ID HSP7A_CAEEL Reviewed; 640 AA. AC P09446; Q93601; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 2. DT 13-FEB-2019, entry version 154. DE RecName: Full=Heat shock 70 kDa protein A; GN Name=hsp-1; Synonyms=hsp70a; ORFNames=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 RT investigating 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., RA Ploegh H.L.; RT "The Caenorhabditis elegans protein FIC-1 is an AMPylase that RT covalently modifies heat-shock 70 family proteins, translation RT elongation factors and histones."; RL PLoS Genet. 12:E1006023-E1006023(2016). CC -!- SUBUNIT: Interacts with E3 ubiquitin-protein ligase chn-1. CC {ECO:0000269|PubMed:15294159}. CC -!- INTERACTION: CC O16259:sti-1; NbExp=3; IntAct=EBI-322448, EBI-6514174; CC G5EG62:unc-45; NbExp=3; IntAct=EBI-322448, EBI-6675165; CC -!- PTM: AMPylated by fic-1. {ECO:0000269|PubMed:27138431}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {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; Z80223; CAB02319.1; -; Genomic_DNA. DR PIR; JT0285; HHKW7A. DR PIR; T21394; T21394. DR RefSeq; NP_503068.1; NM_070667.4. DR UniGene; Cel.5111; -. 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 ProteinModelPortal; P09446; -. DR SMR; P09446; -. DR BioGrid; 43583; 6. DR DIP; DIP-26882N; -. DR IntAct; P09446; 7. DR MINT; P09446; -. DR STRING; 6239.F26D10.3.2; -. 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 eggNOG; COG0443; LUCA. DR GeneTree; ENSGT00940000154813; -. DR HOGENOM; HOG000228135; -. DR InParanoid; P09446; -. DR KO; K03283; -. DR OMA; AYTKNQD; -. 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-8876725; Protein methylation. DR EvolutionaryTrace; P09446; -. DR PRO; PR:P09446; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00002005; Expressed in 6 organ(s), highest expression level in material anatomical entity. 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:0042623; F:ATPase activity, coupled; IBA:GO_Central. 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:0034605; P:cellular response to heat; 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; 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 PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF100920; SSF100920; 1. DR SUPFAM; SSF100934; SSF100934; 1. 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; Complete proteome; Nucleotide-binding; KW Reference proteome; Stress response. FT CHAIN 1 640 Heat shock 70 kDa protein A. FT /FTId=PRO_0000078298. FT CONFLICT 130 130 E -> K (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 137 138 GT -> EP (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 149 149 A -> T (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 272 273 KR -> NE (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 279 279 S -> C (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 370 370 V -> L (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 499 501 QNK -> AKQ (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 509 511 GRL -> DRF (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 595 595 H -> S (in Ref. 1; AAA28078). FT {ECO:0000305}. FT CONFLICT 605 608 NPII -> KPDL (in Ref. 1; AAA28078). FT {ECO:0000305}. FT HELIX 542 554 {ECO:0000244|PDB:2P32}. FT TURN 557 559 {ECO:0000244|PDB:2P32}. FT HELIX 560 562 {ECO:0000244|PDB:2P32}. FT HELIX 565 585 {ECO:0000244|PDB:2P32}. FT HELIX 590 611 {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 //