.
PDB; 3ZYW; X-ray; 1.84 A; A/B=130-232.
PDBsum; 2DIY; -.
PDBsum; 2WZ9; -.
PDBsum; 2YAN; -.
PDBsum; 3ZYW; -.
ProteinModelPortal; O76003; -.
SMR; O76003; -.
BioGrid; 115793; 96.
DIP; DIP-31306N; -.
IntAct; O76003; 95.
MINT; MINT-5002296; -.
STRING; 9606.ENSP00000330836; -.
iPTMnet; O76003; -.
PhosphoSitePlus; O76003; -.
BioMuta; GLRX3; -.
REPRODUCTION-2DPAGE; IPI00008552; -.
EPD; O76003; -.
MaxQB; O76003; -.
PaxDb; O76003; -.
PeptideAtlas; O76003; -.
PRIDE; O76003; -.
Ensembl; ENST00000331244; ENSP00000330836; ENSG00000108010.
Ensembl; ENST00000368644; ENSP00000357633; ENSG00000108010.
Ensembl; ENST00000481034; ENSP00000435445; ENSG00000108010.
GeneID; 10539; -.
KEGG; hsa:10539; -.
UCSC; uc001lkm.3; human.
CTD; 10539; -.
DisGeNET; 10539; -.
EuPathDB; HostDB:ENSG00000108010.11; -.
GeneCards; GLRX3; -.
HGNC; HGNC:15987; GLRX3.
HPA; HPA028941; -.
MIM; 612754; gene.
neXtProt; NX_O76003; -.
OpenTargets; ENSG00000108010; -.
PharmGKB; PA162389829; -.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
GeneTree; ENSGT00550000075030; -.
HOVERGEN; HBG054719; -.
InParanoid; O76003; -.
OMA; NNWPTFP; -.
OrthoDB; EOG091G0YN0; -.
PhylomeDB; O76003; -.
TreeFam; TF314151; -.
Reactome; R-HSA-917937; Iron uptake and transport.
ChiTaRS; GLRX3; human.
EvolutionaryTrace; O76003; -.
GeneWiki; GLRX3; -.
GenomeRNAi; 10539; -.
PMAP-CutDB; O76003; -.
PRO; PR:O76003; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000108010; -.
CleanEx; HS_GLRX3; -.
ExpressionAtlas; O76003; baseline and differential.
Genevisible; O76003; HS.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0044571; P:[2Fe-2S] cluster assembly; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:UniProtKB.
GO; GO:0002026; P:regulation of the force of heart contraction; ISS: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; Polymorphism; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
CHAIN 2 335 Glutaredoxin-3.
/FTId=PRO_0000120019.
DOMAIN 2 117 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 144 236 Glutaredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
DOMAIN 237 335 Glutaredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
METAL 159 159 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000305|PubMed:20226171,
ECO:0000305|PubMed:27519415}.
METAL 261 261 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000305|PubMed:20226171,
ECO:0000305|PubMed:27519415}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 21 21 Q -> H (in dbSNP:rs13991).
{ECO:0000269|PubMed:10636891,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_016875.
VARIANT 123 123 P -> S (in dbSNP:rs2274217).
{ECO:0000269|PubMed:10636891,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_016876.
MUTAGEN 159 159 C->S: Loss of 2Fe-2S-binding; when
associated with S-261. Loss of 2Fe-2S-
binding and interaction with BOLA2; when
associated with 197-D-A-198.
{ECO:0000269|PubMed:20226171,
ECO:0000269|PubMed:27519415}.
MUTAGEN 197 198 WP->DA: Loss of 2Fe-2S-binding and
interaction with BOLA2; when associated
with S-159.
{ECO:0000269|PubMed:27519415}.
MUTAGEN 261 261 C->S: Loss of 2Fe-2S-binding; when
associated with S-159. Loss of 2Fe-2S-
binding and interaction with BOLA2; when
associated with 299-D-A-300.
{ECO:0000269|PubMed:20226171,
ECO:0000269|PubMed:27519415}.
MUTAGEN 299 300 WP->DA: Loss of 2Fe-2S-binding and
interaction with BOLA2; when associated
with S-261.
{ECO:0000269|PubMed:27519415}.
CONFLICT 2 2 A -> E (in Ref. 2; CAA09375).
{ECO:0000305}.
CONFLICT 67 67 K -> R (in Ref. 3; BAG51067).
{ECO:0000305}.
CONFLICT 210 210 I -> T (in Ref. 3; BAG51059).
{ECO:0000305}.
STRAND 13 16 {ECO:0000244|PDB:2WZ9}.
HELIX 19 28 {ECO:0000244|PDB:2WZ9}.
TURN 29 31 {ECO:0000244|PDB:2WZ9}.
STRAND 34 39 {ECO:0000244|PDB:2WZ9}.
HELIX 44 59 {ECO:0000244|PDB:2WZ9}.
STRAND 63 69 {ECO:0000244|PDB:2WZ9}.
TURN 70 72 {ECO:0000244|PDB:2WZ9}.
HELIX 74 79 {ECO:0000244|PDB:2WZ9}.
STRAND 84 92 {ECO:0000244|PDB:2WZ9}.
STRAND 95 103 {ECO:0000244|PDB:2WZ9}.
HELIX 105 115 {ECO:0000244|PDB:2WZ9}.
HELIX 133 141 {ECO:0000244|PDB:3ZYW}.
STRAND 143 152 {ECO:0000244|PDB:3ZYW}.
STRAND 154 159 {ECO:0000244|PDB:3ZYW}.
HELIX 160 171 {ECO:0000244|PDB:3ZYW}.
STRAND 177 180 {ECO:0000244|PDB:3ZYW}.
HELIX 181 183 {ECO:0000244|PDB:3ZYW}.
HELIX 185 195 {ECO:0000244|PDB:3ZYW}.
STRAND 202 205 {ECO:0000244|PDB:3ZYW}.
STRAND 208 211 {ECO:0000244|PDB:3ZYW}.
HELIX 213 221 {ECO:0000244|PDB:3ZYW}.
HELIX 225 228 {ECO:0000244|PDB:3ZYW}.
HELIX 233 243 {ECO:0000244|PDB:2YAN}.
STRAND 245 254 {ECO:0000244|PDB:2YAN}.
STRAND 256 259 {ECO:0000244|PDB:2YAN}.
HELIX 263 273 {ECO:0000244|PDB:2YAN}.
STRAND 279 282 {ECO:0000244|PDB:2YAN}.
HELIX 283 285 {ECO:0000244|PDB:2YAN}.
HELIX 287 297 {ECO:0000244|PDB:2YAN}.
STRAND 304 307 {ECO:0000244|PDB:2YAN}.
STRAND 310 313 {ECO:0000244|PDB:2YAN}.
HELIX 315 323 {ECO:0000244|PDB:2YAN}.
HELIX 327 331 {ECO:0000244|PDB:2YAN}.
SEQUENCE 335 AA; 37432 MW; 46D644413D9EDFDA CRC64;
MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN EVMAELAKEL
PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL DGAHAPELTK KVQRHASSGS
FLPSANEHLK EDLNLRLKKL THAAPCMLFM KGTPQEPRCG FSKQMVEILH KHNIQFSSFD
IFSDEEVRQG LKAYSSWPTY PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK
VLTNKASVML FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP
TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN


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