ID GLRX3_HUMAN Reviewed; 335 AA. AC O76003; B3KMP7; B3KMQ5; D3DRG2; Q5JV01; Q96CE0; Q9P1B0; Q9P1B1; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2003, sequence version 2. DT 31-JAN-2018, entry version 179. DE RecName: Full=Glutaredoxin-3; DE AltName: Full=PKC-interacting cousin of thioredoxin {ECO:0000303|PubMed:10636891}; DE Short=PICOT {ECO:0000303|PubMed:10636891}; DE AltName: Full=PKC-theta-interacting protein; DE Short=PKCq-interacting protein; DE AltName: Full=Thioredoxin-like protein 2; GN Name=GLRX3; Synonyms=PICOT {ECO:0000303|PubMed:10636891}, TXNL2; GN ORFNames=HUSSY-22; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH RP PRKCQ, AND VARIANTS HIS-21 AND SER-123. RC TISSUE=Liver, Spleen, and T-cell lymphoma; RX PubMed=10636891; DOI=10.1074/jbc.275.3.1902; RA Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A.; RT "Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways RT by PICOT, a novel protein kinase C-interacting protein with a RT thioredoxin homology domain."; RL J. Biol. Chem. 275:1902-1909(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Melanocyte; RX PubMed=11124703; RX DOI=10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H; RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., RA Cannata N., Zimbello R., Lanfranchi G., Valle G.; RT "Characterization of 16 novel human genes showing high similarity to RT yeast sequences."; RL Yeast 18:69-80(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-21 AND RP SER-123. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-21 AND RP SER-123. RC TISSUE=Bone marrow, and Urinary bladder; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 59-79; 115-130; 218-231; 246-253; 309-319 AND RP 323-332. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP SUBUNIT, MUTAGENESIS OF CYS-159 AND CYS-261, AND METAL. RX PubMed=20226171; DOI=10.1016/j.bbrc.2010.03.016; RA Haunhorst P., Berndt C., Eitner S., Godoy J.R., Lillig C.H.; RT "Characterization of the human monothiol glutaredoxin 3 (PICOT) as RT iron-sulfur protein."; RL Biochem. Biophys. Res. Commun. 394:372-376(2010). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP INTERACTION WITH BOLA2. RX PubMed=22309771; DOI=10.1021/bi2019089; RA Li H., Mapolelo D.T., Randeniya S., Johnson M.K., Outten C.E.; RT "Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human RT BolA2."; RL Biochemistry 51:1687-1696(2012). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-120, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP FUNCTION. RX PubMed=23615448; DOI=10.1091/mbc.E12-09-0648; RA Haunhorst P., Hanschmann E.M., Brautigam L., Stehling O., Hoffmann B., RA Muhlenhoff U., Lill R., Berndt C., Lillig C.H.; RT "Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron RT homeostasis and hemoglobin maturation."; RL Mol. Biol. Cell 24:1895-1903(2013). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP FUNCTION, AND INTERACTION WITH BOLA2. RX PubMed=26613676; DOI=10.1021/jacs.5b10592; RA Banci L., Camponeschi F., Ciofi-Baffoni S., Muzzioli R.; RT "Elucidating the molecular function of human BOLA2 in GRX3-dependent RT anamorsin maturation pathway."; RL J. Am. Chem. Soc. 137:16133-16143(2015). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH BOLA2, AND RP MUTAGENESIS OF CYS-159; 159-TRP-PRO-160; CYS-261 AND 299-TRP-PRO-300. RX PubMed=27519415; DOI=10.1074/jbc.M116.744946; RA Frey A.G., Palenchar D.J., Wildemann J.D., Philpott C.C.; RT "A glutaredoxin-BolA complex serves as an iron-sulfur cluster RT chaperone for the cytosolic cluster assembly machinery."; RL J. Biol. Chem. 291:22344-22356(2016). RN [19] RP STRUCTURE BY NMR OF 1-119. RG RIKEN structural genomics initiative (RSGI); RT "The solution structure of the thioredoxin domain of human RT thioredoxin-like protein 2."; RL Submitted (APR-2007) to the PDB data bank. CC -!- FUNCTION: Together with BOLA2, acts as a cytosolic iron-sulfur CC (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster CC insertion into a subset of cytosolic proteins (PubMed:26613676, CC PubMed:27519415). Acts as a critical negative regulator of cardiac CC hypertrophy and a positive inotropic regulator (By similarity). CC Required for hemoglobin maturation (PubMed:23615448). Does not CC possess any thyoredoxin activity since it lacks the conserved CC motif that is essential for catalytic activity. CC {ECO:0000250|UniProtKB:Q9CQM9, ECO:0000269|PubMed:23615448, CC ECO:0000269|PubMed:26613676, ECO:0000269|PubMed:27519415}. CC -!- SUBUNIT: Homodimer; the homodimer is independent of 2Fe-2S CC clusters (PubMed:27519415). Heterotrimer; forms a heterotrimeric CC complex composed by two BOLA2 molecules and one GLRX3 molecule; CC linked by [2Fe-2S] clusters (PubMed:22309771, PubMed:26613676, CC PubMed:27519415). Interacts (via N-terminus) with PRKCQ/PKC-theta CC (PubMed:10636891). Interacts (via C-terminus) with CSRP3 (By CC similarity). Interacts with CSRP2 (By similarity). CC {ECO:0000250|UniProtKB:Q9CQM9, ECO:0000269|PubMed:10636891, CC ECO:0000269|PubMed:22309771, ECO:0000269|PubMed:26613676, CC ECO:0000269|PubMed:27519415}. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-374781, EBI-374781; CC Q96Q83:ALKBH3; NbExp=3; IntAct=EBI-374781, EBI-6658697; CC Q9Y3E2:BOLA1; NbExp=9; IntAct=EBI-374781, EBI-1049556; CC Q16790:CA9; NbExp=6; IntAct=EBI-374781, EBI-12259996; CC Q13191:CBLB; NbExp=3; IntAct=EBI-374781, EBI-744027; CC Q9UFW8:CGGBP1; NbExp=3; IntAct=EBI-374781, EBI-723153; CC Q6FI81:CIAPIN1; NbExp=13; IntAct=EBI-374781, EBI-750511; CC Q6FI81-1:CIAPIN1; NbExp=2; IntAct=EBI-374781, EBI-16172762; CC Q9NWS6:FAM118A; NbExp=3; IntAct=EBI-374781, EBI-8638992; CC Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-374781, EBI-10172181; CC P28799:GRN; NbExp=7; IntAct=EBI-374781, EBI-747754; CC Q13422:IKZF1; NbExp=3; IntAct=EBI-374781, EBI-745305; CC Q15323:KRT31; NbExp=3; IntAct=EBI-374781, EBI-948001; CC O76015:KRT38; NbExp=3; IntAct=EBI-374781, EBI-1047263; CC P60412:KRTAP10-11; NbExp=4; IntAct=EBI-374781, EBI-10217483; CC P60370:KRTAP10-5; NbExp=5; IntAct=EBI-374781, EBI-10172150; CC P60410:KRTAP10-8; NbExp=7; IntAct=EBI-374781, EBI-10171774; CC P60411:KRTAP10-9; NbExp=5; IntAct=EBI-374781, EBI-10172052; CC Q9BYQ6:KRTAP4-11; NbExp=5; IntAct=EBI-374781, EBI-10302392; CC Q9BQ66:KRTAP4-12; NbExp=6; IntAct=EBI-374781, EBI-739863; CC Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-374781, EBI-10172511; CC Q9BYR0:KRTAP4-7; NbExp=3; IntAct=EBI-374781, EBI-10302547; CC