HS71L_BOVIN
ID HS71L_BOVIN Reviewed; 641 AA.
AC P0CB32;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Heat shock 70 kDa protein 1-like;
DE Short=Heat shock 70 kDa protein 1L;
GN Name=HSPA1L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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. Positive regulator of
CC PRKN translocation to damaged mitochondria.
CC {ECO:0000250|UniProtKB:P34931}.
CC -!- SUBUNIT: Interacts with PRKN. {ECO:0000250|UniProtKB:P34931}.
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:P34931}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AAFC03097356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001161367.1; NM_001167895.1.
DR RefSeq; XP_005223735.1; XM_005223678.3.
DR AlphaFoldDB; P0CB32; -.
DR SMR; P0CB32; -.
DR STRING; 9913.ENSBTAP00000035635; -.
DR PaxDb; P0CB32; -.
DR PeptideAtlas; P0CB32; -.
DR PRIDE; P0CB32; -.
DR Ensembl; ENSBTAT00000035766; ENSBTAP00000035635; ENSBTAG00000025442.
DR GeneID; 540190; -.
DR KEGG; bta:540190; -.
DR CTD; 3305; -.
DR VEuPathDB; HostDB:ENSBTAG00000025442; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000162096; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P0CB32; -.
DR OMA; ESYAYHM; -.
DR OrthoDB; 288077at2759; -.
DR TreeFam; TF105042; -.
DR Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-BTA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR PRO; PR:P0CB32; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000025442; Expressed in semen and 96 other tissues.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
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:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
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:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
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:1903955; P:positive regulation of protein targeting to mitochondrion; IEA:Ensembl.
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 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..641
FT /note="Heat shock 70 kDa protein 1-like"
FT /id="PRO_0000383115"
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 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"
SQ SEQUENCE 641 AA; 70389 MW; B44CA29796F023ED CRC64;
MAAAKGTAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ
VAMNPQNTVF DAKRLIGRKF NDPVVQSDMK LWPFQVINEG GKPKVMVSYK GEKKAFYPEE
ISSMVLTKMK ETAEAFLGYT VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA
AAIAYGLDKA GQGERHVLIF DLGGGTFDVS VLTIDDGIFE VKATAGDTHL GGEDFDNRLV
SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD
LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTVLIKRNS
TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTRDNNLLGR FDLTGIPPAP RGVPQIEVTF
DIDANGILNV TAMDKSTGKA NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA
KNALESYAFN MKSAVSDEGL QGKISESDKK KILSKCNEVL LWLEANQLAE KDEFDHKRKE
LEQVCNPIIT KLYQGGCTGP SCGTGYTPGR AATGPTIEEV D
