ID HSP1_CAEEL Reviewed; 640 AA. AC P09446; Q93601; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 2. DT 02-DEC-2020, entry version 166. DE RecName: Full=Heat shock protein hsp-1 {ECO:0000305}; DE AltName: Full=Heat shock 70 kDa protein A {ECO:0000303|PubMed:2841196}; GN Name=hsp-1 {ECO:0000312|WormBase:F26D10.3}; GN Synonyms=hsp70a {ECO:0000303|PubMed:2841196}; GN ORFNames=F26D10.3 {ECO:0000312|WormBase:F26D10.3}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2841196; DOI=10.1016/0378-1119(88)90339-3; RA Snutch T.P., Heschl M.F.P., Baillie D.L.; RT "The Caenorhabditis elegans hsp70 gene family: a molecular genetic RT characterization."; RL Gene 64:241-255(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [3] RP INTERACTION WITH CHN-1. RX PubMed=15294159; DOI=10.1016/j.cell.2004.07.014; RA Hoppe T., Cassata G., Barral J.M., Springer W., Hutagalung A.H., RA Epstein H.F., Baumeister R.; RT "Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4- RT multiubiquitylation complex in C. elegans."; RL Cell 118:337-349(2004). RN [4] RP AMPYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=27138431; DOI=10.1371/journal.pgen.1006023; RA Truttmann M.C., Cruz V.E., Guo X., Engert C., Schwartz T.U., Ploegh H.L.; RT "The Caenorhabditis elegans protein FIC-1 is an AMPylase that covalently RT modifies heat-shock 70 family proteins, translation elongation factors and RT histones."; RL PLoS Genet. 12:E1006023-E1006023(2016). RN [5] RP INDUCTION. RX PubMed=29500338; DOI=10.1038/s41467-018-02934-5; RA De Magalhaes Filho C.D., Henriquez B., Seah N.E., Evans R.M., RA Lapierre L.R., Dillin A.; RT "Visible light reduces C. elegans longevity."; RL Nat. Commun. 9:927-927(2018). CC -!- SUBUNIT: Interacts with E3 ubiquitin-protein ligase chn-1. CC {ECO:0000269|PubMed:15294159}. CC -!- INTERACTION: CC P09446; O16259: sti-1; NbExp=3; IntAct=EBI-322448, EBI-6514174; CC P09446; G5EG62: unc-45; NbExp=3; IntAct=EBI-322448, EBI-6675165; CC -!- INDUCTION: Induced by white light exposure. CC {ECO:0000269|PubMed:29500338}. CC -!- PTM: AMPylated by fic-1. {ECO:0000269|PubMed:27138431}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M18540; AAA28078.1; -; Genomic_DNA. DR EMBL; BX284604; CAB02319.1; -; Genomic_DNA. DR PIR; JT0285; HHKW7A. DR PIR; T21394; T21394. DR RefSeq; NP_503068.1; NM_070667.4. DR PDB; 2P32; X-ray; 3.20 A; A/B/C/D/E/F=542-640. DR PDB; 4I2W; X-ray; 3.60 A; B=631-640. DR PDBsum; 2P32; -. DR PDBsum; 4I2W; -. DR SMR; P09446; -. DR BioGRID; 43583; 65. DR DIP; DIP-26882N; -. DR IntAct; P09446; 8. DR MINT; P09446; -. DR STRING; 6239.F26D10.3.1; -. DR iPTMnet; P09446; -. DR World-2DPAGE; 0020:P09446; -. DR EPD; P09446; -. DR PaxDb; P09446; -. DR PeptideAtlas; P09446; -. DR PRIDE; P09446; -. DR EnsemblMetazoa; F26D10.3.1; F26D10.3.1; WBGene00002005. DR EnsemblMetazoa; F26D10.3.2; F26D10.3.2; WBGene00002005. DR GeneID; 178507; -. DR KEGG; cel:CELE_F26D10.3; -. DR UCSC; F26D10.3.1; c. elegans. DR CTD; 178507; -. DR WormBase; F26D10.3; CE09682; WBGene00002005; hsp-1. DR eggNOG; KOG0101; Eukaryota. DR GeneTree; ENSGT00940000154813; -. DR HOGENOM; CLU_005965_3_0_1; -. DR InParanoid; P09446; -. DR OMA; DSSKPKM; -. DR OrthoDB; 288077at2759; -. DR PhylomeDB; P09446; -. DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-CEL-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR). DR Reactome; R-CEL-3371568; Attenuation phase. DR Reactome; R-CEL-3371571; HSF1-dependent transactivation. DR Reactome; R-CEL-6798695; Neutrophil degranulation. DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway. DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis. DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation. DR EvolutionaryTrace; P09446; -. DR PRO; PR:P09446; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00002005; Expressed in material anatomical entity and 6 other tissues. