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-JUL-1999 (Rel. 38, Last annotation update) DE GLUTAREDOXIN (THIOLTRANSFERASE). GN GLRX OR GRX. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RX MEDLINE; 94289487. 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 [2] RP SEQUENCE FROM N.A. RC TISSUE=SPLEEN; RX MEDLINE; 95154298. 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 SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE; 96220709. 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 SEQUENCE FROM N.A. RX MEDLINE; 97473512. 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 SEQUENCE. RC TISSUE=BLOOD; RX MEDLINE; 94290317. 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 [6] RP STRUCTURE BY NMR. RX MEDLINE; 98344107. 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). CC -!- FUNCTION: THE DISULFIDE BOND FUNCTIONS AS AN ELECTRON CARRIER IN CC THE GLUTATHIONE-DEPENDENT SYNTHESIS OF DEOXYRIBONUCLEOTIDES BY THE CC ENZYME RIBONUCLEOTIDE REDUCTASE. IN ADDITION, IT IS ALSO INVOLVED CC IN REDUCING SOME DISULFIDES IN A COUPLED SYSTEM WITH GLUTATHIONE CC REDUCTASE. CC -!- POLYMORPHISM: THE VARIANT IN POSITION 51 COULD BE A POLYMORPHISM, CC BUT COULD ALSO BE AN ARTIFACT OF PURIFICATION. CC -!- SIMILARITY: TO OTHER GLUTAREDOXINS AND TO BACTERIOPHAGE T4 CC THIOREDOXIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; AF115105; AAC98318.1; -. DR EMBL; AF115104; AAC98318.1; JOINED. DR EMBL; AF069668; AAC35798.1; -. DR PIR; B44568; B44568. DR PIR; S47472; S47472. DR PDB; 1JHB; 26-AUG-98. DR MIM; 600443; -. DR PFAM; PF00462; glutaredoxin; 1. DR PROSITE; PS00195; GLUTAREDOXIN; 1. KW Redox-active center; Electron transport; Acetylation; KW Deoxyribonucleotide synthesis; Polymorphism; 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. 1). SQ SEQUENCE 105 AA; 11644 MW; 91889779 CRC32; AQEFVNCKIQ PGKVVVFIKP TCPYCRRAQE ILSQLPIKQG LLEFVDITAT NHTNEIQDYL QQLTGARTVP RVFIGKDCIG GCSDLVSLQQ SGELLTRLKQ IGALQ //