GRP75_CHICK
ID GRP75_CHICK Reviewed; 675 AA.
AC Q5ZM98; P84163;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 {ECO:0000250|UniProtKB:O35501}; ORFNames=RCJMB04_2m8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAG31145.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG31145.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31145.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2] {ECO:0000305}
RP IDENTIFICATION, AND MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX PubMed=16287166; DOI=10.1002/pmic.200402056;
RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA Schneider J., Palomar M.A., Linares R.;
RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT development.";
RL Proteomics 5:4946-4957(2005).
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. Associates with the mitochondrial contact
CC site and cristae organizing system (MICOS) complex (also known as MINOS
CC or MitOS complex). {ECO:0000250|UniProtKB:P38646}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P38646}.
CC -!- MASS SPECTROMETRY: Mass=73967; Mass_error=2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287166};
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000255}.
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DR EMBL; AJ719486; CAG31145.1; -; mRNA.
DR RefSeq; NP_001006147.1; NM_001006147.1.
DR AlphaFoldDB; Q5ZM98; -.
DR SMR; Q5ZM98; -.
DR BioGRID; 677728; 2.
DR STRING; 9031.ENSGALP00000003717; -.
DR PaxDb; Q5ZM98; -.
DR GeneID; 416183; -.
DR KEGG; gga:416183; -.
DR CTD; 3313; -.
DR VEuPathDB; HostDB:geneid_416183; -.
DR eggNOG; KOG0102; Eukaryota.
DR InParanoid; Q5ZM98; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q5ZM98; -.
DR PRO; PR:Q5ZM98; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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: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: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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P38646"
FT CHAIN 49..675
FT /note="Stress-70 protein, mitochondrial"
FT /id="PRO_0000223503"
SQ SEQUENCE 675 AA; 73192 MW; A2F57B18C9E7ECB7 CRC64;
MISASRAAAR LPLLLPRGGP VPAVPGLAQT FWNGLSQNVL RAASSRKYAS EAIKGAVIGI
DLGTTNSCVA VMEGKQAKVL ENSEGARTTP SVVAFTADGE RLVGMPAKRQ AVTNPHNTFY
ATKRLIGRRF DDSEVKKDIK NVPFKIVRAS NGDAWVEAHG KLYSPSQIGA FVLMKMKETA
ENYLGHPAKN AVITVPAYFN DSQRQATKDA GQISGLNVLR VINEPTAAAL AYGLDKSEDK
IIAVYDLGGG TFDISILEIQ KGVFEVKSTN GDTFLGGEDF DQALLQYIVK EFKRETSVDL
TKDNMALQRV REASEKAKCE LSSSVQTDIN LPYLTMDASG PKHLNMKLSR SQFEGIVADL
IKRTVAPCQK AMQDAEVSKS DIGEVILVGG MTRMPKVQQT VQDLFGRAPS KAVNPDEAVA
IGAAIQGGVL AGDVTDVLLL DVTPLSLGIE TLGGVFTKLI NRNTTIPTKK SQVFSTAADG
QTQVEIKVCQ GEREMASDNK LLGQFTLVGI PPAPRGVPQI EVTFDIDANG IVHVSAKDKG
TGREQQIVIQ SSGGLSKDEI ENMVKNAEKY AEEDRRRKER VEAVNLAEGI IHDTESKMEE
FKDQLPADEC NKLKEEIAKM RELLARKDTE TGENIRQAAT SLQQASLKLF EMAYKKMASE
RESSGSSGDQ KEEKQ
