ID GLRX1_HUMAN Reviewed; 106 AA. AC P35754; Q3KQS1; Q6ICT1; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 10-JUL-2007, entry version 74. DE Glutaredoxin-1 (Thioltransferase-1) (TTase-1). GN Name=GLRX; Synonyms=GRX; 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]. RC TISSUE=Brain; RX MEDLINE=94289487; PubMed=8018729; DOI=10.1016/0167-4781(94)90019-1; RA Fernando M.R., Sumimoto H., Nanri H., Kawabata S., Iwanaga S., RA Minakami S., 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 MEDLINE=95154298; PubMed=7851394; RA Padilla C.A., Martinez-Galisteo E., Barcena J.A., Spyrou G., RA Holmgren A.; RT "Purification from placenta, amino acid sequence, structure RT comparisons and cDNA cloning of human glutaredoxin."; RL Eur. J. Biochem. 227:27-34(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=96220709; PubMed=8645179; 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 MEDLINE=97473512; 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 RT 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., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., 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 [GENOMIC DNA]. RA Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., RA Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., RA Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., RA Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [10] 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP PROTEIN SEQUENCE OF 2-106. RC TISSUE=Blood; RX MEDLINE=94290317; PubMed=8019414; RA Papov V.V., Gravina S.A., Mieyal J.J., Biemann K.; RT "The primary structure and properties of thioltransferase RT (glutaredoxin) from human red blood cells."; RL Protein Sci. 3:428-434(1994). RN [12] RP STRUCTURE BY NMR. RX MEDLINE=98344107; 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 [13] RP STRUCTURE BY NMR. RX MEDLINE=99080125; 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, RT C78S, C82S mutant and NMR solution structure of its glutathionyl mixed RT disulfide intermediate reflect catalytic specificity."; RL Biochemistry 37:17145-17156(1998). CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in CC the presence of NADPH and glutathione reductase. Reduces low CC molecular weight disulfides and proteins. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the glutaredoxin family. 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; 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; DQ026062; AAY29058.1; -; Genomic_DNA. DR EMBL; BC005304; AAH05304.1; -; mRNA. DR EMBL; BC010965; AAH10965.1; -; mRNA. DR EMBL; BC106075; AAI06076.1; -; mRNA. DR PIR; S68701; S47472. DR UniGene; Hs.28988; -. DR PDB; 1B4Q; NMR; A=1-106. DR PDB; 1JHB; NMR; @=1-106. DR Ensembl; ENSG00000173221; Homo sapiens. DR KEGG; hsa:2745; -. DR H-InvDB; HIX0005047; -. DR HGNC; HGNC:4330; GLRX. DR MIM; 600443; gene. DR PharmGKB; PA28731; -. DR Reactome; REACT_1698.1; Nucleotide metabolism. DR LinkHub; P35754; -. DR ArrayExpress; P35754; -. DR GermOnline; ENSG00000173221; Homo sapiens. DR RZPD-ProtExp; I0210; -. DR RZPD-ProtExp; RZPDo834D0524; -. DR RZPD-ProtExp; RZPDo834F061; -. DR RZPD-ProtExp; RZPDo839B0462; -. DR GO; GO:0005829; C:cytosol; TAS:UniProtKB. DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; TAS:ProtInc. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR InterPro; IPR011767; GLR_AS. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR014025; Glutaredoxin_sub. DR InterPro; IPR011899; GRX_euk. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR Pfam; PF00462; Glutaredoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR TIGRFAMs; TIGR02180; GRX_euk; 1. DR PROSITE; PS00195; GLUTAREDOXIN; 1. KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Electron transport; Redox-active center; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 106 Glutaredoxin-1. FT /FTId=PRO_0000141600. FT MOD_RES 2 2 N-acetylalanine. FT DISULFID 23 26 Redox-active. FT DISULFID 79 83 FT CONFLICT 96 96 L -> V (in Ref. 1). FT HELIX 3 6 FT STRAND 14 18 FT HELIX 23 34 FT HELIX 39 41 FT STRAND 42 46 FT TURN 47 50 FT HELIX 53 63 FT STRAND 71 74 FT STRAND 77 81 FT HELIX 82 91 FT HELIX 93 101 SQ SEQUENCE 106 AA; 11776 MW; BB86FED55967EBE2 CRC64; MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ //