DERL1_PONAB
ID DERL1_PONAB Reviewed; 251 AA.
AC Q5R9W3;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Derlin-1 {ECO:0000305};
DE AltName: Full=Der1-like protein 1 {ECO:0000250|UniProtKB:Q9BUN8};
GN Name=DERL1 {ECO:0000250|UniProtKB:Q9BUN8};
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=Heart;
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 proteins. Forms homotetramers
CC which encircle a large channel traversing the endoplasmic reticulum
CC (ER) membrane. This allows the retrotranslocation of misfolded proteins
CC from the ER into the cytosol where they are ubiquitinated and degraded
CC by the proteasome. The channel has a lateral gate within the membrane
CC which provides direct access to membrane proteins with no need to
CC reenter the ER lumen first. May mediate the interaction between VCP and
CC the misfolded protein. Also involved in endoplasmic reticulum stress-
CC induced pre-emptive quality control, a mechanism that selectively
CC attenuates the translocation of newly synthesized proteins into the
CC endoplasmic reticulum and reroutes them to the cytosol for proteasomal
CC degradation. By controlling the steady-state expression of the IGF1R
CC receptor, indirectly regulates the insulin-like growth factor receptor
CC signaling pathway. {ECO:0000250|UniProtKB:Q9BUN8}.
CC -!- SUBUNIT: Homotetramer. The four subunits of the tetramer are arranged
CC in a twofold symmetry. Forms homo- and heterooligomers with DERL2 and
CC DERL3; binding to DERL3 is poorer than that between DERL2 and DERL3.
CC Interacts (via SHP-box motif) with VCP. Interacts with AMFR, SELENOS,
CC SEL1L, SELENOK and SYVN1, as well as with SEL1L-SYVN1 and VCP-SELENOS
CC protein complexes; this interaction is weaker than that observed
CC between DERL2 and these complexes. Interacts with NGLY1 and YOD1. Does
CC not bind to EDEM1. Interacts with DNAJB9. Interacts with RNF103.
CC Interacts with HM13. Interacts with XBP1 isoform 1 (via
CC luminal/ectodomain domain); the interaction obviates the need for
CC ectodomain shedding prior HM13/SPP-mediated XBP1 isoform 1 cleavage.
CC Interacts with the signal recognition particle/SRP and the SRP
CC receptor; in the process of endoplasmic reticulum stress-induced pre-
CC emptive quality control. May interact with UBXN6. Interacts with
CC ZFAND2B; probably through VCP. Interacts with CCDC47. Interacts with
CC C18orf32. May interact with TRAM1. {ECO:0000250|UniProtKB:Q99J56,
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; CR859268; CAH91447.1; -; mRNA.
DR RefSeq; NP_001125851.1; NM_001132379.1.
DR AlphaFoldDB; Q5R9W3; -.
DR SMR; Q5R9W3; -.
DR STRING; 9601.ENSPPYP00000021151; -.
DR Ensembl; ENSPPYT00000053447; ENSPPYP00000027809; ENSPPYG00000018852.
DR GeneID; 100172781; -.
DR KEGG; pon:100172781; -.
DR CTD; 79139; -.
DR eggNOG; KOG0858; Eukaryota.
DR GeneTree; ENSGT00530000063156; -.
DR HOGENOM; CLU_051898_3_1_1; -.
DR InParanoid; Q5R9W3; -.
DR OrthoDB; 1609512at2759; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IEA:Ensembl.
DR GO; GO:0036502; C:Derlin-1-VIMP complex; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:Ensembl.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl.
DR GO; GO:0005047; F:signal recognition particle binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
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 Acetylation; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Unfolded protein response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT CHAIN 2..251
FT /note="Derlin-1"
FT /id="PRO_0000219044"
FT TOPO_DOM 2..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TRANSMEM 16..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TOPO_DOM 32..69
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TRANSMEM 70..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TOPO_DOM 90..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TOPO_DOM 116..122
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TRANSMEM 123..137
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TOPO_DOM 138..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TRANSMEM 155..166
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TOPO_DOM 167..170
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TRANSMEM 171..189
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT TOPO_DOM 190..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT REGION 229..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 241..248
FT /note="SHP-box"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN8"
SQ SEQUENCE 251 AA; 28810 MW; 59F3B62CE9703EA9 CRC64;
MSDIGDWFRS IPAITRYWFA ATVAVPLVGK LGLISPAYLF LWPEAFLYRF QIWRPITATF
YFPVGPGTGF LYLVNLYFLY HYSTRLETGA FDGRPADYLF MLLFNWICIV ITGLAMDMQL
LMIPLIMSVL YVWAQLNRDM IVSFWFGTRF KACYLPWVIL GFNYIIGGSV INELIGNLVG
HLYFFLMFRY PMDLGGRNFL STPQFLYRWL PSRRGGVSGF GVPPASMRRA ADQNGGGGRH
NWGQGFRLGD Q
