ID   DERL2_PONAB             Reviewed;         239 AA.
AC   Q5RC74;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Derlin-2 {ECO:0000305};
DE   AltName: Full=Der1-like protein 2 {ECO:0000250|UniProtKB:Q9GZP9};
GN   Name=DERL2 {ECO:0000250|UniProtKB:Q9GZP9};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functional component of endoplasmic reticulum-associated
CC       degradation (ERAD) for misfolded lumenal glycoproteins, but not that of
CC       misfolded nonglycoproteins. May act by forming a channel that allows
CC       the retrotranslocation of misfolded glycoproteins into the cytosol
CC       where they are ubiquitinated and degraded by the proteasome. May
CC       mediate the interaction between VCP and misfolded glycoproteins. May
CC       also be involved in endoplasmic reticulum stress-induced pre-emptive
CC       quality control, a mechanism that selectively attenuates the
CC       translocation of newly synthesized proteins into the endoplasmic
CC       reticulum and reroutes them to the cytosol for proteasomal degradation.
CC       {ECO:0000250|UniProtKB:Q9GZP9}.
CC   -!- SUBUNIT: Forms homo- and heterooligomers with DERL3 and, to a lesser
CC       extent, with DERL1. Interacts with the SEL1L/SYVN1 and VCP/SELENOS
CC       protein complexes. Mediates association between VCP and EDEM1, as well
CC       as that between VCP and the misfolded glycoproteins. Interacts with
CC       OS9. Interacts with SELENOK and SELENOS. Interacts with the signal
CC       recognition particle/SRP and the SRP receptor; in the process of
CC       endoplasmic reticulum stress-induced pre-emptive quality control.
CC       Interacts with CCDC47 (By similarity). {ECO:0000250|UniProtKB:Q8BNI4,
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}.
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DR   EMBL; CR858406; CAH90633.1; -; mRNA.
DR   RefSeq; NP_001127312.1; NM_001133840.2.
DR   AlphaFoldDB; Q5RC74; -.
DR   SMR; Q5RC74; -.
DR   STRING; 9601.ENSPPYP00000008861; -.
DR   Ensembl; ENSPPYT00000009224; ENSPPYP00000008861; ENSPPYG00000007872.
DR   GeneID; 100174373; -.
DR   KEGG; pon:100174373; -.
DR   CTD; 51009; -.
DR   eggNOG; KOG0858; Eukaryota.
DR   GeneTree; ENSGT00530000063156; -.
DR   HOGENOM; CLU_051898_5_2_1; -.
DR   InParanoid; Q5RC74; -.
DR   OMA; WSRKNPD; -.
DR   OrthoDB; 1609512at2759; -.
DR   TreeFam; TF314715; -.
DR   Proteomes; UP000001595; Chromosome 17.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
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:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IEA:Ensembl.
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:0001967; P:suckling behavior; IEA:Ensembl.
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; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..239
FT                   /note="Derlin-2"
FT                   /id="PRO_0000219047"
FT   TOPO_DOM        1..56
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..98
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..150
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        172
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..239
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          215..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  27567 MW;  CAA228487C3CCB5C CRC64;
     MAYQSLRLEY LQIPPVSRAY TTACVLTTAA VQLELITPFQ LYFNPELIFK HFQIWRLITN
     FLFFGPVGFN FLFNMIFLYR YCRMLEEGSF RGRTADFVFM FLFGGFLMTL FGLFVSLVFL
     GQAFTIMLVY VWSRRNPYVR MNFFGLLNFQ APFLPWVLMG FSLLLGNSII VDLLGIAVGH
     IYFFLEDVFP NQPGGIRILK TPSILKAIFD TPDEDPNYNP LPEERPGGFA WGEGQRLGG