HSP7C_RAT
ID HSP7C_RAT Reviewed; 646 AA.
AC P63018; P08109; P12225; Q4FZY7; Q62373; Q62374; Q62375;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Heat shock cognate 71 kDa protein;
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11142};
DE AltName: Full=Heat shock 70 kDa protein 8;
GN Name=Hspa8 {ECO:0000312|RGD:621725}; Synonyms=Hsc70, Hsc73;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3595567; DOI=10.1002/j.1460-2075.1987.tb04850.x;
RA Sorger P.K., Pelham H.R.B.;
RT "Cloning and expression of a gene encoding hsc73, the major hsp70-like
RT protein in unstressed rat cells.";
RL EMBO J. 6:993-998(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3939319; DOI=10.1128/mcb.5.12.3476-3483.1985;
RA O'Malley K., Mauron A., Barchas J.D., Kedes L.;
RT "Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like
RT protein.";
RL Mol. Cell. Biol. 5:3476-3483(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 4-36; 57-71; 77-108; 127-155; 160-171; 237-246;
RP 300-319; 349-357; 424-447; 452-458; 518-526; 540-550; 584-597 AND 602-609,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH DNAJC7.
RX PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
RA Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
RT "Specific interaction of the 70-kDa heat shock cognate protein with the
RT tetratricopeptide repeats.";
RL J. Biol. Chem. 274:34425-34432(1999).
RN [6]
RP INTERACTION WITH SGTA.
RX PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
RA Liou S.T., Wang C.;
RT "Small glutamine-rich tetratricopeptide repeat-containing protein is
RT composed of three structural units with distinct functions.";
RL Arch. Biochem. Biophys. 435:253-263(2005).
RN [7]
RP STRUCTURE BY NMR OF 385-543.
RX PubMed=10373374; DOI=10.1006/jmbi.1999.2776;
RA Morshauser R.C., Hu W., Wang H., Pang Y., Flynn G.C., Zuiderweg E.R.P.;
RT "High-resolution solution structure of the 18 kDa substrate-binding domain
RT of the mammalian chaperone protein Hsc70.";
RL J. Mol. Biol. 289:1387-1403(1999).
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 co-
CC chaperones have been shown to not only regulate different steps of the
CC ATPase cycle of HSP70, but they also have an individual specificity
CC such that one co-chaperone may promote folding of a substrate while
CC another may promote degradation. The affinity of HSP70 for polypeptides
CC is regulated by its nucleotide bound state. In the ATP-bound form, it
CC has a low affinity for substrate proteins. However, upon hydrolysis of
CC the ATP to ADP, it undergoes a conformational change that increases its
CC affinity for substrate proteins. HSP70 goes through repeated cycles of
CC ATP hydrolysis and nucleotide exchange, which permits cycles of
CC substrate binding and release. The HSP70-associated co-chaperones are
CC of three types: J-domain co-chaperones HSP40s (stimulate ATPase
CC hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as
CC BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-
CC bound state thereby promoting substrate release), and the TPR domain
CC chaperones such as HOPX and STUB1. Plays a critical role in
CC mitochondrial import, delivers preproteins to the mitochondrial import
CC receptor TOMM70. Acts as a repressor of transcriptional activation.
CC Inhibits the transcriptional coactivator activity of CITED1 on Smad-
CC mediated transcription. Component of the PRP19-CDC5L complex that forms
CC an integral part of the spliceosome and is required for activating pre-
CC mRNA splicing. May have a scaffolding role in the spliceosome assembly
CC as it contacts all other components of the core complex. Binds
CC bacterial lipopolysaccharide (LPS) and mediates LPS-induced
CC inflammatory response, including TNF secretion by monocytes.
CC Participates in the ER-associated degradation (ERAD) quality control
CC pathway in conjunction with J domain-containing co-chaperones and the
CC E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21.
CC {ECO:0000250|UniProtKB:P11142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P11142};
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs (By similarity). Interacts with PACRG (By
CC similarity). Interacts with HSPH1/HSP105 (By similarity). Interacts
CC with IRAK1BP1 and BAG1 (By similarity). Interacts with DNAJC7
CC (PubMed:10567422). Interacts with DNAJB12 (via J domain) (By
CC similarity). Interacts with DNAJB14 (via J domain) (By similarity).
