ID   HS71L_MESAU             Reviewed;         117 AA.
AC   P86237;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Heat shock 70 kDa protein 1-like {ECO:0000250|UniProtKB:P55063};
DE            Short=Heat shock 70 kDa protein 1L {ECO:0000250|UniProtKB:P55063};
DE   Flags: Fragments;
GN   Name=HSPA1L {ECO:0000250|UniProtKB:P55063};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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   -!- TISSUE SPECIFICITY: Detected at higher levels in caput epididymal
CC       spermatazoa than in cauda epididymal spermatazoa (at protein level).
CC       {ECO:0000269|PubMed:20400973}.
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:0000255}.
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DR   AlphaFoldDB; P86237; -.
DR   SMR; P86237; -.
DR   STRING; 10036.XP_005086889.1; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 3.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           <1..>117
FT                   /note="Heat shock 70 kDa protein 1-like"
FT                   /id="PRO_0000394743"
FT   BINDING         72..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         84..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000305"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000305"
FT   NON_CONS        39..40
FT                   /evidence="ECO:0000305"
FT   NON_CONS        66..67
FT                   /evidence="ECO:0000305"
FT   NON_CONS        73..74
FT                   /evidence="ECO:0000305"
FT   NON_CONS        87..88
FT                   /evidence="ECO:0000305"
FT   NON_CONS        100..101
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         117
SQ   SEQUENCE   117 AA;  13146 MW;  B88BA0992295417E CRC64;
     TTPSYVAFTD TERLWPFQVI NEAGKPKDAG VIAGLNVLRA TAGDTHLGGE DFDNRLVSHF
     VEEFKRLRTA CERAKIHDIV LVGGSTRLLQ DYFNGRDLNK ITITNDKGRL SKEEIER