HSP7C_CAEBR
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 03-AUG-2022, entry version 134.
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.CBG14829; -.
DR PRIDE; 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; 288077at2759; -.
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; 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: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; 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 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
