ID   HSP72_MESAU             Reviewed;         192 AA.
AC   P86204;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Heat shock-related 70 kDa protein 2 {ECO:0000250|UniProtKB:P17156};
DE   Flags: Fragments;
GN   Name=HSPA2 {ECO:0000250|UniProtKB:P17156};
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.
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. In the ATP-
CC       bound form, it has a low affinity for substrate proteins. However, upon
CC       hydrolysis of the ATP to ADP, it undergoes a conformational change that
CC       increases its affinity for substrate proteins. It goes through repeated
CC       cycles of ATP hydrolysis and nucleotide exchange, which permits cycles
CC       of substrate binding and release. Plays a role in spermatogenesis. In
CC       association with SHCBP1L may participate in the maintenance of spindle
CC       integrity during meiosis in male germ cells.
CC       {ECO:0000250|UniProtKB:P17156, ECO:0000250|UniProtKB:P54652}.
CC   -!- SUBUNIT: Interacts with FKBP6. Interacts with ZNF541. Component of the
CC       CatSper complex. Interacts with RABL2/RABL2A; binds preferentially to
CC       GTP-bound RABL2. Interacts with SHCBP1L; this interaction may promote
CC       the recruitment of HSPA2 to the spindle. Interacts with MOV10L1.
CC       {ECO:0000250|UniProtKB:P17156, ECO:0000250|UniProtKB:P54652}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:P17156}. Note=Colocalizes with SHCBP1L at
CC       spindle during the meiosis process. {ECO:0000250|UniProtKB:P17156}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000255}.
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DR   AlphaFoldDB; P86204; -.
DR   SMR; P86204; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0072687; C:meiotic spindle; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 4.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Differentiation;
KW   Methylation; Nucleotide-binding; Reference proteome; Spermatogenesis;
KW   Stress response.
FT   CHAIN           <1..>192
FT                   /note="Heat shock-related 70 kDa protein 2"
FT                   /id="PRO_0000394296"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         186
FT                   /note="N6,N6,N6-trimethyllysine; by METTL21A; in vitro"
FT                   /evidence="ECO:0000250|UniProtKB:P54652"
FT   NON_CONS        47..48
FT                   /evidence="ECO:0000305"
FT   NON_CONS        97..98
FT                   /evidence="ECO:0000305"
FT   NON_CONS        124..125
FT                   /evidence="ECO:0000305"
FT   NON_CONS        136..137
FT                   /evidence="ECO:0000305"
FT   NON_CONS        153..154
FT                   /evidence="ECO:0000305"
FT   NON_CONS        166..167
FT                   /evidence="ECO:0000305"
FT   NON_CONS        175..176
FT                   /evidence="ECO:0000305"
FT   NON_CONS        184..185
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         192
SQ   SEQUENCE   192 AA;  21284 MW;  6DC466F9D7CDF4EC CRC64;
     VEIIANDQGN RTTPSYVAFT DTERLIGDAA KNQVAMNPTN TIFDAKRVQS AVITVPAYFN
     DSQRQATKDA GTITGLNVLR IINEPTAAAI AYGLDKKSTA GDTHLGGEDF DNRMVSHLAE
     EFKRARFEEL NADLFRLDKG QIQEIVLVGG STRLLQDFFN GKELNKITIT NDKGRMVQEA
     ERYKGKISEQ DK