HSP72_BOVIN
ID HSP72_BOVIN Reviewed; 636 AA.
AC P34933; Q3MHP7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Heat shock-related 70 kDa protein 2;
DE AltName: Full=Heat shock 70 kDa protein 3;
DE Short=HSP70.3;
GN Name=HSPA2; Synonyms=HSP70-3, HSPA3;
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 [GENOMIC DNA].
RX PubMed=1478667; DOI=10.1016/s0888-7543(05)80106-5;
RA Grosz M.D., Womack J.E., Skow L.C.;
RT "Syntenic conservation of HSP70 genes in cattle and humans.";
RL Genomics 14:863-868(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P17156,
CC 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 -!- 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:P54652}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; L10428; AAA30569.1; -; Genomic_DNA.
DR EMBL; BC105156; AAI05157.1; -; mRNA.
DR RefSeq; NP_776769.1; NM_174344.1.
DR AlphaFoldDB; P34933; -.
DR SMR; P34933; -.
DR PeptideAtlas; P34933; -.
DR PRIDE; P34933; -.
DR GeneID; 281827; -.
DR KEGG; bta:281827; -.
DR CTD; 3306; -.
DR InParanoid; P34933; -.
DR OrthoDB; 288077at2759; -.
DR PRO; PR:P34933; -.
DR Proteomes; UP000009136; 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:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0009408; P:response to heat; ISS:AgBase.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Differentiation;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Stress response.
FT CHAIN 1..636
FT /note="Heat shock-related 70 kDa protein 2"
FT /id="PRO_0000078261"
FT REGION 2..389
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 397..512
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 613..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 205..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 271..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 342..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14659"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14659"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14659"
FT MOD_RES 564
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P54652"
FT CONFLICT 54
FT /note="D -> T (in Ref. 1; AAA30569)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="S -> R (in Ref. 1; AAA30569)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="L -> W (in Ref. 1; AAA30569)"
FT /evidence="ECO:0000305"
FT CONFLICT 259..264
FT /note="NKRAVR -> A (in Ref. 1; AAA30569)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..316
FT /note="GT -> VP (in Ref. 1; AAA30569)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="R -> C (in Ref. 1; AAA30569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 69740 MW; 2F53195A2855EE58 CRC64;
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG EIKTFFPEEI
SSMVLTKMKE IAEAYLGGKV QSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA
AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNSM
VSHLAEEFKR KHKKDIAPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK
ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN
TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT
FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA
AKNAVESYTY NIKQTVEDEK LRGKISDQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK
ELERVCNPII SKLYQGGPGG GGGSGASGGP TIEEVD
