GRP75_BOVIN
ID GRP75_BOVIN Reviewed; 679 AA.
AC Q3ZCH0; A5D9A6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Flags: Precursor;
GN Name=HSPA9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 probably via stabilization of ISC assembly.
CC May play a role in the control of cell proliferation and cellular
CC aging. {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:0000250|UniProtKB:P38646}.
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; BT030525; ABQ12965.1; -; mRNA.
DR EMBL; BC102334; AAI02335.1; -; mRNA.
DR RefSeq; NP_001029696.1; NM_001034524.2.
DR AlphaFoldDB; Q3ZCH0; -.
DR SMR; Q3ZCH0; -.
DR IntAct; Q3ZCH0; 1.
DR STRING; 9913.ENSBTAP00000015172; -.
DR PaxDb; Q3ZCH0; -.
DR PeptideAtlas; Q3ZCH0; -.
DR PRIDE; Q3ZCH0; -.
DR Ensembl; ENSBTAT00000015172; ENSBTAP00000015172; ENSBTAG00000011419.
DR GeneID; 517535; -.
DR KEGG; bta:517535; -.
DR CTD; 3313; -.
DR VEuPathDB; HostDB:ENSBTAG00000011419; -.
DR VGNC; VGNC:52243; HSPA9.
DR eggNOG; KOG0102; Eukaryota.
DR GeneTree; ENSGT00920000149123; -.
DR HOGENOM; CLU_005965_2_4_1; -.
DR InParanoid; Q3ZCH0; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 288077at2759; -.
DR TreeFam; TF105046; -.
DR Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:Q3ZCH0; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000011419; Expressed in adult mammalian kidney and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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:0031072; F:heat shock protein binding; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
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: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:0006611; P:protein export from nucleus; IEA:Ensembl.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chaperone; Methylation; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW 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_0000289950"
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 656..679
FT /note="Disordered"
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 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"
SQ SEQUENCE 679 AA; 73742 MW; C71EB246E9CED09B CRC64;
MISASRAAVS RFVGTAASRG PTAARHQDGW NGLSHEAFRI VSRRDYASEA IKGAVVGIDL
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT
KRLIGRRYDD PEVQKDIKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKII
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ FEGIVTDLIR
RTIAPCQKAM QDAEVSKSDI 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
GSGSSGTGEQ KDNQKEEKQ
