GRP75_RAT
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 03-AUG-2022, entry version 159.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 rat
RT 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 normal
RT 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 interact
RT 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 and
CC stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU.
CC Regulates erythropoiesis via stabilization of ISC assembly. May play a
CC role in the control of cell proliferation and cellular aging.
CC {ECO:0000250|UniProtKB:P38646, 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 the
CC mitochondrial contact site and cristae organizing system (MICOS)
CC complex, composed of at least MICOS10/MIC10, CHCHD3/MIC19,
CC CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13.
CC This complex was also known under the names MINOS or MitOS complex. The
CC MICOS complex associates with mitochondrial outer membrane proteins
CC SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein
CC TMEM11 and with HSPA9. Interacts with DNLZ, the interaction is required
CC to prevent self-aggregation. Interacts with TESPA1. Interacts with
CC PDPN. Interacts with NFU1, NFS1 and ISCU.
CC {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. {ECO:0000305}.
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DR EMBL; S75280; AAB33049.1; -; mRNA.
DR EMBL; S78556; AAB34982.1; -; mRNA.
DR PIR; I56581; I56581.
DR AlphaFoldDB; P48721; -.
DR SMR; P48721; -.
DR IntAct; P48721; 5.
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 jPOST; P48721; -.
DR PaxDb; P48721; -.
DR PRIDE; P48721; -.
DR ABCD; P48721; 1 sequenced antibody.
DR UCSC; RGD:1311806; rat.
DR RGD; 1311806; Hspa9.
DR eggNOG; KOG0102; Eukaryota.
DR InParanoid; P48721; -.
DR PhylomeDB; P48721; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:P48721; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO: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; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; IPI:RGD.
DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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:0006611; P:protein export from nucleus; ISO:RGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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; IPR043129; ATPase_NBD.
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 SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
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; Direct protein sequencing;
KW Methylation; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT CHAIN 47..679
FT /note="Stress-70 protein, mitochondrial"
FT /id="PRO_0000013565"
FT REGION 1..432
FT /note="Interaction with NFS1"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT REGION 432..679
FT /note="Interaction with FXN and ISCU"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT REGION 655..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 135
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 135
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 138
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 138
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 206
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 206
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 206
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 300
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 300
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 360
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 360
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 368
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 394
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 513
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 567
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 567
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 600
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 600
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 610
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 612
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 646
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 646
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT CONFLICT 37
FT /note="V -> A (in Ref. 2; AAB34982)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> S (in Ref. 1; AAB33049)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="R -> A (in Ref. 2; AAB34982)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="C -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="M -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="I -> V (in Ref. 1; AAB33049)"
FT /evidence="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
