ID   DERL3_BOVIN             Reviewed;         231 AA.
AC   Q0P5E4;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Derlin-3 {ECO:0000305};
DE   AltName: Full=Der1-like protein 3 {ECO:0000250|UniProtKB:Q96Q80};
GN   Name=DERL3 {ECO:0000250|UniProtKB:Q96Q80};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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 the misfolded glycoproteins.
CC       May 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:Q96Q80}.
CC   -!- SUBUNIT: Forms homo- and heterooligomers with DERL2 and, to a lesser
CC       extent, with DERL1. Interacts with VCP and EDEM1. Interacts with
CC       SELENOK and SELENOS. Interacts with the signal recognition particle/SRP
CC       and the SRP receptor; in the process of endoplasmic reticulum stress-
CC       induced pre-emptive quality control. {ECO:0000250|UniProtKB:Q96Q80}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q96Q80}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q96Q80}.
CC   -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
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DR   EMBL; BC120164; AAI20165.1; -; mRNA.
DR   RefSeq; NP_001069791.1; NM_001076323.2.
DR   AlphaFoldDB; Q0P5E4; -.
DR   SMR; Q0P5E4; -.
DR   STRING; 9913.ENSBTAP00000029459; -.
DR   PaxDb; Q0P5E4; -.
DR   GeneID; 614334; -.
DR   KEGG; bta:614334; -.
DR   CTD; 91319; -.
DR   eggNOG; KOG0858; Eukaryota.
DR   InParanoid; Q0P5E4; -.
DR   OrthoDB; 1609512at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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: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:0018279; P:protein N-linked glycosylation via asparagine; 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; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..231
FT                   /note="Derlin-3"
FT                   /id="PRO_0000284077"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..43
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..58
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..157
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   231 AA;  26248 MW;  BA834B1BC45C3B04 CRC64;
     MAWQGLATEF LQVPAVTRTY TAACVLTTAA VQLELLSPFQ LYFNPHLVFR KFQVWRLITN
     FLFFGPLGFS FFFNMLFVFR YCRMLEEGSF RGRTADFVFM FLFGGVLMTL LGLLGSLFFL
     GQALTAMLVY VWSRRSPGVR VNFFGLLTFQ APFLPWALMG LPMLLGNSIL VDLLGIAVGH
     VYYFLEDVFP NQPGGKRLLL TPSFLKLLLD APEEDPNYLP LPEEQPGPLQ Q