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-DEC-1998 (REL. 37, LAST ANNOTATION UPDATE) DE GLUTAREDOXIN (THIOLTRANSFERASE). GN GLRX OR GRX. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC 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 RT acid-reducing activity from human neutrophils: identification as RT glutaredoxin."; RL BIOCHEM. J. 315:931-938(1996). RN [4] 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 [5] 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 RT reduced 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; G643695; -. DR EMBL; X76648; G531405; -. DR EMBL; U40574; G1172131; -. DR EMBL; S82191; G1839483; -. DR PIR; B44568; B44568. DR PIR; S47472; S47472. DR PDB; 1JHB; 26-AUG-98. DR MIM; 600443; -. DR PROSITE; PS00195; GLUTAREDOXIN; 1. DR PFAM; PF00462; 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 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 //