HS105_CRIGR
ID HS105_CRIGR Reviewed; 858 AA.
AC Q60446;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Heat shock protein 105 kDa;
DE AltName: Full=Heat shock 110 kDa protein;
GN Name=HSPH1; Synonyms=HSP105, HSP110;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7797574; DOI=10.1074/jbc.270.26.15725;
RA Lee-Yoon D., Easton D., Murawski M., Burd R., Subjeck J.R.;
RT "Identification of a major subfamily of large hsp70-like proteins through
RT the cloning of the mammalian 110-kDa heat shock protein.";
RL J. Biol. Chem. 270:15725-15733(1995).
RN [2]
RP FUNCTION.
RX PubMed=9395504; DOI=10.1074/jbc.272.50.31636;
RA Oh H.J., Chen X., Subjeck J.R.;
RT "Hsp110 protects heat-denatured proteins and confers cellular
RT thermoresistance.";
RL J. Biol. Chem. 272:31636-31640(1997).
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 (By similarity). Prevents the
CC aggregation of denatured proteins in cells under severe stress, on
CC which the ATP levels decrease markedly (PubMed:9395504). Inhibits
CC HSPA8/HSC70 ATPase and chaperone activities (By similarity).
CC {ECO:0000250|UniProtKB:Q61699, ECO:0000250|UniProtKB:Q92598,
CC ECO:0000269|PubMed:9395504}.
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 -!- TISSUE SPECIFICITY: Predominantly expressed in the brain and also found
CC in the liver.
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; Z47807; CAA87768.1; -; mRNA.
DR PIR; A57513; A57513.
DR RefSeq; NP_001233649.1; NM_001246720.1.
DR AlphaFoldDB; Q60446; -.
DR SMR; Q60446; -.
DR STRING; 10029.NP_001233649.1; -.
DR GeneID; 100689462; -.
DR KEGG; cge:100689462; -.
DR CTD; 10808; -.
DR eggNOG; KOG0103; Eukaryota.
DR OrthoDB; 406172at2759; -.
DR PRO; PR:Q60446; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; 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 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 Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT CHAIN 2..858
FT /note="Heat shock protein 105 kDa"
FT /id="PRO_0000078283"
FT REGION 500..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..561
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 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 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 858 AA; 96151 MW; 33B3CD01A97162DE CRC64;
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGPKNRTIGV AAKNQQITHA
NNTVSSFKRF HGRAFSDPFI QKEKESLSYD LVPMKNGGVG IKVMYMDEEH LFSVEQITAM
LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
YGIYKQDLPN ADEKPQGSGV CGHGPSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL
VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSAK
MNRSQFEELC AELLQKIEVP LHSLMEQTHL KTEDVSAIEI VGGATRIPAV KERIAKFFGK
DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSKVKV
KVRVNTHGIF TISTASMVEK VPTEEDDGSS VEADMECPNQ KPAESSDVDK NSQQDNSEAG
TQPQVQTDGQ QTSQSPPSPE LPSEENKIPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE
ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICQ
QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG NPVKVRFQEA EERPKVLEEL
GQRLQHYAKI AADFRSKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLDQDPV
VRTHEIRAKV KELNNVCEPV VNQPKPKIES PKLERTPNGP NLDKKEDLEG KDNFGAEAPH
QNGECHPNEK GSVNMDLD
