ID GLRX1_HUMAN STANDARD; PRT; 105 AA. AC P35754; Q6ICT1; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) 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; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP PROTEIN SEQUENCE. 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 [2] 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 [3] 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 [4] 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 [5] 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 [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin, and Urinary bladder; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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: Cytoplasmic. 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 PIR; S68701; S47472. DR PDB; 1B4Q; NMR; A=1-105. DR PDB; 1JHB; NMR; @=1-105. DR Ensembl; ENSG00000118990; Homo sapiens. DR HGNC; HGNC:4330; GLRX. DR H-InvDB; HIX0005047; -. DR Reactome; P35754; -. DR MIM; 600443; -. DR LinkHub; P35754; -. DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; TAS. DR InterPro; IPR011767; GLR_AS. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR011899; GRX_euk. DR InterPro; IPR006663; Thioredox_dom2. DR InterPro; IPR012336; Thioredoxin-like. DR InterPro; IPR012335; Thioredoxin_fold. DR Pfam; PF00462; Glutaredoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR TIGRFAMs; TIGR02180; GRX_euk; 1. DR PROSITE; PS00195; GLUTAREDOXIN; 1. KW 3D-structure; Acetylation; Direct protein sequencing; KW Electron transport; Redox-active center; Transport. FT INIT_MET 0 0 FT MOD_RES 1 1 N-acetylalanine. FT DISULFID 22 25 Redox-active. FT DISULFID 78 82 FT CONFLICT 95 95 L -> V (in Ref. 2). FT HELIX 3 8 FT TURN 11 12 FT STRAND 14 18 FT TURN 20 21 FT HELIX 23 33 FT TURN 34 34 FT TURN 39 41 FT STRAND 42 46 FT HELIX 53 64 FT STRAND 71 74 FT TURN 75 76 FT STRAND 77 80 FT HELIX 82 90 FT HELIX 93 100 FT TURN 101 102 SQ SEQUENCE 105 AA; 11645 MW; 59EC6B26965B1877 CRC64; AQEFVNCKIQ PGKVVVFIKP TCPYCRRAQE ILSQLPIKQG LLEFVDITAT NHTNEIQDYL QQLTGARTVP RVFIGKDCIG GCSDLVSLQQ SGELLTRLKQ IGALQ //