Q6L8H2:KRTAP5-3; NbExp=4; IntAct=EBI-374781, EBI-11974251; CC Q6L8G9:KRTAP5-6; NbExp=3; IntAct=EBI-374781, EBI-10250562; CC P26371:KRTAP5-9; NbExp=7; IntAct=EBI-374781, EBI-3958099; CC Q9BYQ4:KRTAP9-2; NbExp=5; IntAct=EBI-374781, EBI-1044640; CC Q5TA82:LCE2D; NbExp=3; IntAct=EBI-374781, EBI-10246750; CC O60336:MAPKBP1; NbExp=5; IntAct=EBI-374781, EBI-947402; CC Q6UVY6:MOXD1; NbExp=5; IntAct=EBI-374781, EBI-7134667; CC Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-374781, EBI-945833; CC Q96PB7:OLFM3; NbExp=3; IntAct=EBI-374781, EBI-10292253; CC Q92824:PCSK5; NbExp=3; IntAct=EBI-374781, EBI-751290; CC Q99471:PFDN5; NbExp=3; IntAct=EBI-374781, EBI-357275; CC O15162:PLSCR1; NbExp=4; IntAct=EBI-374781, EBI-740019; CC Q04759:PRKCQ; NbExp=5; IntAct=EBI-374781, EBI-374762; CC Q9P2K3-2:RCOR3; NbExp=4; IntAct=EBI-374781, EBI-1504830; CC O76081:RGS20; NbExp=3; IntAct=EBI-374781, EBI-1052678; CC O76081-6:RGS20; NbExp=3; IntAct=EBI-374781, EBI-10178530; CC Q9BT81:SOX7; NbExp=3; IntAct=EBI-374781, EBI-7239117; CC O95793:STAU1; NbExp=3; IntAct=EBI-374781, EBI-358174; CC Q9BX79-6:STRA6; NbExp=4; IntAct=EBI-374781, EBI-12140683; CC P15884:TCF4; NbExp=3; IntAct=EBI-374781, EBI-533224; CC Q86YD3:TMEM25; NbExp=3; IntAct=EBI-374781, EBI-10260688; CC Q13077:TRAF1; NbExp=5; IntAct=EBI-374781, EBI-359224; CC Q9NQ86:TRIM36; NbExp=5; IntAct=EBI-374781, EBI-2341518; CC Q8IWZ5:TRIM42; NbExp=6; IntAct=EBI-374781, EBI-5235829; CC Q16851:UGP2; NbExp=3; IntAct=EBI-374781, EBI-743729; CC Q8NCP5:ZBTB44; NbExp=3; IntAct=EBI-374781, EBI-5658292; CC Q9UQR1:ZNF148; NbExp=3; IntAct=EBI-374781, EBI-2688184; CC P17027:ZNF23; NbExp=3; IntAct=EBI-374781, EBI-5657766; CC Q9BUY5:ZNF426; NbExp=3; IntAct=EBI-374781, EBI-743265; CC Q6NX49:ZNF544; NbExp=3; IntAct=EBI-374781, EBI-2841978; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000305|PubMed:27519415}. Cytoplasm, cell cortex CC {ECO:0000269|PubMed:10636891}. Cytoplasm, myofibril, sarcomere, Z CC line {ECO:0000250|UniProtKB:Q9CQM9}. Note=Under the plasma CC membrane (By similarity). After PMA stimulation, GLRX3 and CC PRKCQ/PKC-theta translocate to a more extended submembrane area CC (By similarity). In the Z line, found associated with CSRP3 (By CC similarity). {ECO:0000250|UniProtKB:Q9CQM9}. CC -!- TISSUE SPECIFICITY: Expressed in heart, spleen, testis and, to a CC lower extent, in thymus and peripheral blood leukocytes. Weakly CC expressed in lung, placenta, colon and small intestine. CC -!- DOMAIN: The thioredoxin domain lacks the two redox-active CC cysteines. This strongly suggests that it lacks thioredoxin CC activity. {ECO:0000305}. CC -!- MISCELLANEOUS: Silencing of Grx3 in HeLa cells decreases the CC activities of several cytosolic Fe/S proteins, such as ACO1, a CC major component of post-transcriptional iron regulation. As a CC consequence, Grx3-depleted cells show decreased levels of ferritin CC and increased levels of transferrin receptor, features CC characteristic of cellular iron starvation (PubMed:23615448). CC {ECO:0000305|PubMed:23615448}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF118649; AAF28841.1; -; mRNA. DR EMBL; AF118652; AAF28844.1; -; mRNA. DR EMBL; AJ010841; CAA09375.1; -; mRNA. DR EMBL; AK022131; BAG51067.1; -; mRNA. DR EMBL; AK021926; BAG51059.1; -; mRNA. DR EMBL; AL139123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49152.