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   27-MAR-2024, entry version 167.
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; 69.
DR   IntAct; P27420; 2.
DR   STRING; 6239.C15H9.6a.5; -.
DR   EPD; P27420; -.
DR   PaxDb; 6239-C15H9-6-1; -.
DR   PeptideAtlas; P27420; -.
DR   EnsemblMetazoa; C15H9.6a.1; C15H9.6a.1; WBGene00002007.
DR   EnsemblMetazoa; C15H9.6a.2; C15H9.6a.2; WBGene00002007.
DR   UCSC; C15H9.6.1; c. elegans.
DR   AGR; WB:WBGene00002007; -.
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; 143at2759; -.
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 cell types or 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; IEA:UniProtKB-KW.
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:0044183; F:protein folding chaperone; 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; 3.30.420.40; -; 2.
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:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
DR   World-2DPAGE; 0020:P27420; -.
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
//