ID   HSP7C_DANRE             Reviewed;         649 AA.
AC   Q90473;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Heat shock cognate 71 kDa protein;
DE   AltName: Full=Heat shock 70 kDa protein 8;
GN   Name=hspa8; Synonyms=hsc70;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9204550; DOI=10.1007/bf00057591;
RA   Graser R.T., Malnar-Dragojevic D., Vincek V.;
RT   "Cloning and characterization of a 70 kd heat shock cognate (hsc70) gene
RT   from the zebrafish (Danio rerio).";
RL   Genetica 98:273-276(1996).
CC   -!- FUNCTION: Molecular chaperone implicated in a wide variety of cellular
CC       processes, including protection of the proteome from stress, folding
CC       and transport of newly synthesized polypeptides, activation of
CC       proteolysis of misfolded proteins and the formation and dissociation of
CC       protein complexes. Plays a pivotal role in the protein quality control
CC       system, ensuring the correct folding of proteins, the re-folding of
CC       misfolded proteins and controlling the targeting of proteins for
CC       subsequent degradation. This is achieved through cycles of ATP binding,
CC       ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity
CC       of HSP70 for polypeptides is regulated by its nucleotide bound state.
CC       In the ATP-bound form, it has a low affinity for substrate proteins.
CC       However, upon hydrolysis of the ATP to ADP, it undergoes a
CC       conformational change that increases its affinity for substrate
CC       proteins. HSP70 goes through repeated cycles of ATP hydrolysis and
CC       nucleotide exchange, which permits cycles of substrate binding and
CC       release. {ECO:0000250|UniProtKB:P11142}.
CC   -!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as
CC       the ATPase domain) is responsible for binding and hydrolyzing ATP. The
CC       C-terminal substrate-binding domain (SBD) (also known as peptide-
CC       binding domain) binds to the client/substrate proteins. The two domains
CC       are allosterically coupled so that, when ATP is bound to the NBD, the
CC       SBD binds relatively weakly to clients. When ADP is bound in the NBD, a
CC       conformational change enhances the affinity of the SBD for client
CC       proteins. {ECO:0000250|UniProtKB:P11142}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; L77146; AAB03704.1; -; mRNA.
DR   AlphaFoldDB; Q90473; -.
DR   SMR; Q90473; -.
DR   STRING; 7955.ENSDARP00000090766; -.
DR   PaxDb; Q90473; -.
DR   ZFIN; ZDB-GENE-990415-92; hspa8.
DR   eggNOG; KOG0101; Eukaryota.
DR   InParanoid; Q90473; -.
DR   PhylomeDB; Q90473; -.
DR   Reactome; R-DRE-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-DRE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-DRE-3371568; Attenuation phase.
DR   PRO; PR:Q90473; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0031101; P:fin regeneration; IEP:ZFIN.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:ZFIN.
DR   GO; GO:1902946; P:protein localization to early endosome; IMP:ZFIN.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IMP:ZFIN.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
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   ATP-binding; Nucleotide-binding; Reference proteome; Stress response.
FT   CHAIN           1..649
FT                   /note="Heat shock cognate 71 kDa protein"
FT                   /id="PRO_0000078276"
FT   REGION          2..386
FT                   /note="Nucleotide-binding domain (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   REGION          394..509
FT                   /note="Substrate-binding domain (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   REGION          614..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  70974 MW;  D486B85CA8E8938C CRC64;
     MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
     MNPTNTVLDA NRLNGRQFDD GVVQSDMKHW PFNVINDNSR PKVQVEYKGE SKSFYPEEIS
     SMVLTKMKEI AEAYLGKTVS NAVITVPAYS NDSQRQATKD AGTISGLNVL VIINEPTAAA
     IAYGLDKKVG AERNVLIFDL GGGSFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
     FITEFKRKHK KDISDNKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
     RFEELNADLF RGTLDPVEKA LRDAKMDKAQ IHDIVLVGGS TRIPKIQKLL QDYFNGKELN
     KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
     PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
     DANGIMNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDD VQRDKVSAKN
     GLESYAFNMK STVEDEKLKG KISDEDKQKI LDKCNEVIGW LDKNQTAERE EFEHQQKELE
     KVCNPIITKL YQSAGGMPGG MPEGMPGGFP GAGAAPGGGS SGPTIEEVD