HSP70_CHICK
ID HSP70_CHICK Reviewed; 634 AA.
AC P08106;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Heat shock 70 kDa protein;
DE Short=HSP70;
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 [GENOMIC DNA].
RX PubMed=3017985; DOI=10.1016/s0021-9258(18)67147-9;
RA Morimoto R.I., Hunt C., Huang S.-Y., Berg K.L., Banerji S.S.;
RT "Organization, nucleotide sequence, and transcription of the chicken HSP70
RT gene.";
RL J. Biol. Chem. 261:12692-12699(1986).
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 -!- INTERACTION:
CC P08106; Q8AYS8: KCNMA1; NbExp=3; IntAct=EBI-1636307, EBI-1635766;
CC P08106; Q9DGW5: MDV005; Xeno; NbExp=5; IntAct=EBI-1636307, EBI-10889526;
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; J02579; AAA48825.1; -; Genomic_DNA.
DR PIR; A25646; A25646.
DR RefSeq; NP_001006686.1; NM_001006685.1.
DR AlphaFoldDB; P08106; -.
DR SMR; P08106; -.
DR BioGRID; 684024; 6.
DR IntAct; P08106; 2.
DR STRING; 9031.ENSGALP00000019120; -.
DR PaxDb; P08106; -.
DR PRIDE; P08106; -.
DR GeneID; 423504; -.
DR KEGG; gga:423504; -.
DR CTD; 3306; -.
DR VEuPathDB; HostDB:geneid_423504; -.
DR eggNOG; KOG0101; Eukaryota.
DR OrthoDB; 288077at2759; -.
DR PRO; PR:P08106; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0043204; C:perikaryon; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; IDA:AgBase.
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:0033142; F:nuclear progesterone receptor 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:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IDA:AgBase.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:AgBase.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA:AgBase.
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; Nucleotide-binding; Reference proteome; Stress response.
FT CHAIN 1..634
FT /note="Heat shock 70 kDa protein"
FT /id="PRO_0000078279"
FT REGION 3..389
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 397..512
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
SQ SEQUENCE 634 AA; 69751 MW; 4270F7F08D365AEB CRC64;
MSGKGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
AMNPTNTIFD AKRLIGRKYD DPTVQSDMKH WPFRVVNEGG KPKVQVEYKG EMKTFFPEEI
SSMVLTKMKE IAEAYLGKKV ETAVITVPAY FNDSQRQATK DAGTITGLNV MRIINEPTAA
AIAYGLDKKG TRAGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM
VNRFVEEFKG KHKRDNAGNK RAVRRLRTAC ERARRTLSSS TQASIEIDSL FEGIDFYTSI
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK
ELNKSINPDE AVAYGAAVQA AILMGDKSEN VQDLLLLDVT PLSLGIETAG GVMTALIKRN
TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT
FDIDANGILN VSAVDKSTGK ENKITITNDK GRLSKDDIDR MVQEAEKYKA EDEANRDRVG
AKNSLESYTY NMKQTVEDEK LKGKISDQDK QKVLDKCQEV ISSLDRNQMA EKEEYEHKQK
ELEKLCNPIV TKLYQGAGGA GAGGSGGPTI EEVD
