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 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAREDOXIN (THIOLTRANSFERASE). GN GRX. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE. RC TISSUE=BLOOD; RA PAPOV V.V., GRAVINA S.A., MIEYAL J.J., BIEMANN K.; RL PROTEIN SCI. 3:428-434(1994). 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 GLUTATIONE CC REDUCTASE. CC -!- SIMILARITY: TO OTHER GLUTAREDOXINS AND TO BACTERIOPHAGE T4 CC THIOREDOXIN. CC -!- POLYMORPHISM: THE VARIANT IN POSITION 51 COULD BE A POLYMORPHISM, CC BUT COULD ALSO BE AN ARTIFACT OF PURIFICATION. 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 PIR; B44568; B44568. DR PROSITE; PS00195; GLUTAREDOXIN. KW REDOX-ACTIVE CENTER; ELECTRON TRANSPORT; ACETYLATION; KW DEOXYRIBONUCLEOTIDE SYNTHESIS; POLYMORPHISM. FT MOD_RES 1 1 ACETYLATION. FT DISULFID 22 25 REDOX-ACTIVE. FT DISULFID 78 82 FT VARIANT 51 51 N -> D. SQ SEQUENCE 105 AA; 11644 MW; 54382 CN; AQEFVNCKIQ PGKVVVFIKP TCPYCRRAQE ILSQLPIKQG LLEFVDITAT NHTNEIQDYL QQLTGARTVP RVFIGKDCIG GCSDLVSLQQ SGELLTRLKQ IGALQ //