HS105_BOVIN
ID HS105_BOVIN Reviewed; 859 AA.
AC Q0IIM3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Heat shock protein 105 kDa;
DE AltName: Full=Heat shock 110 kDa protein;
GN Name=HSPH1;
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 MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a nucleotide-exchange factor (NEF) for chaperone
CC proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B
CC thereby triggering substrate release. Prevents the aggregation of
CC denatured proteins in cells under severe stress, on which the ATP
CC levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone
CC activities. {ECO:0000250|UniProtKB:Q61699,
CC ECO:0000250|UniProtKB:Q92598}.
CC -!- SUBUNIT: Interacts with HSPA8/HSC70. Interacts with HSPA1A (via NBD)
CC and HSPA1B (via NBD). {ECO:0000250|UniProtKB:Q61699,
CC ECO:0000250|UniProtKB:Q92598}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92598}.
CC -!- PTM: Phosphorylation on Ser-509 may be important for regulation of the
CC HSPA8/HSC70 chaperone activity. {ECO:0000250|UniProtKB:Q61699}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; BC122574; AAI22575.1; -; mRNA.
DR RefSeq; NP_001068770.1; NM_001075302.1.
DR AlphaFoldDB; Q0IIM3; -.
DR SMR; Q0IIM3; -.
DR STRING; 9913.ENSBTAP00000006600; -.
DR iPTMnet; Q0IIM3; -.
DR PaxDb; Q0IIM3; -.
DR PeptideAtlas; Q0IIM3; -.
DR PRIDE; Q0IIM3; -.
DR Ensembl; ENSBTAT00000006600; ENSBTAP00000006600; ENSBTAG00000005012.
DR GeneID; 507165; -.
DR KEGG; bta:507165; -.
DR CTD; 10808; -.
DR VEuPathDB; HostDB:ENSBTAG00000005012; -.
DR VGNC; VGNC:53817; HSPH1.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000159635; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; Q0IIM3; -.
DR OMA; NMLSHAY; -.
DR OrthoDB; 406172at2759; -.
DR TreeFam; TF105043; -.
DR Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:Q0IIM3; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000005012; Expressed in occipital lobe and 101 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
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:0051085; P:chaperone cofactor-dependent protein refolding; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd11739; HSPH1_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 2.
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 InterPro; IPR042053; HSPH1_NBD.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT CHAIN 2..859
FT /note="Heat shock protein 105 kDa"
FT /id="PRO_0000289944"
FT REGION 515..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 471
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61699"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61699"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61699"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 816
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
SQ SEQUENCE 859 AA; 96726 MW; EA9EF778D194A5CB CRC64;
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKSQQITHA
NNTVSNFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEEH LFSVEQITAM
LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
YGIYKQDLPS LDEKPRIVVF VDMGHSAFQV SACAFNKGKL KVLGTAFDPF LGGKNFDAKL
VEYFCAEFKT KYKLDAKSKI RALLRLYQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK
MNRAQFEELC ADLLQKIEVP LYLLMEQTQL KVEDVSAVEI VGGTTRIPAV KEKIAKFFGK
DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWSHDS EDAEGVHEVF
SRNHAAPFSK VLTFLRSGPF ELEAFYSDPQ GVPYPEAKIG RFIVQNVSAQ KDGEKSRVKV
KVRVNTHGIF TISTASMVEK IPAEENEVSS LEADMDCQNQ RPPENPDAEK NIQQDNNEAG
TQPQVQTDGH QTSQSPPSPE LTSEENKIPD ADKANEKKVD QPPEAKKPKI KVVNVELPIE
ANLVWQLGKD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE EYVYEFRDKL CGPYEKFICE
QDHQKFLRLL TETENWLYEE GEDQAKQAYV DKLEELMKIG TPIKVRFQEA EERPKIFEEL
GQRLQHYAKI AADFRNNDEK YNHIDESEMK KVEKSVNEMM EWMNNVMSAQ AKKSLDQDPV
VCAQEIRAKI KELNNNCEPV VTQPKPKIES PKLERTPNGP STDKKEEDLD GKNNFSAEPP
HQNGECYPNE KSSINMDLD