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49154.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49155.1; -; Genomic_DNA. DR EMBL; BC005289; AAH05289.1; -; mRNA. DR EMBL; BC014372; AAH14372.2; -; mRNA. DR CCDS; CCDS7661.1; -. DR RefSeq; NP_001186797.1; NM_001199868.1. DR RefSeq; NP_006532.2; NM_006541.4. DR UniGene; Hs.42644; -. DR PDB; 2DIY; NMR; -; A=1-117. DR PDB; 2WZ9; X-ray; 1.55 A; A=1-125. DR PDB; 2YAN; X-ray; 1.90 A; A/B=232-334. DR PDB; 3ZYW; X-ray; 1.84 A; A/B=130-232. DR PDBsum; 2DIY; -. DR PDBsum; 2WZ9; -. DR PDBsum; 2YAN; -. DR PDBsum; 3ZYW; -. DR ProteinModelPortal; O76003; -. DR SMR; O76003; -. DR BioGrid; 115793; 96. DR DIP; DIP-31306N; -. DR IntAct; O76003; 95. DR MINT; MINT-5002296; -. DR STRING; 9606.ENSP00000330836; -. DR iPTMnet; O76003; -. DR PhosphoSitePlus; O76003; -. DR BioMuta; GLRX3; -. DR REPRODUCTION-2DPAGE; IPI00008552; -. DR EPD; O76003; -. DR MaxQB; O76003; -. DR PaxDb; O76003; -. DR PeptideAtlas; O76003; -. DR PRIDE; O76003; -. DR Ensembl; ENST00000331244; ENSP00000330836; ENSG00000108010. DR Ensembl; ENST00000368644; ENSP00000357633; ENSG00000108010. DR Ensembl; ENST00000481034; ENSP00000435445; ENSG00000108010. DR GeneID; 10539; -. DR KEGG; hsa:10539; -. DR UCSC; uc001lkm.3; human. DR CTD; 10539; -. DR DisGeNET; 10539; -. DR EuPathDB; HostDB:ENSG00000108010.11; -. DR GeneCards; GLRX3; -. DR HGNC; HGNC:15987; GLRX3. DR HPA; HPA028941; -. DR MIM; 612754; gene. DR neXtProt; NX_O76003; -. DR OpenTargets; ENSG00000108010; -. DR PharmGKB; PA162389829; -. DR eggNOG; KOG0911; Eukaryota. DR eggNOG; COG0278; LUCA. DR GeneTree; ENSGT00550000075030; -. DR HOVERGEN; HBG054719; -. DR InParanoid; O76003; -. DR OMA; NNWPTFP; -. DR OrthoDB; EOG091G0YN0; -. DR PhylomeDB; O76003; -. DR TreeFam; TF314151; -. DR Reactome; R-HSA-917937; Iron uptake and transport. DR ChiTaRS; GLRX3; human. DR EvolutionaryTrace; O76003; -. DR GeneWiki; GLRX3; -. DR GenomeRNAi; 10539; -. DR PMAP-CutDB; O76003; -. DR PRO; PR:O76003; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000108010; -. DR CleanEx; HS_GLRX3; -. DR ExpressionAtlas; O76003; baseline and differential. DR Genevisible; O76003; HS. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IDA:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:UniProtKB. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:UniProtKB. DR GO; GO:0002026; P:regulation of the force of heart contraction; ISS:UniProtKB. DR CDD; cd03028; GRX_PICOT_like; 2. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR033658; GRX_PICOT-like. DR InterPro; IPR004480; Monothiol_GRX-rel. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10293; PTHR10293; 1. DR Pfam; PF00462; Glutaredoxin; 2. DR Pfam; PF00085; Thioredoxin; 1. DR SUPFAM; SSF52833; SSF52833; 3. DR TIGRFAMs; TIGR00365; TIGR00365; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 2. