HSP7C_CAEEL
ID HSP7C_CAEEL Reviewed; 661 AA.
AC P27420; Q7JNW0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Heat shock 70 kDa protein C;
DE Flags: Precursor;
GN Name=hsp-3; Synonyms=hsp70c; ORFNames=C15H9.6;
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=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 [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 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).
CC -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC multimeric protein complexes inside the ER. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
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; M26604; AAA28074.1; -; Genomic_DNA.
DR EMBL; FO080555; CCD64632.1; -; Genomic_DNA.
DR PIR; A32475; A32475.
DR PIR; T15513; T15513.
DR RefSeq; NP_509019.1; NM_076618.5.
DR AlphaFoldDB; P27420; -.
DR SMR; P27420; -.
DR BioGRID; 45812; 67.
DR IntAct; P27420; 2.
DR STRING; 6239.C15H9.6.1; -.
DR World-2DPAGE; 0020:P27420; -.
DR EPD; P27420; -.
DR PaxDb; P27420; -.
DR PeptideAtlas; P27420; -.
DR PRIDE; P27420; -.
DR EnsemblMetazoa; C15H9.6a.1; C15H9.6a.1; WBGene00002007.
DR EnsemblMetazoa; C15H9.6a.2; C15H9.6a.2; WBGene00002007.
DR GeneID; 180880; -.
DR UCSC; C15H9.6.1; c. elegans.
DR CTD; 180880; -.
DR WormBase; C15H9.6a; CE08177; WBGene00002007; hsp-3.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; P27420; -.
DR OMA; AYTKNQD; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P27420; -.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:P27420; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002007; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P27420; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:WormBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS: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:0030968; P:endoplasmic reticulum unfolded protein response; IEP:WormBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_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; PS00014; ER_TARGET; 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 ATP-binding; Endoplasmic reticulum; Nucleotide-binding; Reference proteome;
KW Signal; Stress response.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..661
FT /note="Heat shock 70 kDa protein C"
FT /id="PRO_0000013541"
FT REGION 639..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 658..661
FT /note="Prevents secretion from ER"
FT CONFLICT 9
FT /note="L -> M (in Ref. 1; AAA28074)"
FT /evidence="ECO:0000305"
FT CONFLICT 12..13
FT /note="LS -> IT (in Ref. 1; AAA28074)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="V -> I (in Ref. 1; AAA28074)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="E -> K (in Ref. 1; AAA28074)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="G -> E (in Ref. 1; AAA28074)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="R -> A (in Ref. 1; AAA28074)"
FT /evidence="ECO:0000305"
FT CONFLICT 647..655
FT /note="GEEAPEEGS -> ERRPQKRDL (in Ref. 1; AAA28074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 73023 MW; 4DFB79714C3EC52A CRC64;
MKTLFLLGLI ALSAVSVYCE EEEKTEKKET KYGTIIGIDL GTTYSCVGVY KNGRVEIIAN
DQGNRITPSY VAFSGDQGDR LIGDAAKNQL TINPENTIFD AKRLIGRDYN DKTVQADIKH
WPFKVIDKSN KPSVEVKVGS DNKQFTPEEV SAMVLVKMKE IAESYLGKEV KNAVVTVPAY
FNDAQRQATK DAGTIAGLNV VRIINEPTAA AIAYGLDKKD GERNILVFDL GGGTFDVSML
TIDNGVFEVL ATNGDTHLGG EDFDQRVMEY FIKLYKKKSG KDLRKDKRAV QKLRREVEKA
KRALSTQHQT KVEIESLFDG EDFSETLTRA KFEELNMDLF RATLKPVQKV LEDSDLKKDD
VHEIVLVGGS TRIPKVQQLI KEFFNGKEPS RGINPDEAVA YGAAVQGGVI SGEEDTGEIV
LLDVNPLTMG IETVGGVMTK LIGRNTVIPT KKSQVFSTAA DNQPTVTIQV FEGERPMTKD
NHQLGKFDLT GLPPAPRGVP QIEVTFEIDV NGILHVTAED KGTGNKNKIT ITNDQNRLSP
EDIERMINDA EKFAEDDKKV KDKAEARNEL ESYAYNLKNQ IEDKEKLGGK LDEDDKKTIE
EAVEEAISWL GSNAEASAEE LKEQKKDLES KVQPIVSKLY KDAGAGGEEA PEEGSDDKDE
L
