ID   HSP7C_CAEBR             Reviewed;         661 AA.
AC   P19208; A8XKS6; Q617T9;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Heat shock 70 kDa protein C;
DE   Flags: Precursor;
GN   Name=hsp-3; ORFNames=CBG14829;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-441.
RX   PubMed=2116528; DOI=10.1007/bf02101786;
RA   Heschl M.F.P., Baillie D.L.;
RT   "Functional elements and domains inferred from sequence comparisons of a
RT   heat shock gene in two nematodes.";
RL   J. Mol. Evol. 31:3-9(1990).
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:0000250|UniProtKB:P27420}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; HE600983; CAP33250.1; -; Genomic_DNA.
DR   EMBL; M26906; AAA28075.1; -; Genomic_DNA.
DR   RefSeq; XP_002644811.1; XM_002644765.1.
DR   AlphaFoldDB; P19208; -.
DR   SMR; P19208; -.
DR   STRING; 6238.P19208; -.
DR   EnsemblMetazoa; CBG14829.1; CBG14829.1; WBGene00035220.
DR   GeneID; 8586807; -.
DR   KEGG; cbr:CBG_14829; -.
DR   CTD; 8586807; -.
DR   WormBase; CBG14829; CBP03479; WBGene00035220; Cbr-hsp-3.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_7_0_1; -.
DR   InParanoid; P19208; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
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; 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: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; IBA:GO_Central.
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.
PE   3: Inferred from homology;
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_0000013540"
FT   REGION          618..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           658..661
FT                   /note="Prevents secretion from ER"
FT   COMPBIAS        618..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        126
FT                   /note="L -> F (in Ref. 2; AAA28075)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="A -> S (in Ref. 2; AAA28075)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="D -> V (in Ref. 2; AAA28075)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189..191
FT                   /note="TKD -> LKY (in Ref. 2; AAA28075)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="A -> V (in Ref. 2; AAA28075)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   661 AA;  72945 MW;  4358AA747A128F0D CRC64;
     MKTLFLLGLI ALTAVSVYCE EEEKTEKKET KYGTIIGIDL GTTYSCVGVY KNGRVEIIAN
     DQGNRITPSY VAFSGEQGDR LIGDAAKNQL TINPENTIFD AKRLIGRDYN DKTVQADIKH
     WPFKVLDKSN KPSVEVKVGA DNKQFTPEEV SAMVLVKMKE IAESYLGKEV KHAVVTVPAY
     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 LISRNTVIPT KKSQVFSTAA DNQPTVTIQV FEGERPMTKD
     NHQLGKFDLT GIPPAPRGVP QIEVTFEIDV NGILHVTAED KGTGNKNKIT ITNDQNRLSP
     EDIERMINDA EKFAEDDKKV KEKAEARNEL ESYAYSLKNQ IGDKEKLGGK LDEDDKKTIE
     EAVDEAISWL GSNADASAEE LKEQKKELEG KVQPIVSKLY KDGGAGGEEA PEEGSDDKDE
     L
//