DERL2_CAEEL
ID DERL2_CAEEL Reviewed; 237 AA.
AC Q21997; Q9UA08;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Derlin-2 {ECO:0000305};
DE AltName: Full=DER1-like protein 2;
DE AltName: Full=cDerlin-2 {ECO:0000303|PubMed:15215856};
GN ORFNames=R151.6 {ECO:0000312|WormBase:R151.6};
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 [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=10446229; DOI=10.1093/nar/27.17.3424;
RA Hough R.F., Lingam A.T., Bass B.L.;
RT "Caenorhabditis elegans mRNAs that encode a protein similar to ADARs derive
RT from an operon containing six genes.";
RL Nucleic Acids Res. 27:3424-3432(1999).
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 FUNCTION.
RX PubMed=15093775; DOI=10.1016/j.femsyr.2004.02.003;
RA Hitt R., Wolf D.H.;
RT "Der1p, a protein required for degradation of malfolded soluble proteins of
RT the endoplasmic reticulum: topology and Der1-like proteins.";
RL FEMS Yeast Res. 4:721-729(2004).
RN [4]
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: May be required for the degradation process of some specific
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 Its precise function remains unclear, but its ability to complement
CC der1 mutations in C.cerevisiae, suggests a similar function in the
CC degradation of ER misfolded proteins. {ECO:0000269|PubMed:15093775,
CC ECO:0000269|PubMed:15215856}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9GZP9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9GZP9}.
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC {ECO:0000269|PubMed:15215856}.
CC -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
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DR EMBL; AF143152; AAD37863.1; -; mRNA.
DR EMBL; FO081317; CCD70760.1; -; Genomic_DNA.
DR PIR; T16766; T16766.
DR RefSeq; NP_498590.4; NM_066189.5.
DR AlphaFoldDB; Q21997; -.
DR SMR; Q21997; -.
DR BioGRID; 41230; 5.
DR DIP; DIP-26928N; -.
DR STRING; 6239.R151.6; -.
DR EPD; Q21997; -.
DR PaxDb; Q21997; -.
DR PeptideAtlas; Q21997; -.
DR EnsemblMetazoa; R151.6.1; R151.6.1; WBGene00020109.
DR GeneID; 176018; -.
DR UCSC; R151.6; c. elegans.
DR CTD; 42005; -.
DR WormBase; R151.6; CE39620; WBGene00020109; -.
DR eggNOG; KOG0858; Eukaryota.
DR GeneTree; ENSGT00530000063156; -.
DR HOGENOM; CLU_051898_5_2_1; -.
DR InParanoid; Q21997; -.
DR OMA; WSRKNPD; -.
DR OrthoDB; 1609512at2759; -.
DR PhylomeDB; Q21997; -.
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-5358346; Hedgehog ligand biogenesis.
DR PRO; PR:Q21997; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020109; Expressed in germ line (C elegans) and 4 other tissues.
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; ISS:UniProtKB.
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:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
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..237
FT /note="Derlin-2"
FT /id="PRO_0000219051"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..54
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..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..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 212..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 28034 MW; F040E1C4DF0BB054 CRC64;
MNGVVAALEE MPPVTRFYTG ACVLLTTAVH LEFVTPFHLY FNWELIIRKY QFWRLITSFC
FFGSFGFSFL FNMIFTYRYC MMLEEGSFRG RRADFVYMFL FGAVLMILSG IFVQILFLGQ
AFTIMLVYIW SRRNPMIQMN FFGVLTFTAP YLPWVLLLFS LLLGNNAVVD FMGIACGHIY
FFLEDVFPFQ EHGKRFLKTP QWLVYLFDER RPEPLPEDER PGGFEWGDEQ PEQEQHD
