HSP1_CAEEL
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 03-AUG-2022, entry version 173.
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}.
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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 AlphaFoldDB; P09446; -.
DR SMR; P09446; -.
DR BioGRID; 43583; 85.
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 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; YQNAGGM; -.
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) in the presence of ligand.
DR Reactome; R-CEL-3371571; HSF1-dependent transactivation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P09446; -.
DR PRO; PR:P09446; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002005; Expressed in adult organism and 5 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:ATP hydrolysis activity; IDA:WormBase.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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:0042147; P:retrograde transport, endosome to Golgi; IMP:WormBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR DisProt; DP02984; -.
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 REGION 613..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:2P32"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:2P32"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:2P32"
FT HELIX 565..585
FT /evidence="ECO:0007829|PDB:2P32"
FT HELIX 590..611
FT /evidence="ECO:0007829|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