CC Interacts (via C-terminus) with the E3 ligase STUB1 forming a 210 kDa
CC complex of one STUB1 and two HSPA8 molecules (By similarity). Interacts
CC with CITED1 (via N-terminus); the interaction suppresses the
CC association of CITED1 to p300/CBP and Smad-mediated transcription
CC transactivation (By similarity). Component of the PRP19-CDC5L splicing
CC complex composed of a core complex comprising a homotetramer of PRPF19,
CC CDC5L, PLRG1 and BCAS2, and at least three less stably associated
CC proteins CTNNBL1, CWC15 and HSPA8 (By similarity). Interacts with TRIM5
CC (By similarity). Part of a complex composed at least of ASCL2, EMSY,
CC HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this
CC complex may have a histone H3-specific methyltransferase activity (By
CC similarity). Interacts with METTL21A (By similarity). Following LPS
CC binding, may form a complex with CXCR4, GDF5 and HSP90AA1 (By
CC similarity). Interacts with PRKN (By similarity). Interacts with FOXP3
CC (By similarity). Interacts with DNAJC9 (via J domain) (By similarity).
CC Interacts with MLLT11 (By similarity). Interacts with RNF207 (By
CC similarity). Interacts with DNAJC21 (By similarity). Interacts with
CC DNAJB2 (By similarity). Interacts with TTC1 (via TPR repeats) (By
CC similarity). Interacts with SGTA (via TPR repeats) (PubMed:15708368).
CC Interacts with HSF1 (via transactivation domain) (By similarity).
CC Interacts with HOPX, STUB1, HSP40, HSP90, BAG2 and BAG3 (By
CC similarity). Interacts with DNAJC12 (By similarity). Interacts with
CC HSPC138 (By similarity). Interacts with ZMYND10 (By similarity).
CC Interacts with VGF-derived peptide TLQP-21 (By similarity). Interacts
CC with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is
CC impaired in the absence of GIMAP5 (By similarity). Interacts with
CC NLPR12 (By similarity). Interacts with TTC4 (By similarity). Interacts
CC with TOMM70; the interaction is required for preprotein mitochondrial
CC import (By similarity). May interact with DNJC9; the interaction seems
CC to be histone-dependent (By similarity). {ECO:0000250|UniProtKB:P11142,
CC ECO:0000250|UniProtKB:P63017, ECO:0000269|PubMed:10567422,
CC ECO:0000269|PubMed:15708368}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs. Translocates rapidly from the cytoplasm to the
CC nuclei, and especially to the nucleoli, upon heat shock (By
CC similarity). {ECO:0000250}.
CC -!- INDUCTION: Constitutively synthesized.
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 -!- PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P11142}.
CC -!- PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding.
CC {ECO:0000250|UniProtKB:P11142}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; Y00054; CAA68265.1; -; Genomic_DNA.
DR EMBL; M11942; AAA41354.1; -; mRNA.
DR EMBL; BC061547; AAH61547.1; -; mRNA.
DR EMBL; BC098914; AAH98914.1; -; mRNA.
DR PIR; S07197; S07197.
DR RefSeq; NP_077327.1; NM_024351.2.
DR PDB; 1CKR; NMR; -; A=385-543.
DR PDB; 1UD0; X-ray; 3.45 A; A/B/C/D=542-646.
DR PDB; 2V7Z; X-ray; 3.50 A; A/B=1-543.
DR PDB; 7HSC; NMR; -; A=385-543.
DR PDBsum; 1CKR; -.
DR PDBsum; 1UD0; -.
DR PDBsum; 2V7Z; -.
DR PDBsum; 7HSC; -.
DR AlphaFoldDB; P63018; -.
DR SMR; P63018; -.
DR BioGRID; 246629; 24.
DR CORUM; P63018; -.
DR DIP; DIP-33262N; -.
DR IntAct; P63018; 13.
DR MINT; P63018; -.
DR STRING; 10116.ENSRNOP00000058593; -.
DR iPTMnet; P63018; -.
DR PhosphoSitePlus; P63018; -.
DR SwissPalm; P63018; -.
DR World-2DPAGE; 0004:P63018; -.
DR jPOST; P63018; -.
DR PaxDb; P63018; -.
DR PRIDE; P63018; -.
