ID GR75_RAT STANDARD; PRT; 679 AA. AC P48721; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE MITOCHONDRIAL STRESS-70 PROTEIN PRECURSOR (75 KD GLUCOSE REGULATED DE PROTEIN) (GRP 75) (PEPTIDE-BINDING PROTEIN 74) (PBP74) (MTHSP70) DE (MORTALIN). GN HSPA9 OR GRP75. OS RATTUS NORVEGICUS (RAT). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC RODENTIA; SCIUROGNATHI; MURIDAE; MURINAE; RATTUS. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95110439. RA WEBSTER T.J., NAYLOR D.J., HARTMAN D.J., HOJ P.B., HOOGENRAAD N.J.; RT "cDNA cloning and efficient mitochondrial import of pre-mtHSP70 from RT rat liver."; RL DNA CELL BIOL. 13:1213-1220(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 95356254. RA MASSA S.M., LONGO F.M., ZUO J., WANG S., CHEN J., SHARP F.R.; RT "Cloning of rat grp75, an hsp70-family member, and its expression in RT normal and ischemic brain."; RL J. NEUROSCI. RES. 40:807-819(1995). CC -!- FUNCTION: IMPLICATED IN THE CONTROL OF CELL PROLIFERATION AND CC CELLULAR AGING. MAY ALSO ACT AS A CHAPERONE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY. 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; S75280; G896232; -. DR EMBL; S78556; G1000439; -. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. DR PFAM; PF00012; HSP70; 1. DR HSSP; P04475; 1DKX. KW ATP-BINDING; MITOCHONDRION; TRANSIT PEPTIDE. FT TRANSIT 1 46 MITOCHONDRION (BY SIMILARITY). FT CHAIN 47 679 MITOCHONDRIAL STRESS-70 PROTEIN. FT CONFLICT 37 37 V -> A (IN REF. 2). FT CONFLICT 81 81 S -> A (IN REF. 2). FT CONFLICT 373 373 R -> A (IN REF. 2). FT CONFLICT 589 589 V -> I (IN REF. 2). SQ SEQUENCE 679 AA; 73859 MW; CF595322 CRC32; MISASRAAAA RLVGTTASRS PAAARHQDGW NGLSHEVFRF VSRRDYASEA IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN SEGARTTPSV VAFTPDGERL VGMPAKRQAV TNPNNTFYAT KRLIGRRYDD PEVQKDTKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ FEGIVTDLIK RTIAPCQKAM QDREVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIVH DTETKMEEFK DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE GSGSSSTGEQ KEDQKEEKQ //