GLRX1_HUMAN
ID GLRX1_HUMAN Reviewed; 106 AA.
AC P35754; B2R4L2; Q3KQS1; Q6ICT1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Glutaredoxin-1;
DE AltName: Full=Thioltransferase-1;
DE Short=TTase-1;
GN Name=GLRX; Synonyms=GRX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8018729; DOI=10.1016/0167-4781(94)90019-1;
RA Fernando M.R., Sumimoto H., Nanri H., Kawabata S., Iwanaga S., Minakami S.,
RA Fukumaki Y., Takeshige K.;
RT "Cloning and sequencing of the cDNA encoding human glutaredoxin.";
RL Biochim. Biophys. Acta 1218:229-231(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=7851394; DOI=10.1111/j.1432-1033.1995.tb20356.x;
RA Padilla C.A., Martinez-Galisteo E., Barcena J.A., Spyrou G., Holmgren A.;
RT "Purification from placenta, amino acid sequence, structure comparisons and
RT cDNA cloning of human glutaredoxin.";
RL Eur. J. Biochem. 227:27-34(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8645179; DOI=10.1042/bj3150931;
RA Park J.B., Levine M.;
RT "Purification, cloning and expression of dehydroascorbic acid-reducing
RT activity from human neutrophils: identification as glutaredoxin.";
RL Biochem. J. 315:931-938(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9332366; DOI=10.1016/s0378-1119(97)00262-x;
RA Park J.B., Levine M.;
RT "The human glutaredoxin gene: determination of its organization,
RT transcription start point, and promoter analysis.";
RL Gene 197:189-193(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=11222536;
RA Qiao F., Xing K.Y., Liu A., Ehlers N., Raghavachari N., Lou M.F.;
RT "Human lens thioltransferase: cloning, purification, and function.";
RL Invest. Ophthalmol. Vis. Sci. 42:743-751(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, Skin, 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP PROTEIN SEQUENCE OF 2-106.
RC TISSUE=Blood;
RX PubMed=8019414; DOI=10.1002/pro.5560030307;
RA Papov V.V., Gravina S.A., Mieyal J.J., Biemann K.;
RT "The primary structure and properties of thioltransferase (glutaredoxin)
RT from human red blood cells.";
RL Protein Sci. 3:428-434(1994).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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., Buerckstuemmer T.,
RA 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 [16]
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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA 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 STRUCTURE BY NMR.
RX PubMed=9677297; DOI=10.1006/jmbi.1998.1913;
RA Sun C., Berardi M.J., Bushweller J.H.;
RT "The NMR solution structure of human glutaredoxin in the fully reduced
RT form.";
RL J. Mol. Biol. 280:687-701(1998).
RN [19]
RP STRUCTURE BY NMR.
RX PubMed=9860827; DOI=10.1021/bi9806504;
RA Yang Y., Jao S.C., Nanduri S., Starke D.W., Mieyal J.J., Qin J.;
RT "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S,
RT C82S mutant and NMR solution structure of its glutathionyl mixed disulfide
RT intermediate reflect catalytic specificity.";
RL Biochemistry 37:17145-17156(1998).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins.
CC -!- INTERACTION:
CC P35754; Q9BVG3: TRIM62; NbExp=5; IntAct=EBI-3905236, EBI-6929619;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/glrx/";
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DR EMBL; D21238; BAA04769.1; -; mRNA.
DR EMBL; X76648; CAA54094.1; -; mRNA.
DR EMBL; AF069668; AAC35798.1; -; mRNA.
DR EMBL; AF115105; AAC98318.1; -; Genomic_DNA.
DR EMBL; AF115104; AAC98318.1; JOINED; Genomic_DNA.
DR EMBL; AF162769; AAD43353.1; -; mRNA.
DR EMBL; BT006689; AAP35335.1; -; mRNA.
DR EMBL; CR450312; CAG29308.1; -; mRNA.
DR EMBL; CR542165; CAG46962.1; -; mRNA.
DR EMBL; AK311868; BAG34809.1; -; mRNA.
DR EMBL; DQ026062; AAY29058.1; -; Genomic_DNA.
DR EMBL; CH471084; EAW96056.1; -; Genomic_DNA.
DR EMBL; BC005304; AAH05304.1; -; mRNA.
DR EMBL; BC010965; AAH10965.1; -; mRNA.
DR EMBL; BC106075; AAI06076.1; -; mRNA.
DR CCDS; CCDS4078.1; -.
DR PIR; S68701; S47472.
DR RefSeq; NP_001112362.1; NM_001118890.1.
DR RefSeq; NP_001230587.1; NM_001243658.1.
