HSP7C_CHICK
ID HSP7C_CHICK Reviewed; 646 AA.
AC O73885;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Heat shock cognate 71 kDa protein;
DE AltName: Full=Heat shock 70 kDa protein 8;
GN Name=HSPA8; Synonyms=HSC70;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=9707581; DOI=10.1073/pnas.95.17.9950;
RA de la Rosa E.J., Vega-Nunez E., Morales A.V., Serna J., Rubio E.,
RA de Pablo F.;
RT "Modulation of the chaperone heat shock cognate 70 by embryonic
RT (pro)insulin correlates with prevention of apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9950-9955(1998).
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 (By similarity). May play a role in regulating apoptosis during
CC embryonic development. {ECO:0000250|UniProtKB:P11142,
CC ECO:0000269|PubMed:9707581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Translocates
CC rapidly from the cytoplasm to the nuclei, and especially to the
CC nucleoli, upon heat shock. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: First detected at 0.5 days of embryonic
CC development (at protein level). Detected at higher levels from 1 to 2.5
CC days of embryonic development (at protein level). First detected at 0.5
CC days of embryonic development. Levels increase strongly from 1 to 2.5
CC days of embryonic development. {ECO:0000269|PubMed:9707581}.
CC -!- INDUCTION: Up-regulated by insulin in cultured embryos.
CC {ECO:0000269|PubMed:9707581}.
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; AJ004940; CAA06233.1; -; mRNA.
DR RefSeq; NP_990334.1; NM_205003.2.
DR AlphaFoldDB; O73885; -.
DR BMRB; O73885; -.
DR SMR; O73885; -.
DR BioGRID; 676126; 3.
DR IntAct; O73885; 1.
DR STRING; 9031.ENSGALP00000010510; -.
DR PaxDb; O73885; -.
DR GeneID; 395853; -.
DR KEGG; gga:395853; -.
DR CTD; 3312; -.
DR VEuPathDB; HostDB:geneid_395853; -.
DR eggNOG; KOG0101; Eukaryota.
DR InParanoid; O73885; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; O73885; -.
DR PRO; PR:O73885; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IMP:AgBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IMP:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0099524; C:postsynaptic cytosol; IBA:GO_Central.
DR GO; GO:0099523; C:presynaptic cytosol; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; 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:1990833; F:clathrin-uncoating ATPase activity; IBA:GO_Central.
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:0051219; F:phosphoprotein binding; IPI:AgBase.
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:1904764; P:chaperone-mediated autophagy translocation complex disassembly; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEP:AgBase.
DR GO; GO:0048568; P:embryonic organ development; IEP:AgBase.
DR GO; GO:0007369; P:gastrulation; IEP:AgBase.
DR GO; GO:0061738; P:late endosomal microautophagy; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IBA:GO_Central.
DR GO; GO:1990832; P:slow axonal transport; 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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..646
FT /note="Heat shock cognate 71 kDa protein"
FT /id="PRO_0000304725"
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..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70827 MW; 2151332ED42C5B9B CRC64;
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTNTVFDA KRLIGRRFDD SVVQSDMKHW PFTVVNDAGR PKVQVEYKGE TKSFYPEEIS
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQGTKD AGTIAGLNVL RIINEPTAAA
IAYGLDKKVG AERNLLIFDL GGGTFDVSIL TIENGIFEVK STAGDTHLGG EDFDNRLVNH
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
RFEKLNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
SLDSYAFNMK ATVEDEKLPG KILDEDHQNI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
