ID   DERL1_DICDI             Reviewed;         242 AA.
AC   Q54IC9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable derlin-1 homolog {ECO:0000305};
GN   Name=derl1 {ECO:0000312|dictyBase:DDB_G0288833};
GN   ORFNames=DDB_G0288833 {ECO:0000312|dictyBase:DDB_G0288833};
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: May be involved in the degradation process of specific
CC       misfolded endoplasmic reticulum (ER) luminal proteins. May also
CC       involved in endoplasmic reticulum stress-induced pre-emptive quality
CC       control, a mechanism that selectively attenuates the translocation of
CC       newly synthesized proteins into the endoplasmic reticulum and reroutes
CC       them to the cytosol for proteasomal degradation.
CC       {ECO:0000250|UniProtKB:Q9BUN8}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9BUN8}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9BUN8}.
CC   -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
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DR   EMBL; AAFI02000125; EAL63038.1; -; Genomic_DNA.
DR   RefSeq; XP_636548.1; XM_631456.1.
DR   AlphaFoldDB; Q54IC9; -.
DR   SMR; Q54IC9; -.
DR   STRING; 44689.DDB0266772; -.
DR   PaxDb; Q54IC9; -.
DR   EnsemblProtists; EAL63038; EAL63038; DDB_G0288833.
DR   GeneID; 8626833; -.
DR   KEGG; ddi:DDB_G0288833; -.
DR   dictyBase; DDB_G0288833; derl1.
DR   eggNOG; KOG0858; Eukaryota.
DR   HOGENOM; CLU_051898_5_2_1; -.
DR   InParanoid; Q54IC9; -.
DR   OMA; WSKRNPL; -.
DR   PhylomeDB; Q54IC9; -.
DR   PRO; PR:Q54IC9; -.
DR   Proteomes; UP000002195; Chromosome 5.
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:dictyBase.
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; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:dictyBase.
DR   InterPro; IPR007599; DER1.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   Pfam; PF04511; DER1; 1.
DR   SUPFAM; SSF144091; SSF144091; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Unfolded protein response.
FT   CHAIN           1..242
FT                   /note="Probable derlin-1 homolog"
FT                   /id="PRO_0000328358"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..98
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..167
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          214..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   242 AA;  28120 MW;  206056AF3E8839CF CRC64;
     MDGVKEWFNS IPPVSRYMFA IFLGIPVLAA MHLISFNYLY LDFTFTFKHF HLWRLITAPC
     IISSLGPMFL FNLIFFYQYT TRLESLNYAG KSDDYLFCII FISICNIIFG LIFEYYFLGT
     MTIMSLIYIY SRMNPTGTSN FYGFFSFKTI YLPWVFLVAH FLQTGHPPYS DFLAIVSGHI
     FFYLTDIYPR ANGVPALIKT PKFITNIFNK GDRNPNNVRR DPRTGRPIQE GGYNWGQGHA
     LG