HSP6_CAEEL
ID HSP6_CAEEL Reviewed; 657 AA.
AC P11141; P91135;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Heat shock protein hsp-6 {ECO:0000305};
DE AltName: Full=Heat shock 70 kDa protein F, mitochondrial {ECO:0000303|PubMed:2766926};
DE Flags: Precursor;
GN Name=hsp-6 {ECO:0000312|WormBase:C37H5.8};
GN Synonyms=hsp70f {ECO:0000303|PubMed:2766926},
GN mot-2 {ECO:0000312|WormBase:C37H5.8};
GN ORFNames=C37H5.8 {ECO:0000312|WormBase:C37H5.8};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-487.
RC STRAIN=Bristol N2;
RX PubMed=2766926; DOI=10.1089/dna.1.1989.8.233;
RA Heschl M.F.P., Baillie D.L.;
RT "Characterization of the hsp70 multigene family of Caenorhabditis
RT elegans.";
RL DNA 8:233-243(1989).
RN [3]
RP INDUCTION BY MITOCHONDRIAL STRESS.
RX PubMed=26212459; DOI=10.1016/j.molcel.2015.06.027;
RA Labbadia J., Morimoto R.I.;
RT "Repression of the heat shock response is a programmed event at the onset
RT of reproduction.";
RL Mol. Cell 59:639-650(2015).
RN [4]
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 -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- INDUCTION: By mitochondrial stress. Induced by white light exposure
CC (PubMed:29500338). {ECO:0000269|PubMed:26212459,
CC ECO:0000269|PubMed:29500338}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; BX284605; CCD66987.1; -; Genomic_DNA.
DR EMBL; X07678; CAA30525.1; -; Genomic_DNA.
DR PIR; B32475; B32475.
DR PIR; T25613; T25613.
DR RefSeq; NP_504291.1; NM_071890.4.
DR PDB; 3DQG; X-ray; 1.72 A; A/B/C/D=418-565.
DR PDBsum; 3DQG; -.
DR AlphaFoldDB; P11141; -.
DR SMR; P11141; -.
DR BioGRID; 43923; 52.
DR IntAct; P11141; 2.
DR STRING; 6239.C37H5.8; -.
DR World-2DPAGE; 0020:P11141; -.
DR EPD; P11141; -.
DR PaxDb; P11141; -.
DR PeptideAtlas; P11141; -.
DR PRIDE; P11141; -.
DR EnsemblMetazoa; C37H5.8.1; C37H5.8.1; WBGene00002010.
DR GeneID; 178873; -.
DR UCSC; C37H5.8; c. elegans.
DR CTD; 178873; -.
DR WormBase; C37H5.8; CE08631; WBGene00002010; hsp-6.
DR eggNOG; KOG0102; Eukaryota.
DR GeneTree; ENSGT00920000149123; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P11141; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P11141; -.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR EvolutionaryTrace; P11141; -.
DR PRO; PR:P11141; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00002010; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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:0034514; P:mitochondrial unfolded protein response; IMP:WormBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 TIGRFAMs; TIGR02350; prok_dnaK; 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; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..657
FT /note="Heat shock protein hsp-6"
FT /id="PRO_0000013543"
FT REGION 637..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 138
FT /note="V -> E (in Ref. 2; CAA30525)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="S -> P (in Ref. 2; CAA30525)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="A -> P (in Ref. 2; CAA30525)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..348
FT /note="KA -> NV (in Ref. 2; CAA30525)"
FT /evidence="ECO:0000305"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:3DQG"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 442..455
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 460..469
FT /evidence="ECO:0007829|PDB:3DQG"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 476..485
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 507..515
FT /evidence="ECO:0007829|PDB:3DQG"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 529..532
FT /evidence="ECO:0007829|PDB:3DQG"
FT HELIX 534..551
FT /evidence="ECO:0007829|PDB:3DQG"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:3DQG"
SQ SEQUENCE 657 AA; 70845 MW; 637A1636B6ABB836 CRC64;
MLSARSFLSS ARTIARSSLM SARSLSDKPK GHVIGIDLGT TNSCVSIMEG KTPKVIENAE
GVRTTPSTVA FTADGERLVG APAKRQAVTN SANTLFATKR LIGRRYEDPE VQKDLKVVPY
KIVKASNGDA WVEAQGKVYS PSQVGAFVLM KMKETAESYL GTTVNNAVVT VPAYFNDSQR
QATKDAGQIS GLNVLRVINE PTAAALAYGL DKDAGDKIIA VYDLGGGTFD VSILEIQKGV
FEVKSTNGDT FLGGEDFDHA LVHHLVGEFK KEQGVDLTKD PQAMQRLREA AEKAKCELSS
TTQTDINLPY ITMDQSGPKH LNLKLTRAKF EQIVGDLIKR TIEPCRKALH DAEVKSSQIA
DVLLVGGMSR MPKVQATVQE IFGKVPSKAV NPDEAVAMGA AIQGAVLAGD VTDVLLLDVT
PLSLGIETLG GIMTKLITRN TTIPTKKSQV FSTAADGQTQ VQIKVFQGER EMATSNKLLG
QFSLVGIPPA PRGVPQVEVT FDIDANGIVN VSARDRGTGK EQQIVIQSSG GLSKDQIENM
IKEAEKNAAE DAKRKELVEV INQAEGIIHD TEAKMTEFAD QLPKDECEAL RTKIADTKKI
LDNKDNETPE AIKEACNTLQ QQSLKLFEAA YKNMAAKNSG GDAQEAKTAE EPKKEQN
