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 19-MAR-2014, entry version 114. DE RecName: Full=Stress-70 protein, mitochondrial; DE AltName: Full=75 kDa glucose-regulated protein; DE Short=GRP-75; DE AltName: Full=Heat shock 70 kDa protein 9; DE AltName: Full=Mortalin; DE AltName: Full=Peptide-binding protein 74; DE Short=PBP74; DE AltName: Full=mtHSP70; DE Flags: Precursor; GN Name=Hspa9; Synonyms=Grp75, Hspa9a; 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 PubMed=7811387; DOI=10.1089/dna.1994.13.1213; 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 PubMed=7629893; DOI=10.1002/jnr.490400612; 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; DOI=10.1016/0006-291X(90)91281-V; 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 188-202; 266-284; 499-513 AND 577-595, AND MASS RP SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Vishwanath V., Afjehi-Sadat L.; RL Submitted (NOV-2006) to UniProtKB. CC -!- FUNCTION: Implicated in the control of cell proliferation and CC cellular aging. May also act as a chaperone. CC -!- SUBUNIT: Interacts with FXN. Interacts with HSCB (By similarity). CC Component of the MINOS/MitOS complex, that includes IMMT, HSPA9 CC and CHCHD3 and associates with mitochondrial outer membrane CC proteins SAMM50, MTX1 and MTX2. Interacts with DNLZ, the CC interaction is required to prevent self-aggregation (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus, nucleolus (By CC similarity). 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 UniGene; Rn.7535; -. DR ProteinModelPortal; P48721; -. DR SMR; P48721; 55-580. DR BioGrid; 253601; 5. DR IntAct; P48721; 3. DR MINT; MINT-4592308; -. DR STRING; 10116.ENSRNOP00000026696; -. DR PhosphoSite; P48721; -. DR World-2DPAGE; 0004:P48721; -. DR PaxDb; P48721; -. DR PRIDE; P48721; -. DR UCSC; RGD:1311806; rat. DR RGD; 1311806; Hspa9. DR eggNOG; COG0443; -. DR HOGENOM; HOG000228136; -. DR HOVERGEN; HBG051845; -. DR InParanoid; P48721; -. DR NextBio; 632983; -. DR PRO; PR:P48721; -. DR Genevestigator; P48721; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR HAMAP; MF_00332; DnaK; 1. DR InterPro; IPR012725; Chaperone_DnaK. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR013126; Hsp_70_fam. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR TIGRFAMs; TIGR02350; prok_dnaK; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; Chaperone; Complete proteome; KW Direct protein sequencing; Mitochondrion; Nucleotide-binding; Nucleus; KW Reference proteome; Transit peptide. FT TRANSIT 1 46 Mitochondrion (By similarity). FT CHAIN 47 679 Stress-70 protein, mitochondrial. FT /FTId=PRO_0000013565. FT MOD_RES 76 76 N6-acetyllysine (By similarity). FT MOD_RES 135 135 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 135 135 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 138 138 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 138 138 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 143 143 N6-acetyllysine (By similarity). FT MOD_RES 206 206 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 206 206 N6-malonyllysine; alternate (By FT similarity). FT MOD_RES 206 206 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 234 234 N6-acetyllysine (By similarity). FT MOD_RES 288 288 N6-acetyllysine (By similarity). FT MOD_RES 300 300 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 300 300 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 360 360 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 360 360 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 368 368 N6-succinyllysine (By similarity). FT MOD_RES 394 394 N6-succinyllysine (By similarity). FT MOD_RES 567 567 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 567 567 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 600 600 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 600 600 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 610 610 N6-succinyllysine (By similarity). FT MOD_RES 612 612 N6-acetyllysine (By similarity). FT MOD_RES 646 646 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 646 646 N6-succinyllysine; alternate (By FT similarity). FT CONFLICT 37 37 V -> A (in Ref. 2; AAB34982). FT CONFLICT 81 81 A -> S (in Ref. 1; AAB33049). FT CONFLICT 373 373 R -> A (in Ref. 2; AAB34982). FT CONFLICT 487 487 C -> T (in Ref. 3; AA sequence). FT CONFLICT 493 493 M -> Q (in Ref. 3; AA sequence). FT CONFLICT 589 589 I -> V (in Ref. 1; AAB33049). 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 //