GRP75_CRIGR
ID GRP75_CRIGR Reviewed; 679 AA.
AC O35501;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=9260887; DOI=10.1006/excr.1997.3609;
RA Singh B., Soltys B.J., Wu Z.C., Patel H.V., Freeman K.B., Gupta R.S.;
RT "Cloning and some novel characteristics of mitochondrial Hsp70 from Chinese
RT hamster cells.";
RL Exp. Cell Res. 234:205-216(1997).
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:9260887}.
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; U92313; AAB62091.1; -; mRNA.
DR RefSeq; NP_001233758.1; NM_001246829.1.
DR AlphaFoldDB; O35501; -.
DR SMR; O35501; -.
DR STRING; 10029.NP_001233758.1; -.
DR PRIDE; O35501; -.
DR GeneID; 100689405; -.
DR KEGG; cge:100689405; -.
DR CTD; 3313; -.
DR eggNOG; KOG0102; Eukaryota.
DR OrthoDB; 288077at2759; -.
DR PRO; PR:O35501; -.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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: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; 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_0000013562"
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 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"
SQ SEQUENCE 679 AA; 73731 MW; CCE62241B12ECA70 CRC64;
MISATRAAAA RLVGTAASRT PAAARHQDGW NGLSHEAFRF VSRRDYASET IKGAVVGIDL
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT
KRLIGRRYDD PEVQKDTKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKII
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ FEGIVTDLIK
RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG
AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT
QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDLDANGIV HVSAKDKGTG
REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK
DQLPADECNK LKEEISKMRE LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE
GSGSSGTGEQ KEDQKEEKQ