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0005829; C:cytosol; IDA:WormBase. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0016887; F:ATPase activity; IDA:WormBase. DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central. DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central. DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central. DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase. DR GO; GO:0042026; P:protein refolding; IBA:GO_Central. DR GO; GO:0009408; P:response to heat; IDA:WormBase. DR GO; GO:0006986; P:response to unfolded protein; IBA:GO_Central. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:WormBase. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR Gene3D; 1.20.1270.10; -; 1. 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 PANTHER; PTHR19375; PTHR19375; 1. DR Pfam; PF00012; HSP70; 1. DR SUPFAM; SSF100920; SSF100920; 1. DR SUPFAM; SSF100934; SSF100934; 1. DR SUPFAM; SSF53067; SSF53067; 2. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome; KW Stress response. FT CHAIN 1..640 FT /note="Heat shock protein hsp-1" FT /id="PRO_0000078298" FT CONFLICT 130 FT /note="E -> K (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 137..138 FT /note="GT -> EP (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="A -> T (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 272..273 FT /note="KR -> NE (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="S -> C (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="V -> L (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 499..501 FT /note="QNK -> AKQ (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 509..511 FT /note="GRL -> DRF (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 595 FT /note="H -> S (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT CONFLICT 605..608 FT /note="NPII -> KPDL (in Ref. 1; AAA28078)" FT /evidence="ECO:0000305" FT HELIX 542..554 FT /evidence="ECO:0000244|PDB:2P32" FT TURN 557..559 FT /evidence="ECO:0000244|PDB:2P32" FT HELIX 560..562 FT /evidence="ECO:0000244|PDB:2P32" FT HELIX 565..585 FT /evidence="ECO:0000244|PDB:2P32" FT HELIX 590..611 FT /evidence="ECO:0000244|PDB:2P32" SQ SEQUENCE 640 AA; 69723 MW; 5D7B46B812E7A1DA CRC64; MSKHNAVGID LGTTYSCVGV FMHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPHNTVFDA KRLIGRKFDD PAVQSDMKHW PFKVISAEGA KPKVQVEYKG ENKIFTPEEI SSMVLLKMKE TAEAFLGTTV KDAVVTVPAY FNDSQRQATK DAGAIAGLNV LRIINEPTAA AIAYGLDKKG HGERNVLIFD LGGGTFDVSI LTIEDGIFEV KSTAGDTHLG GEDFDNRMVN HFCAEFKRKH KKDLASNPRA LRRLRTACER AKRTLSSSSQ ASIEIDSLFE GIDFYTNITR ARFEELCADL FRSTMDPVEK SLRDAKMDKS QVHDIVLVGG STRIPKVQKL LSDLFSGKEL NKSINPDEAV AYGAAVQAAI LSGDKSEAVQ DLLLLDVAPL SLGIETAGGV MTALIKRNTT IPTKTAQTFT TYSDNQPGVL IQVYEGERAM TKDNNLLGKF ELSGIPPAPR GVPQIEVTFD IDANGILNVS ATDKSTGKQN KITITNDKGR LSKDDIERMV NEAEKYKADD EAQKDRIGAK NGLESYAFNL KQTIEDEKLK DKISPEDKKK IEDKCDEILK WLDSNQTAEK EEFEHQQKDL EGLANPIISK LYQSAGGAPP GAAPGGAAGG AGGPTIEEVD //