ID GRP75_RAT Reviewed; 679 AA. AC P48721; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 12-DEC-2006, entry version 50. DE Stress-70 protein, mitochondrial precursor (75 kDa glucose-regulated DE protein) (GRP 75) (Peptide-binding protein 74) (PBP74) (MTHSP70) DE (Mortalin). GN Name=Hspa9; Synonyms=Grp75; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95110439; PubMed=7811387; RA Webster T.J., Naylor D.J., Hartman D.J., Hoej 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 NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95356254; PubMed=7629893; 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). RN [3] RP PROTEIN SEQUENCE OF 80-98 AND 484-503. RX PubMed=2372296; RA Akamizu T., Saji M., Kohn L.D.; RT "A microsequencing approach to identify proteins which appear to RT interact with thyrotropin in rat FRTL-5 thyroid cells."; RL Biochem. Biophys. Res. Commun. 170:351-358(1990). RN [4] RP PROTEIN SEQUENCE OF 577-595. RA Lubec G., Vishwanath V.; RL Submitted (SEP-2006) to Swiss-Prot. CC -!- FUNCTION: Implicated in the control of cell proliferation and CC cellular aging. May also act as a chaperone. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the heat shock protein 70 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; S75280; AAB33049.1; -; mRNA. DR EMBL; S78556; AAB34982.1; -; mRNA. DR PIR; I56581; I56581. DR HSSP; P04475; 1DG4. DR IntAct; P48721; -. DR GermOnline; ENSRNOG00000019525; Rattus norvegicus. DR Ensembl; ENSRNOG00000019525; Rattus norvegicus. DR RGD; 1311806; Hspa9a. DR ArrayExpress; P48721; -. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW Acetylation; ATP-binding; Chaperone; Direct protein sequencing; KW Mitochondrion; Nucleotide-binding; Transit peptide. FT TRANSIT 1 46 Mitochondrion (By similarity). FT CHAIN 47 679 Stress-70 protein. FT /FTId=PRO_0000013565. FT MOD_RES 288 288 N6-acetyllysine (By similarity). FT MOD_RES 300 300 N6-acetyllysine (By similarity). FT MOD_RES 360 360 N6-acetyllysine (By similarity). FT CONFLICT 37 37 V -> A (in Ref. 2). FT CONFLICT 81 81 A -> S (in Ref. 1). FT CONFLICT 373 373 R -> A (in Ref. 2). FT CONFLICT 487 487 C -> T (in Ref. 3). FT CONFLICT 493 493 M -> Q (in Ref. 3). FT CONFLICT 589 589 I -> V (in Ref. 1). SQ SEQUENCE 679 AA; 73858 MW; 4616EDE5307691A4 CRC64; MISASRAAAA RLVGTTASRS PAAARHQDGW NGLSHEVFRF VSRRDYASEA IKGAVVGIDL GTTNSCVAVM EGKQAKVLEN AEGARTTPSV 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 AVNMAEGIIH DTETKMEEFK DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE GSGSSSTGEQ KEDQKEEKQ //