DR Ensembl; ENSRNOT00000044608; ENSRNOP00000042159; ENSRNOG00000034066.
DR GeneID; 24468; -.
DR KEGG; rno:24468; -.
DR UCSC; RGD:621725; rat.
DR CTD; 3312; -.
DR RGD; 621725; Hspa8.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00950000183206; -.
DR InParanoid; P63018; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P63018; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-3371568; Attenuation phase.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8876725; Protein methylation.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR EvolutionaryTrace; P63018; -.
DR PRO; PR:P63018; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0005776; C:autophagosome; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0101031; C:chaperone complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0070062; C:extracellular exosome; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0005882; C:intermediate filament; IDA:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:1990836; C:lysosomal matrix; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0044309; C:neuron spine; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:RGD.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:ParkinsonsUK-UCL.
DR GO; GO:0099634; C:postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0031686; F:A1 adenosine receptor binding; IPI:RGD.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; ISO:RGD.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:1990833; F:clathrin-uncoating ATPase activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:1904593; F:prostaglandin binding; IPI:RGD.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IMP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0008088; P:axo-dendritic transport; IEP:RGD.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
DR GO; GO:0034605; P:cellular response to heat; IEP:RGD.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:RGD.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IDA:ParkinsonsUK-UCL.
DR GO; GO:1904764; P:chaperone-mediated autophagy translocation complex disassembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:RGD.
DR GO; GO:0072318; P:clathrin coat disassembly; IDA:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEP:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0061738; P:late endosomal microautophagy; ISO:RGD.
DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; IDA:SynGO.
DR GO; GO:0044788; P:modulation by host of viral process; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IEP:RGD.
DR GO; GO:1902904; P:negative regulation of supramolecular fiber organization; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0097214; P:positive regulation of lysosomal membrane permeability; IMP:RGD.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
DR GO; GO:1904592; P:positive regulation of protein refolding; IDA:RGD.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:RGD.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:RGD.
DR GO; GO:0042026; P:protein refolding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; ISO:RGD.
DR GO; GO:0044743; P:protein transmembrane import into intracellular organelle; IEP:RGD.
DR GO; GO:0032984; P:protein-containing complex disassembly; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR GO; GO:0061635; P:regulation of protein complex stability; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0010045; P:response to nickel cation; IEP:RGD.
DR GO; GO:1990834; P:response to odorant; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEP:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
DR GO; GO:1990832; P:slow axonal transport; IEP:RGD.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IC:SynGO.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR DisProt; DP02986; -.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR IDEAL; IID50176; -.
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 3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Isopeptide bond; Membrane;
KW Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Spliceosome;
KW Stress response; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT CHAIN 2..646
FT /note="Heat shock cognate 71 kDa protein"
FT /id="PRO_0000078273"
FT REGION 2..386
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 186..377
FT /note="Interaction with BAG1"
FT /evidence="ECO:0000250"
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"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 202..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 339..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63017"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 246
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 319
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 319
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63017"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63017"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 469
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 512
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63017"
FT MOD_RES 512
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63017"
FT MOD_RES 524
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63017"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 561
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 561
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 589
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 597
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT MOD_RES 601
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:2V7Z"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2V7Z"
FT TURN 71..75
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:2V7Z"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 257..276
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 278..288
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:2V7Z"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2V7Z"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2V7Z"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:2V7Z"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:1CKR"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 418..429
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 452..461
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:7HSC"
FT STRAND 472..481
FT /evidence="ECO:0007829|PDB:1CKR"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 485..492
FT /evidence="ECO:0007829|PDB:1CKR"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:1CKR"
FT HELIX 511..518
FT /evidence="ECO:0007829|PDB:1CKR"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:1CKR"
FT HELIX 522..527
FT /evidence="ECO:0007829|PDB:1CKR"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:1CKR"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:1CKR"
FT HELIX 542..553
FT /evidence="ECO:0007829|PDB:1UD0"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:1UD0"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:1UD0"
FT HELIX 564..595
FT /evidence="ECO:0007829|PDB:1UD0"
FT HELIX 597..610
FT /evidence="ECO:0007829|PDB:1UD0"
SQ SEQUENCE 646 AA; 70871 MW; 03A27B30E6C076ED CRC64;
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