DR RefSeq; NP_001230588.1; NM_001243659.1.
DR RefSeq; NP_002055.1; NM_002064.2.
DR PDB; 1B4Q; NMR; -; A=2-106.
DR PDB; 1JHB; NMR; -; A=1-106.
DR PDB; 4RQR; X-ray; 1.08 A; A=2-106.
DR PDBsum; 1B4Q; -.
DR PDBsum; 1JHB; -.
DR PDBsum; 4RQR; -.
DR AlphaFoldDB; P35754; -.
DR SMR; P35754; -.
DR BioGRID; 109007; 49.
DR IntAct; P35754; 10.
DR MINT; P35754; -.
DR STRING; 9606.ENSP00000369314; -.
DR BindingDB; P35754; -.
DR DrugBank; DB00143; Glutathione.
DR GlyGen; P35754; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P35754; -.
DR PhosphoSitePlus; P35754; -.
DR BioMuta; GLRX; -.
DR DMDM; 1346143; -.
DR UCD-2DPAGE; P35754; -.
DR EPD; P35754; -.
DR jPOST; P35754; -.
DR MassIVE; P35754; -.
DR MaxQB; P35754; -.
DR PaxDb; P35754; -.
DR PeptideAtlas; P35754; -.
DR PRIDE; P35754; -.
DR ProteomicsDB; 55150; -.
DR Antibodypedia; 3264; 271 antibodies from 31 providers.
DR DNASU; 2745; -.
DR Ensembl; ENST00000237858.11; ENSP00000237858.6; ENSG00000173221.14.
DR Ensembl; ENST00000379979.8; ENSP00000369314.4; ENSG00000173221.14.
DR Ensembl; ENST00000505427.1; ENSP00000427353.1; ENSG00000173221.14.
DR Ensembl; ENST00000508780.5; ENSP00000422708.1; ENSG00000173221.14.
DR Ensembl; ENST00000512469.2; ENSP00000424636.2; ENSG00000173221.14.
DR GeneID; 2745; -.
DR KEGG; hsa:2745; -.
DR MANE-Select; ENST00000237858.11; ENSP00000237858.6; NM_001118890.2; NP_001112362.1.
DR UCSC; uc003kln.5; human.
DR CTD; 2745; -.
DR DisGeNET; 2745; -.
DR GeneCards; GLRX; -.
DR HGNC; HGNC:4330; GLRX.
DR HPA; ENSG00000173221; Tissue enhanced (skeletal).
DR MIM; 600443; gene.
DR neXtProt; NX_P35754; -.
DR OpenTargets; ENSG00000173221; -.
DR PharmGKB; PA28731; -.
DR VEuPathDB; HostDB:ENSG00000173221; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00900000141068; -.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; P35754; -.
DR OMA; KPGHLEC; -.
DR OrthoDB; 1535999at2759; -.
DR PhylomeDB; P35754; -.
DR TreeFam; TF326994; -.
DR BioCyc; MetaCyc:HS04268-MON; -.
DR PathwayCommons; P35754; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; P35754; -.
DR SignaLink; P35754; -.
DR BioGRID-ORCS; 2745; 34 hits in 1016 CRISPR screens.
DR ChiTaRS; GLRX; human.
DR EvolutionaryTrace; P35754; -.
DR GeneWiki; GLRX; -.
DR GenomeRNAi; 2745; -.
DR Pharos; P35754; Tbio.
DR PRO; PR:P35754; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P35754; protein.
DR Bgee; ENSG00000173221; Expressed in jejunal mucosa and 200 other tissues.
DR ExpressionAtlas; P35754; baseline and differential.
DR Genevisible; P35754; HS.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; EXP:Reactome.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; TAS:BHF-UCL.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0045838; P:positive regulation of membrane potential; IDA:BHF-UCL.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0080058; P:protein deglutathionylation; TAS:BHF-UCL.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8019414,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..106
FT /note="Glutaredoxin-1"
FT /id="PRO_0000141600"
FT DOMAIN 3..106
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 9
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QUH0"
FT DISULFID 23..26
FT /note="Redox-active"
FT DISULFID 79..83
FT VARIANT 47
FT /note="D -> Y (in dbSNP:rs4767)"
FT /id="VAR_049189"
FT CONFLICT 96
FT /note="L -> V (in Ref. 1; BAA04769)"
FT /evidence="ECO:0000305"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:4RQR"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4RQR"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:4RQR"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4RQR"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:4RQR"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:4RQR"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4RQR"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4RQR"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:4RQR"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:4RQR"
SQ SEQUENCE 106 AA; 11776 MW; BB86FED55967EBE2 CRC64;
MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY
LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ
