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Database: UniProt
Entry: Q5ZM98
LinkDB: Q5ZM98
Original site: Q5ZM98 
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   27-MAR-2024, entry version 110.
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       Nucleus, nucleolus {ECO:0000250|UniProtKB:P38646}. Cytoplasm
CC       {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; 9031-ENSGALP00000003717; -.
DR   GeneID; 416183; -.
DR   KEGG; gga:416183; -.
DR   CTD; 3313; -.
DR   VEuPathDB; HostDB:geneid_416183; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   InParanoid; Q5ZM98; -.
DR   PhylomeDB; Q5ZM98; -.
DR   PRO; PR:Q5ZM98; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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   CDD; cd11733; HSPA9-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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; Cytoplasm; Mitochondrion; Nucleotide-binding;
KW   Nucleus; 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
//
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