ID   DERL2_DICDI             Reviewed;         254 AA.
AC   Q54NN1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable derlin-2 homolog {ECO:0000305};
GN   Name=derl2 {ECO:0000312|dictyBase:DDB_G0285131};
GN   ORFNames=DDB_G0285131 {ECO:0000312|dictyBase:DDB_G0285131};
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 be
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:Q9GZP9}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9GZP9}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9GZP9}.
CC   -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000074; EAL64878.1; -; Genomic_DNA.
DR   RefSeq; XP_639885.1; XM_634793.1.
DR   AlphaFoldDB; Q54NN1; -.
DR   SMR; Q54NN1; -.
DR   STRING; 44689.DDB0266773; -.
DR   PaxDb; Q54NN1; -.
DR   EnsemblProtists; EAL64878; EAL64878; DDB_G0285131.
DR   GeneID; 8624956; -.
DR   KEGG; ddi:DDB_G0285131; -.
DR   dictyBase; DDB_G0285131; derl2.
DR   eggNOG; KOG0858; Eukaryota.
DR   HOGENOM; CLU_051898_5_2_1; -.
DR   InParanoid; Q54NN1; -.
DR   OMA; WSRKNPD; -.
DR   PhylomeDB; Q54NN1; -.
DR   PRO; PR:Q54NN1; -.
DR   Proteomes; UP000002195; Chromosome 4.
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..254
FT                   /note="Probable derlin-2 homolog"
FT                   /id="PRO_0000328359"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..95
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..146
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  29964 MW;  0EBBFCC46C3E3FCF CRC64;
     MAQPFEDWYK NLPIVTKIYM TGCVVTSVSV YLGLVGPLRL YLNFPLVFGK YEFWRLFTNF
     FFYDEIGMNF FFHMYFLVRH SRLLEESSFR GRSADYLFMW IFGSFLLLIM DAFLFYTKIV
     TKVLFLAPSI AFMVIYVWSR RNPNMHISFL GLFTFSAPYL PWVILIMGYL FNHDLTTDLL
     GAVAGHAYYF LEDAYPLISN RRLLKTPGFL KNLMDGQEQP IVDAHQQQEV QQAQQQEVQQ
     PVQNFLNEDD LDQQ