HSP76_PIG
ID HSP76_PIG Reviewed; 643 AA.
AC Q04967;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Heat shock 70 kDa protein 6;
DE AltName: Full=Heat shock 70 kDa protein B';
GN Name=HSPA6; Synonyms=HSP70B';
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphocyte;
RX PubMed=7687468; DOI=10.1016/0167-4781(93)90087-t;
RA Dezeure F., Vaiman M., Chardon P.;
RT "Characterization of a polymorphic heat shock protein 70 gene in swine
RT outside the SLA major histocompatibility complex.";
RL Biochim. Biophys. Acta 1174:17-26(1993).
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:P17066}.
CC -!- INTERACTION:
CC Q04967; B1PVV8; Xeno; NbExp=5; IntAct=EBI-12556695, EBI-12556408;
CC -!- INDUCTION: By heat shock.
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:P17066}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; X68213; CAA48295.1; -; mRNA.
DR PIR; S34625; S25585.
DR RefSeq; NP_001116599.1; NM_001123127.1.
DR AlphaFoldDB; Q04967; -.
DR SMR; Q04967; -.
DR ELM; Q04967; -.
DR IntAct; Q04967; 1.
DR PeptideAtlas; Q04967; -.
DR PRIDE; Q04967; -.
DR GeneID; 396906; -.
DR KEGG; ssc:396906; -.
DR CTD; 3310; -.
DR InParanoid; Q04967; -.
DR OrthoDB; 288077at2759; -.
DR PRO; PR:Q04967; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0031625; F:ubiquitin protein ligase binding; 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 1: Evidence at protein level;
KW ATP-binding; Methylation; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..643
FT /note="Heat shock 70 kDa protein 6"
FT /id="PRO_0000078265"
FT REGION 3..388
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 396..511
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 620..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 204..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 270..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 341..344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 563
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P17066"
SQ SEQUENCE 643 AA; 71109 MW; 70C7F3BF766B4C03 CRC64;
MSAAREVAIG IDLGTTYSCV GVFQHGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ
AALNPQNTVF DAKRLIGRKF ADPTVQSDLK HWPFQVVSEG GKPKVRVSYR GEDKAFYPEE
ISSMVLSKMK ETAEAYLGQP VRHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA
AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLTIDAGVFE VKATAGDTHL GGEDFDNRLV
NHFMEEFRRK HRKDLSRNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDIVLVG GSTRIPKIQK LLQDFFNGRE
LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA
TIPTKQTQTF TTYSDNQPGV LIQVYEGERA MTRDNNLLGR FELSGIPPAP RGVPQIEVTF
DIDANGILSV TATDRSTGRA NKITITNDKG RLSKEEVERM VREADEYKVE DEAQRDRVAA
KNSLEAYVFH VKGSLHEESL RDKIPEEDRC KVQDKCQEVL TWLEHNQLAE KEEYEHQKRE
LEQICRPIFS RLYGAPGIPG GSSCGAQARQ GAPSTGPVIE EVD
