GRP75_MESAU
ID GRP75_MESAU Reviewed; 370 AA.
AC P86233;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Stress-70 protein, mitochondrial {ECO:0000250|UniProtKB:P38646};
DE AltName: Full=75 kDa glucose-regulated protein {ECO:0000250|UniProtKB:P38646};
DE Short=GRP-75 {ECO:0000250|UniProtKB:P38646};
DE AltName: Full=Heat shock 70 kDa protein 9 {ECO:0000250|UniProtKB:P38646};
DE Flags: Fragments;
GN Name=HSPA9 {ECO:0000250|UniProtKB:P38646};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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:0000250|UniProtKB:P38646}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P38646}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000255}.
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DR AlphaFoldDB; P86233; -.
DR SMR; P86233; -.
DR IntAct; P86233; 1.
DR PRIDE; P86233; -.
DR Proteomes; UP000189706; Unplaced.
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: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 InterPro; IPR043129; ATPase_NBD.
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; 4.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Methylation; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN <1..>370
FT /note="Stress-70 protein, mitochondrial"
FT /id="PRO_0000394740"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 68
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 124
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 163
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 163
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 182
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 182
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 260
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 304
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT MOD_RES 304
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 335
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT MOD_RES 335
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38647"
FT NON_CONS 21..22
FT /evidence="ECO:0000305"
FT NON_CONS 44..45
FT /evidence="ECO:0000305"
FT NON_CONS 59..60
FT /evidence="ECO:0000305"
FT NON_CONS 68..69
FT /evidence="ECO:0000305"
FT NON_CONS 105..106
FT /evidence="ECO:0000305"
FT NON_CONS 136..137
FT /evidence="ECO:0000305"
FT NON_CONS 155..156
FT /evidence="ECO:0000305"
FT NON_CONS 170..171
FT /evidence="ECO:0000305"
FT NON_CONS 183..184
FT /evidence="ECO:0000305"
FT NON_CONS 206..207
FT /evidence="ECO:0000305"
FT NON_CONS 221..222
FT /evidence="ECO:0000305"
FT NON_CONS 238..239
FT /evidence="ECO:0000305"
FT NON_CONS 282..283
FT /evidence="ECO:0000305"
FT NON_CONS 304..305
FT /evidence="ECO:0000305"
FT NON_CONS 311..312
FT /evidence="ECO:0000305"
FT NON_CONS 345..346
FT /evidence="ECO:0000305"
FT NON_CONS 362..363
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 370
SQ SEQUENCE 370 AA; 40501 MW; 936138923CE8EE19 CRC64;
GAVVGIDLGT TNSCVAVMEG KVLENAEGAR TTPSVVAFTA DGERQAVTNP NNTFYATKRR
YDDPEVQKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKNAVIT VPAYFNDSQR
QATKDAGQIS GLNVLRSTNG DTFLGGEDFD QALLRETGVD LTKDNMALQR AQFEGIVTDL
IKRAMQDAEV SKSDIGEVIL VGGMTRVQQT VQDLFGRAPS KSQVFSTAAD GQTQVEIKEM
AGDNKLLGQF TLIGIPPAPR GVPQIEVTFD IDANGIVHVS AKEQQIVIQS SGGLSKDDIE
NMVKYAEEDR RERVEAVNMA EGIIHDTETK MEEFKDQLPA DECNKMRELL ARKDSETGEN
IRLFEMAYKK
