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 16-OCT-2001 (Rel. 40, Last annotation update) DE Glutaredoxin (Thioltransferase). 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 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 [2] 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 [3] 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 [4] 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 [5] 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 [6] 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). 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; 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 InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR000063; Thioredoxin. 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. 1). SQ SEQUENCE 105 AA; 11644 MW; 59EC6B26965B1877 CRC64; AQEFVNCKIQ PGKVVVFIKP TCPYCRRAQE ILSQLPIKQG LLEFVDITAT NHTNEIQDYL QQLTGARTVP RVFIGKDCIG GCSDLVSLQQ SGELLTRLKQ IGALQ //