ID GLRX_HUMAN STANDARD; PRT; 105 AA. AC P35754; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Glutaredoxin (Thioltransferase) (TTase). GN GLRX OR GRX. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP 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 SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=94289487; PubMed=8018729; RA Fernando M.R., Sumimoto H., Nanri H., Kawabata S.I., 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 SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A., AND PARTIAL 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 SEQUENCE FROM N.A. RX MEDLINE=97473512; PubMed=9332366; 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 SEQUENCE FROM N.A. RC TISSUE=Lens; RA Xing K.Y., Lou M.F.; RT "Cloning and expression of human lens thioltransferase gene."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. RC TISSUE=Skin, and Urinary bladder; RA Strausberg R.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP STRUCTURE BY NMR. RX MEDLINE=98344107; PubMed=9677297; 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 [9] RP STRUCTURE BY NMR. RX MEDLINE=99080125; PubMed=9860827; 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 RT mixed 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 -!- POLYMORPHISM: THE VARIANT IN POSITION 51 COULD BE A POLYMORPHISM, CC BUT COULD ALSO BE AN ARTIFACT OF PURIFICATION. 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; -. DR EMBL; X76648; CAA54094.1; -. DR EMBL; AF069668; AAC35798.1; -. DR EMBL; AF115105; AAC98318.1; -. DR EMBL; AF115104; AAC98318.1; JOINED. DR EMBL; AF162769; AAD43353.1; -. DR EMBL; BC005304; AAH05304.1; -. DR EMBL; BC010965; AAH10965.1; -. DR PIR; B44568; B44568. DR PIR; S47472; S47472. DR PDB; 1JHB; 26-AUG-98. DR PDB; 1B4Q; 23-DEC-99. DR Genew; HGNC:4330; GLRX. DR MIM; 600443; -. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR000063; Thiored. DR Pfam; PF00462; glutaredoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR PROSITE; PS00195; GLUTAREDOXIN; 1. KW Redox-active center; Electron transport; Acetylation; Polymorphism; KW 3D-structure. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT DISULFID 22 25 REDOX-ACTIVE. FT DISULFID 78 82 FT VARIANT 51 51 N -> D. FT /FTId=VAR_003187. 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; 11644 MW; 59EC6B26965B1877 CRC64; AQEFVNCKIQ PGKVVVFIKP TCPYCRRAQE ILSQLPIKQG LLEFVDITAT NHTNEIQDYL QQLTGARTVP RVFIGKDCIG GCSDLVSLQQ SGELLTRLKQ IGALQ //