HS105_PONAB
ID HS105_PONAB Reviewed; 858 AA.
AC Q5R606;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Heat shock protein 105 kDa;
DE AltName: Full=Heat shock 110 kDa protein;
GN Name=HSPH1; Synonyms=HSP105, HSP110;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860694; CAH92810.1; -; mRNA.
DR RefSeq; NP_001126639.1; NM_001133167.1.
DR AlphaFoldDB; Q5R606; -.
DR SMR; Q5R606; -.
DR STRING; 9601.ENSPPYP00000005987; -.
DR PRIDE; Q5R606; -.
DR GeneID; 100173637; -.
DR KEGG; pon:100173637; -.
DR CTD; 10808; -.
DR eggNOG; KOG0103; Eukaryota.
DR InParanoid; Q5R606; -.
DR OrthoDB; 406172at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 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_0000235975"
FT REGION 500..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..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 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 561
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
FT MOD_RES 815
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92598"
SQ SEQUENCE 858 AA; 96866 MW; 3E07B999E034015C CRC64;
MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA
NNTVSNFKRF HGRAFNDPFI QKEKENLSYD LVPLKNGGVG IKVMYMGEEH LFSVEQITAM
LLTKLKETAE NSLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
YGIYKQDLPS LDEKPRIVVF VDMGHSAFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL
VEHFCAEFKT KYKLDAKSKI RALLRLYQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK
MNRSQFEELC AELLQKIEVP LYSLLEQTHL KVEDVSAVEI VGGATRIPAV KERIAKFFGK
DISTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLIWNHDS EDTEGVHEVF
SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV
KVRVNTHGIF TISTASMVEK VPTEENEMSS EADMECLNQR PPENPDTDKN VQQDNSEAGT
QPQVQTDAQQ TSQSPPSPEL TSEENKIPDA DKANEKKVDQ PPEAKKPKIK VVNVELPIEA
NLVWQLGKDL LNMYIETEGK MIMQDKLEKE RNDAKNAVEE YVYEFRDKLC GPYEKFICEQ
DHQNFLRLLT ETEDWLYEEG EDQAKQAYVD KLEELMKIGT PVKVRFQEAE ERPKMFEELG
QRLQHYAKIA ADFRNKDEKY NHIDESEMKK VEKSVNEVME WMNNVMNAQA KESLDQDPVV
RAQEIKTKIK ELNNTCEPVV TQPKPKIESP KLERTPNGPN IDKKEEDLED KNNFGAEPPH
QNGECYPNEK NSVNMDLD
