ID HS105_RAT Reviewed; 858 AA.
AC Q66HA8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 136.
DE RecName: Full=Heat shock protein 105 kDa;
DE AltName: Full=Heat shock 110 kDa protein;
GN Name=Hsph1; Synonyms=Hsp105, Hsp110;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558 AND SER-810, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC081945; AAH81945.1; -; mRNA.
DR RefSeq; NP_001011901.1; NM_001011901.1.
DR AlphaFoldDB; Q66HA8; -.
DR SMR; Q66HA8; -.
DR BioGRID; 252555; 3.
DR STRING; 10116.ENSRNOP00000001201; -.
DR GlyGen; Q66HA8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q66HA8; -.
DR PhosphoSitePlus; Q66HA8; -.
DR SwissPalm; Q66HA8; -.
DR jPOST; Q66HA8; -.
DR PaxDb; 10116-ENSRNOP00000001201; -.
DR Ensembl; ENSRNOT00000001201.8; ENSRNOP00000001201.6; ENSRNOG00000000902.8.
DR Ensembl; ENSRNOT00055006245; ENSRNOP00055004765; ENSRNOG00055003922.
DR Ensembl; ENSRNOT00060003473; ENSRNOP00060002370; ENSRNOG00060002220.
DR Ensembl; ENSRNOT00065009424; ENSRNOP00065006758; ENSRNOG00065006176.
DR GeneID; 288444; -.
DR KEGG; rno:288444; -.
DR UCSC; RGD:1311609; rat.
DR AGR; RGD:1311609; -.
DR CTD; 10808; -.
DR RGD; 1311609; Hsph1.
DR eggNOG; KOG0103; Eukaryota.
DR GeneTree; ENSGT00940000159635; -.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; Q66HA8; -.
DR OMA; NEFTDRC; -.
DR OrthoDB; 276440at2759; -.
DR PhylomeDB; Q66HA8; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR ChiTaRS; Hspa4; rat.
DR PRO; PR:Q66HA8; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000902; Expressed in frontal cortex and 20 other cell types or tissues.
DR Genevisible; Q66HA8; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; ISO:RGD.
DR GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; ISO:RGD.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:RGD.
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; 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 InterPro; IPR042053; HSPH1_NBD.
DR PANTHER; PTHR45639:SF2; HEAT SHOCK PROTEIN 105 KDA; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 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; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein 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..858
FT /note="Heat shock protein 105 kDa"
FT /id="PRO_0000235976"
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..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..833
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:0007744|PubMed:22673903"
FT MOD_RES 562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 816
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
SQ SEQUENCE 858 AA; 96419 MW; 0AF62115FF795C66 CRC64;
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGPKNRTIGV AAKNQQITHA
NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEDH LFSVEQITAM
LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
YGIYKQDLPN ADEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL
VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSAK
MNRSQFEELC AELLQKIEVP LHLLMEQTHL KTEEVSAIEI VGGATRIPAV KERIARFFGK
DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ AVPYPEAKIG RFVVQNVSAQ KDGEKSKVKV
KVRVNTHGIF TISTASMVEK VPTEEEDGSS VEADMECPNQ KPAESSDVDK NIQQDNSEAG
TQPQVQTDGQ QTSQSPPSPE LTSEENKIPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE
ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE
QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPRVLEEL
GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLHQDPV
VRTHEISAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NMDKKEDLEG KSNLGADAPH
QNGECHPNEK GSVSMDLD
//
