ID A0A2J8N1X7_PANTR Unreviewed; 646 AA.
AC A0A2J8N1X7; A0A2I3SCB6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Heat shock cognate 71 kDa protein {ECO:0000256|ARBA:ARBA00040611};
DE AltName: Full=Heat shock 70 kDa protein 8 {ECO:0000256|ARBA:ARBA00042369};
GN Name=HSPA8 {ECO:0000313|Ensembl:ENSPTRP00000074489.1,
GN ECO:0000313|VGNC:VGNC:11823};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000074489.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000074489.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000074489.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; AACZ04006719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003313441.2; XM_003313393.4.
DR AlphaFoldDB; A0A2J8N1X7; -.
DR SMR; A0A2J8N1X7; -.
DR STRING; 9598.ENSPTRP00000074489; -.
DR PaxDb; 9598-ENSPTRP00000007540; -.
DR Ensembl; ENSPTRT00000078598.1; ENSPTRP00000074489.1; ENSPTRG00000004404.6.
DR GeneID; 451629; -.
DR KEGG; ptr:451629; -.
DR CTD; 3312; -.
DR VGNC; VGNC:11823; HSPA8.
DR GeneTree; ENSGT00950000183206; -.
DR InParanoid; A0A2J8N1X7; -.
DR OMA; KANPIMM; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000004404; Expressed in Brodmann (1909) area 10 and 21 other cell types or tissues.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; 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:0099524; C:postsynaptic cytosol; IBA:GO_Central.
DR GO; GO:0099523; C:presynaptic cytosol; IBA:GO_Central.
DR GO; GO:0101031; C:protein folding chaperone complex; IEA:Ensembl.
DR GO; GO:0000974; C:Prp19 complex; IEA:Ensembl.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; IEA:Ensembl.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; IEA:Ensembl.
DR GO; GO:1990833; F:clathrin-uncoating ATPase activity; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
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:0072318; P:clathrin coat disassembly; IBA:GO_Central.
DR GO; GO:0061738; P:late endosomal microautophagy; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:1902904; P:negative regulation of supramolecular fiber organization; IEA:Ensembl.
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:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:1990832; P:slow axonal transport; IBA:GO_Central.
DR CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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:SF379; HEAT SHOCK COGNATE 71 KDA PROTEIN; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT REGION 614..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70898 MW; 9AA27B210730670C 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 LDKCNEIINW LDKNQTAEKE EFEHQQKELE
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
//