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 23-MAY-2018, entry version 140. 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; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. 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 RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Vishwanath V., Afjehi-Sadat L.; RL Submitted (NOV-2006) to UniProtKB. CC -!- FUNCTION: Chaperone protein which plays an important role in CC mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with CC and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and CC ISCU. Regulates erythropoiesis via stabilization of ISC assembly. CC May play a role in the control of cell proliferation and cellular CC aging. {ECO:0000250|UniProtKB:P38646, CC ECO:0000250|UniProtKB:P38647}. CC -!- SUBUNIT: Interacts strongly with the intermediate form of FXN and CC weakly with its mature form. Interacts with HSCB. Associates with CC the mitochondrial contact site and cristae organizing system CC (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CC CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and CC QIL1/MIC13. This complex was also known under the names MINOS or CC MitOS complex. The MICOS complex associates with mitochondrial CC outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, CC mitochondrial inner membrane protein TMEM11 and with HSPA9. CC Interacts with DNLZ, the interaction is required to prevent self- CC aggregation. Interacts with TESPA1. Interacts with PDPN. Interacts CC with NFU1, NFS1 and ISCU. {ECO:0000250|UniProtKB:P38646}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7811387}. CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P38646}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000305}. 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; -. DR IntAct; P48721; 4. DR MINT; P48721; -. DR STRING; 10116.ENSRNOP00000026696; -. DR CarbonylDB; P48721; -. DR iPTMnet; P48721; -. DR PhosphoSitePlus; P48721; -. DR SwissPalm; P48721; -. DR World-2DPAGE; 0004:P48721; -. DR PaxDb; P48721; -. DR PRIDE; P48721; -. DR UCSC; RGD:1311806; rat. DR RGD; 1311806; Hspa9. DR eggNOG; KOG0102; Eukaryota. DR eggNOG; COG0443; LUCA. DR HOGENOM; HOG000228136; -. DR HOVERGEN; HBG051845; -. DR InParanoid; P48721; -. DR PhylomeDB; P48721; -. DR PRO; PR:P48721; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; IDA:RGD. DR GO; GO:0005739; C:mitochondrion; IDA:RGD. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD. DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB. DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD. DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; ISS:UniProtKB. DR GO; GO:1903707; P:negative regulation of hemopoiesis; ISS:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0045646; P:regulation of erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:0051593; P:response to folic acid; IEP:RGD. DR GO; GO:0097068; P:response to thyroxine; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR Gene3D; 1.20.1270.10; -; 1. DR Gene3D; 2.60.34.10; -; 1. DR HAMAP; MF_00332; DnaK; 1. DR InterPro; IPR012725; Chaperone_DnaK. DR InterPro; IPR018181; Heat_shock_70_CS. DR InterPro; IPR029048; HSP70_C_sf. DR InterPro; IPR029047; HSP70_peptide-bd_sf. DR InterPro; IPR013126; Hsp_70_fam. DR PANTHER; PTHR19375; PTHR19375; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF100920; SSF100920; 1. 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; Methylation; Mitochondrion; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Transit peptide. FT TRANSIT 1 46 Mitochondrion. FT {ECO:0000250|UniProtKB:P38646}. FT CHAIN 47 679 Stress-70 protein, mitochondrial. FT /FTId=PRO_0000013565. FT REGION 1 432 Interaction with NFS1. FT {ECO:0000250|UniProtKB:P38646}. FT REGION 432 679 Interaction with FXN and ISCU. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 76 76 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 87 87 Phosphothreonine. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 135 135 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 135 135 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 138 138 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 138 138 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 143 143 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 206 206 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 206 206 N6-malonyllysine; alternate. FT {ECO:0000250}. FT MOD_RES 206 206 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 234 234 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 288 288 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 300 300 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 300 300 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 360 360 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 360 360 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 368 368 N6-succinyllysine. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 394 394 N6-succinyllysine. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 408 408 Phosphoserine. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 513 513 Omega-N-methylarginine. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 567 567 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 567 567 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 600 600 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 600 600 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 610 610 N6-succinyllysine. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 612 612 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P38647}. FT MOD_RES 646 646 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P38646}. FT MOD_RES 646 646 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P38647}. FT CONFLICT 37 37 V -> A (in Ref. 2; AAB34982). FT {ECO:0000305}. FT CONFLICT 81 81 A -> S (in Ref. 1; AAB33049). FT {ECO:0000305}. FT CONFLICT 373 373 R -> A (in Ref. 2; AAB34982). FT {ECO:0000305}. FT CONFLICT 487 487 C -> T (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 493 493 M -> Q (in Ref. 3; AA sequence). FT {ECO:0000305}. FT CONFLICT 589 589 I -> V (in Ref. 1; AAB33049). FT {ECO:0000305}. 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 //