ENPL1_CAEEL
ID ENPL1_CAEEL Reviewed; 760 AA.
AC Q22235; E9P859;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Endoplasmin homolog {ECO:0000312|WormBase:T05E11.3a};
DE Flags: Precursor;
GN Name=enpl-1 {ECO:0000312|WormBase:T05E11.3a};
GN ORFNames=T05E11.3 {ECO:0000312|WormBase:T05E11.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=24058864; DOI=10.4161/worm.24059;
RA Natarajan B., Gaur R., Hemmingsson O., Kao G., Naredi P.;
RT "Depletion of the ER chaperone ENPL-1 sensitizes C. elegans to the
RT anticancer drug cisplatin.";
RL Worm 2:E24059-E24059(2013).
CC -!- FUNCTION: Molecular chaperone that functions in the processing and
CC transport of secreted proteins. {ECO:0000250|UniProtKB:P14625}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P14625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T05E11.3a};
CC IsoId=Q22235-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T05E11.3b};
CC IsoId=Q22235-2; Sequence=VSP_057488;
CC -!- DISRUPTION PHENOTYPE: Adults show increased sensitivity to cisplatin,
CC sodium arsenite and zinc. RNAi-mediated knockdown results in induction
CC of the unfolded protein response. {ECO:0000269|PubMed:24058864}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; Z68751; CAA92973.1; -; Genomic_DNA.
DR EMBL; Z68751; CBZ01798.1; -; Genomic_DNA.
DR PIR; T24521; T24521.
DR RefSeq; NP_001255536.1; NM_001268607.1. [Q22235-1]
DR RefSeq; NP_001255537.1; NM_001268608.1. [Q22235-2]
DR AlphaFoldDB; Q22235; -.
DR SMR; Q22235; -.
DR DIP; DIP-24557N; -.
DR STRING; 6239.T05E11.3a.1; -.
DR World-2DPAGE; 0020:Q22235; -.
DR EPD; Q22235; -.
DR PaxDb; Q22235; -.
DR PeptideAtlas; Q22235; -.
DR PRIDE; Q22235; -.
DR EnsemblMetazoa; T05E11.3a.1; T05E11.3a.1; WBGene00011480. [Q22235-1]
DR EnsemblMetazoa; T05E11.3a.2; T05E11.3a.2; WBGene00011480. [Q22235-1]
DR EnsemblMetazoa; T05E11.3b.1; T05E11.3b.1; WBGene00011480. [Q22235-2]
DR GeneID; 178014; -.
DR KEGG; cel:CELE_T05E11.3; -.
DR UCSC; T05E11.3.1; c. elegans. [Q22235-1]
DR CTD; 178014; -.
DR WormBase; T05E11.3a; CE06362; WBGene00011480; enpl-1. [Q22235-1]
DR WormBase; T05E11.3b; CE45764; WBGene00011480; enpl-1. [Q22235-2]
DR eggNOG; KOG0020; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q22235; -.
DR OMA; KVSKTTW; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q22235; -.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q22235; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00011480; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Chaperone; Endoplasmic reticulum;
KW Glycoprotein; Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..760
FT /note="Endoplasmin homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432144"
FT REGION 727..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 757..760
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000305"
FT COMPBIAS 739..760
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 426
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057488"
SQ SEQUENCE 760 AA; 87112 MW; 9B870D370165F2BD CRC64;
MRFLLVGFVA LLAVSAFIPN VYAEDEIEDA PKETKEETRE EDSIKLDGLS VSQIKELRSK
AEKHEFQAEV NRMMKLIINS LYRNKEIFLR ELISNASDAL DKIRLLSLTD PEQLRETEEM
SVKIKADREN RLLHITDTGV GMTRQDLINN LGTIARSGTS EFLSKLMDTA TSSDQQQDLI
GQFGVGFYAA FLVADRVVVT TKNNDDDQYI WESDSASFTI SKDPRGNTLK RGTQITLYLK
EEAADFLEPD TLKNLVHKYS QFINFDIFLW QSKTEMVEEA VEEEPATTED GAVEEEKEEK
KTKKVEKTTW DWEKVNNVKP IWMRKPNQVE EDEYKQFYKS ITKDSEEPLS HVHFSAEGEV
SFRSILYVPK KSPNDMFQNY GKVIENIKLY VRRVFITDDF ADMLPKYLSF IRGIVDSDDL
PLNVSRENLQ QHKLLKVIKK KLVRKVLDML KKLDGAQFDD FWSEFSTNIK LGVMEDPSNR
MRLAKLLRFQ SSNDADKTTT LAAYVERMKE KQDAIYYMAG TSRKEVETSP FVERLIAKGY
EVLFLTEAVD EYCIQAMPEY ESKKFQNVAK EGVTIDDGEK AKEAHKGLEE EFKPLTDWLK
ETALKDLIEK AVVSQRLVKS PSALVASSYG WSGNMERIMK SQAYAKAKDP TQDFYATQKK
TFEINPRHPV IKELLKRVTA SEEDTTAAST AKLLFETATL RSGFSLQDQV GFADRIEAVL
RQSLDVSQDA QVETEQHIEE AEPEPEAAEE TTIEEEHSEL
