HSP7C_ORYLA
ID HSP7C_ORYLA Reviewed; 686 AA.
AC Q9W6Y1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Heat shock cognate 71 kDa protein;
DE AltName: Full=Hsc70.1;
GN Name=hsc70;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=HB32;
RX PubMed=7632444; DOI=10.1266/jjg.70.423;
RA Arai A., Naruse K., Mitani H., Shima A.;
RT "Cloning and characterization of cDNAs for 70-kDa heat-shock proteins
RT (Hsp70) from two fish species of the genus Oryzias.";
RL Jpn. J. Genet. 70:423-433(1995).
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 for polypeptides is regulated by its nucleotide bound state. In the
CC ATP-bound form, it has a low affinity for substrate proteins. However,
CC upon hydrolysis of the ATP to ADP, it undergoes a conformational change
CC that increases its affinity for substrate proteins. It goes through
CC repeated cycles of ATP hydrolysis and nucleotide exchange, which
CC permits cycles of substrate binding and release.
CC {ECO:0000250|UniProtKB:P0DMV8}.
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:P0DMV8}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D13669; BAA76887.1; -; mRNA.
DR RefSeq; NP_001098270.1; NM_001104800.1.
DR AlphaFoldDB; Q9W6Y1; -.
DR SMR; Q9W6Y1; -.
DR STRING; 8090.ENSORLP00000006701; -.
DR PRIDE; Q9W6Y1; -.
DR GeneID; 100049425; -.
DR KEGG; ola:100049425; -.
DR CTD; 3312; -.
DR eggNOG; KOG0101; Eukaryota.
DR InParanoid; Q9W6Y1; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
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:0042026; P:protein refolding; IBA:GO_Central.
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..686
FT /note="Heat shock cognate 71 kDa protein"
FT /id="PRO_0000078278"
FT REGION 2..386
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 394..507
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
SQ SEQUENCE 686 AA; 76169 MW; 9D89A2C7662FABB4 CRC64;
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTNTVFDA KRLIGRRFDD HVVQSDMNDW PFNVINDNTR PKVQVEYKGE TKSFYPEEVS
SMVLTKMKEI AEAYLGKTVN NAVITVPAYF NDSQRQATKD AGTISGLNVL RIINEPTAAA
IAYGLDKKVG SERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
FIAEFKRKYK KDISDNKRAV RRLRSACERA KRTLSSSTQA SIEIDSLYEG VDFYTSITRA
RFEELNADLF RGTLDPVEKS LRDAKMDKGQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
PTKQTQTFTT YSDNQPGVLN QVYEVGAMTK DNNLLGKFEL TGIPPALWCP QIEVTFDIDA
NGIMNVSAVD KSTGKENKIT ITNDKGRLSK EDIERMVQEA EKYKAEDDVQ RDKVSAKNGL
ESYAFNMKST VEDEKLAGKI SDEDKQKILD KCNEVISWLD KNQTAERDEY VHQQKELEKV
CNPIITKLYQ SAGGMPGGCQ RECQEVSLEL VVLLAVALLD QPLKKLIKHS MTSPSKIFTK
KTLFKCNMQS IKSVMRLNQF PFITIT
