DERL1_CAEEL
ID DERL1_CAEEL Reviewed; 245 AA.
AC Q93561;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Derlin-1 {ECO:0000305};
DE AltName: Full=Coelomocyte uptake defective protein 2 {ECO:0000303|PubMed:11560892};
DE AltName: Full=DER1-like protein 1 {ECO:0000303|PubMed:15215856};
DE AltName: Full=cDerlin-1 {ECO:0000303|PubMed:15215856};
GN Name=cup-2 {ECO:0000312|WormBase:F25D7.1}; Synonyms=der-1;
GN ORFNames=F25D7.1 {ECO:0000312|WormBase:F25D7.1};
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 [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 [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11560892; DOI=10.1093/genetics/159.1.133;
RA Fares H., Greenwald I.;
RT "Genetic analysis of endocytosis in Caenorhabditis elegans: coelomocyte
RT uptake defective mutants.";
RL Genetics 159:133-145(2001).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=15215856; DOI=10.1038/nature02656;
RA Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.;
RT "A membrane protein complex mediates retro-translocation from the ER lumen
RT into the cytosol.";
RL Nature 429:841-847(2004).
CC -!- FUNCTION: Specifically required for the degradation process of
CC misfolded endoplasmic reticulum (ER) luminal proteins. Participates in
CC the transfer of misfolded proteins from the ER to the cytosol, where
CC they are destroyed by the proteasome in a ubiquitin-dependent manner.
CC {ECO:0000269|PubMed:11560892, ECO:0000269|PubMed:15215856}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BUN8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9BUN8}.
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC {ECO:0000269|PubMed:15215856}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit coelomocyte uptake defective (cup)
CC phenotypes. Coelomocytes are scavenger cells that continuously and non-
CC specifically endocytose fluid from the pseudocoelom (body cavity).
CC Endocytosis by coelomocytes is not essential for growth or survival.
CC {ECO:0000269|PubMed:11560892}.
CC -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
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DR EMBL; Z78418; CAB01696.1; -; Genomic_DNA.
DR PIR; T21337; T21337.
DR RefSeq; NP_492721.1; NM_060320.6.
DR AlphaFoldDB; Q93561; -.
DR SMR; Q93561; -.
DR BioGRID; 38331; 7.
DR DIP; DIP-25923N; -.
DR IntAct; Q93561; 3.
DR STRING; 6239.F25D7.1.1; -.
DR EPD; Q93561; -.
DR PaxDb; Q93561; -.
DR PeptideAtlas; Q93561; -.
DR EnsemblMetazoa; F25D7.1.1; F25D7.1.1; WBGene00000843.
DR GeneID; 172915; -.
DR KEGG; cel:CELE_F25D7.1; -.
DR UCSC; F25D7.1.1; c. elegans.
DR CTD; 172915; -.
DR WormBase; F25D7.1; CE09629; WBGene00000843; cup-2.
DR eggNOG; KOG0858; Eukaryota.
DR GeneTree; ENSGT00530000063156; -.
DR HOGENOM; CLU_051898_3_1_1; -.
DR InParanoid; Q93561; -.
DR OMA; GTRFKAM; -.
DR OrthoDB; 1609512at2759; -.
DR PhylomeDB; Q93561; -.
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR PRO; PR:Q93561; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000843; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005769; C:early endosome; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005768; C:endosome; IDA:WormBase.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0005047; F:signal recognition particle binding; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:WormBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051788; P:response to misfolded protein; IMP:WormBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR007599; DER1.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF04511; DER1; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..245
FT /note="Derlin-1"
FT /id="PRO_0000219050"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..57
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..166
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 218..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 245 AA; 28465 MW; F0169684E0C27643 CRC64;
MDLENFLLGI PIVTRYWFLA STIIPLLGRF GFINVQWMFL QWDLVVNKFQ FWRPLTALIY
YPVTPQTGFH WLMMCYFLYN YSKALESETY RGRSADYLFM LIFNWFFCSG LCMALDIYFL
LEPMVISVLY VWCQVNKDTI VSFWFGMRFP ARYLPWVLWG FNAVLRGGGT NELVGILVGH
AYFFVALKYP DEYGVDLIST PEFLHRLIPD EDGGIHGQDG NIRGARQQPR GHQWPGGVGA
RLGGN
