ID A7E3Q2_BOVIN Unreviewed; 636 AA.
AC A7E3Q2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Heat shock-related 70 kDa protein 2 {ECO:0000256|ARBA:ARBA00039557};
GN Name=HSPA2 {ECO:0000313|EMBL:ABS44989.1,
GN ECO:0000313|Ensembl:ENSBTAP00000061981.1,
GN ECO:0000313|VGNC:VGNC:112631};
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 {ECO:0000313|EMBL:ABS44989.1};
RN [1] {ECO:0000313|EMBL:ABS44989.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABS44989.1};
RX PubMed=12140684; DOI=10.1007/s00335-001-2145-4;
RA Sonstegard T.S., Capuco A.V., White J., Van Tassell C.P., Connor E.E.,
RA Cho J., Sultana R., Shade L., Wray J.E., Wells K.D., Quackenbush J.;
RT "Analysis of bovine mammary gland EST and functional annotation of the Bos
RT taurus gene index.";
RL Mamm. Genome 13:373-379(2002).
RN [2] {ECO:0000313|EMBL:ABS44989.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABS44989.1};
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3] {ECO:0000313|EMBL:ABS44989.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABS44989.1};
RA Harhay G.P., Sonstegard T.S., Van Tassell C.P., Clawson M.L., Heaton M.P.,
RA Keele J.W., Snelling W.M., Weidmann R.T., Smith T.P.L.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSBTAP00000061981.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000061981.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Ensembl:ENSBTAP00000061981.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000061981.1};
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; BT030673; ABS44989.1; -; mRNA.
DR Ensembl; ENSBTAT00000010270.3; ENSBTAP00000061981.1; ENSBTAG00000007807.3.
DR VEuPathDB; HostDB:ENSBTAG00000007807; -.
DR VGNC; VGNC:112631; HSPA2.
DR GeneTree; ENSGT00940000154813; -.
DR OMA; SYAYNIK; -.
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 Reactome; R-BTA-3371568; Attenuation phase.
DR Reactome; R-BTA-9833482; PKR-mediated signaling.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000007807; Expressed in spermatocyte and 105 other cell types or tissues.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0009408; P:response to heat; ISS:AgBase.
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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF382; HEAT SHOCK-RELATED 70 KDA PROTEIN 2; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Stress response {ECO:0000313|EMBL:ABS44989.1}.
FT REGION 613..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 69809 MW; 11326930235E7B23 CRC64;
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG EIKTFFPEEI
SSMVLTKMKE IAEAYLGGKV QSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA
AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM
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
//