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000244|PubMed:25944712}. FT CHAIN 2 335 Glutaredoxin-3. FT /FTId=PRO_0000120019. FT DOMAIN 2 117 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DOMAIN 144 236 Glutaredoxin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00686}. FT DOMAIN 237 335 Glutaredoxin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00686}. FT METAL 159 159 Iron-sulfur (2Fe-2S); shared with dimeric FT partner. {ECO:0000305|PubMed:20226171, FT ECO:0000305|PubMed:27519415}. FT METAL 261 261 Iron-sulfur (2Fe-2S); shared with dimeric FT partner. {ECO:0000305|PubMed:20226171, FT ECO:0000305|PubMed:27519415}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000244|PubMed:25944712}. FT MOD_RES 117 117 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 120 120 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT VARIANT 21 21 Q -> H (in dbSNP:rs13991). FT {ECO:0000269|PubMed:10636891, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_016875. FT VARIANT 123 123 P -> S (in dbSNP:rs2274217). FT {ECO:0000269|PubMed:10636891, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_016876. FT MUTAGEN 159 159 C->S: Loss of 2Fe-2S-binding; when FT associated with S-261. Loss of 2Fe-2S- FT binding and interaction with BOLA2; when FT associated with 197-D-A-198. FT {ECO:0000269|PubMed:20226171, FT ECO:0000269|PubMed:27519415}. FT MUTAGEN 197 198 WP->DA: Loss of 2Fe-2S-binding and FT interaction with BOLA2; when associated FT with S-159. FT {ECO:0000269|PubMed:27519415}. FT MUTAGEN 261 261 C->S: Loss of 2Fe-2S-binding; when FT associated with S-159. Loss of 2Fe-2S- FT binding and interaction with BOLA2; when FT associated with 299-D-A-300. FT {ECO:0000269|PubMed:20226171, FT ECO:0000269|PubMed:27519415}. FT MUTAGEN 299 300 WP->DA: Loss of 2Fe-2S-binding and FT interaction with BOLA2; when associated FT with S-261. FT {ECO:0000269|PubMed:27519415}. FT CONFLICT 2 2 A -> E (in Ref. 2; CAA09375). FT {ECO:0000305}. FT CONFLICT 67 67 K -> R (in Ref. 3; BAG51067). FT {ECO:0000305}. FT CONFLICT 210 210 I -> T (in Ref. 3; BAG51059). FT {ECO:0000305}. FT STRAND 13 16 {ECO:0000244|PDB:2WZ9}. FT HELIX 19 28 {ECO:0000244|PDB:2WZ9}. FT TURN 29 31 {ECO:0000244|PDB:2WZ9}. FT STRAND 34 39 {ECO:0000244|PDB:2WZ9}. FT HELIX 44 59 {ECO:0000244|PDB:2WZ9}. FT STRAND 63 69 {ECO:0000244|PDB:2WZ9}. FT TURN 70 72 {ECO:0000244|PDB:2WZ9}. FT HELIX 74 79 {ECO:0000244|PDB:2WZ9}. FT STRAND 84 92 {ECO:0000244|PDB:2WZ9}. FT STRAND 95 103 {ECO:0000244|PDB:2WZ9}. FT HELIX 105 115 {ECO:0000244|PDB:2WZ9}. FT HELIX 133 141 {ECO:0000244|PDB:3ZYW}. FT STRAND 143 152 {ECO:0000244|PDB:3ZYW}. FT STRAND 154 159 {ECO:0000244|PDB:3ZYW}. FT HELIX 160 171 {ECO:0000244|PDB:3ZYW}. FT STRAND 177 180 {ECO:0000244|PDB:3ZYW}. FT HELIX 181 183 {ECO:0000244|PDB:3ZYW}. FT HELIX 185 195 {ECO:0000244|PDB:3ZYW}. FT STRAND 202 205 {ECO:0000244|PDB:3ZYW}. FT STRAND 208 211 {ECO:0000244|PDB:3ZYW}. FT HELIX 213 221 {ECO:0000244|PDB:3ZYW}. FT HELIX 225 228 {ECO:0000244|PDB:3ZYW}. FT HELIX 233 243 {ECO:0000244|PDB:2YAN}. FT STRAND 245 254 {ECO:0000244|PDB:2YAN}. FT STRAND 256 259 {ECO:0000244|PDB:2YAN}. FT HELIX 263 273 {ECO:0000244|PDB:2YAN}. FT STRAND 279 282 {ECO:0000244|PDB:2YAN}. FT HELIX 283 285 {ECO:0000244|PDB:2YAN}. FT HELIX 287 297 {ECO:0000244|PDB:2YAN}. FT STRAND 304 307 {ECO:0000244|PDB:2YAN}. FT STRAND 310 313 {ECO:0000244|PDB:2YAN}. FT HELIX 315 323 {ECO:0000244|PDB:2YAN}. FT HELIX 327 331 {ECO:0000244|PDB:2YAN}. SQ 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 //