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Derlin-2 (Degradation in endoplasmic reticulum protein 2) (DERtrin-2) (Der1-like protein 2) (F-LAN-1) (F-LANa)

 DERL2_HUMAN             Reviewed;         239 AA.
Q9GZP9; Q9Y3A7;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-MAY-2022, entry version 164.
RecName: Full=Derlin-2 {ECO:0000303|PubMed:15215855};
AltName: Full=Degradation in endoplasmic reticulum protein 2;
Short=DERtrin-2;
AltName: Full=Der1-like protein 2 {ECO:0000303|PubMed:15215855};
AltName: Full=F-LAN-1 {ECO:0000312|EMBL:AAG43049.1};
AltName: Full=F-LANa {ECO:0000303|PubMed:11500051};
Name=DERL2 {ECO:0000312|HGNC:HGNC:17943};
Synonyms=DER2, FLANA {ECO:0000305|PubMed:11500051};
ORFNames=CGI-101 {ECO:0000312|EMBL:AAD34096.1}, SBBI53
{ECO:0000312|EMBL:AAF99603.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=11500051; DOI=10.1006/bbrc.2001.5390;
Ying H., Yu Y., Xu Y.;
"Cloning and characterization of F-LANa, upregulated in human liver
cancer.";
Biochem. Biophys. Res. Commun. 286:394-400(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Dendritic cell;
Zhang W., Wan T., Cao X.;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
PubMed=15215855; DOI=10.1038/nature02592;
Lilley B.N., Ploegh H.L.;
"A membrane protein required for dislocation of misfolded proteins from the
ER.";
Nature 429:834-840(2004).
[7]
FUNCTION, OLIGOMERIZATION, AND INTERACTION WITH SELENOS; SEL1L AND SYVN1.
PubMed=16186509; DOI=10.1073/pnas.0505014102;
Lilley B.N., Ploegh H.L.;
"Multiprotein complexes that link dislocation, ubiquitination, and
extraction of misfolded proteins from the endoplasmic reticulum membrane.";
Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, TISSUE SPECIFICITY,
INDUCTION, OLIGOMERIZATION, AND INTERACTION WITH VCP AND EDEM1.
PubMed=16449189; DOI=10.1083/jcb.200507057;
Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.;
"Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein
response and are required for ER-associated degradation.";
J. Cell Biol. 172:383-393(2006).
[9]
INTERACTION WITH OS9.
PubMed=19084021; DOI=10.1016/j.jmb.2008.11.045;
Alcock F., Swanton E.;
"Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress
and facilitates ubiquitination of misfolded glycoproteins.";
J. Mol. Biol. 385:1032-1042(2009).
[10]
INTERACTION WITH SELENOK AND SELENOS.
PubMed=22016385; DOI=10.1074/jbc.m111.310920;
Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L.,
Gladyshev V.N.;
"Selenoprotein K binds multiprotein complexes and is involved in the
regulation of endoplasmic reticulum homeostasis.";
J. Biol. Chem. 286:42937-42948(2011).
[11]
FUNCTION, AND SUBUNIT.
PubMed=26565908; DOI=10.1016/j.celrep.2015.09.047;
Kadowaki H., Nagai A., Maruyama T., Takami Y., Satrimafitrah P., Kato H.,
Honda A., Hatta T., Natsume T., Sato T., Kai H., Ichijo H., Nishitoh H.;
"Pre-emptive quality control protects the ER from protein overload via the
proximity of ERAD components and SRP.";
Cell Rep. 13:944-956(2015).
-!- FUNCTION: Functional component of endoplasmic reticulum-associated
degradation (ERAD) for misfolded lumenal glycoproteins, but not that of
misfolded nonglycoproteins. May act by forming a channel that allows
the retrotranslocation of misfolded glycoproteins into the cytosol
where they are ubiquitinated and degraded by the proteasome. May
mediate the interaction between VCP and misfolded glycoproteins
(PubMed:16186509, PubMed:16449189). May also be involved in endoplasmic
reticulum stress-induced pre-emptive quality control, a mechanism that
selectively attenuates the translocation of newly synthesized proteins
into the endoplasmic reticulum and reroutes them to the cytosol for
proteasomal degradation (PubMed:26565908).
{ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189,
ECO:0000269|PubMed:26565908}.
-!- FUNCTION: (Microbial infection) In contrast to DERL1, it is not
involved in the degradation of MHC class I heavy chains following
infection by cytomegaloviruses. {ECO:0000269|PubMed:15215855}.
-!- SUBUNIT: Forms homo- and heterooligomers with DERL3 and, to a lesser
extent, with DERL1 (PubMed:16186509). Interacts with the SEL1L/SYVN1
and VCP/SELENOS protein complexes (PubMed:16186509). Mediates
association between VCP and EDEM1, as well as that between VCP and the
misfolded glycoproteins (PubMed:16449189). Interacts with OS9
(PubMed:19084021). Interacts with SELENOK and SELENOS
(PubMed:22016385). Interacts with the signal recognition particle/SRP
and the SRP receptor; in the process of endoplasmic reticulum stress-
induced pre-emptive quality control (PubMed:26565908). Interacts with
CCDC47 (By similarity). {ECO:0000250|UniProtKB:Q8BNI4,
ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16449189,
ECO:0000269|PubMed:19084021, ECO:0000269|PubMed:22016385,
ECO:0000269|PubMed:26565908}.
-!- INTERACTION:
Q9GZP9; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-7962814, EBI-517508;
Q9GZP9; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-7962814, EBI-713304;
Q9GZP9; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-7962814, EBI-10172290;
Q9GZP9; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-7962814, EBI-10171774;
Q9GZP9; Q00013: MPP1; NbExp=3; IntAct=EBI-7962814, EBI-711788;
Q9GZP9; P43378: PTPN9; NbExp=3; IntAct=EBI-7962814, EBI-742898;
Q9GZP9; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-7962814, EBI-3232108;
Q9GZP9; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-7962814, EBI-2854842;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15215855, ECO:0000269|PubMed:16449189}; Multi-pass
membrane protein {ECO:0000269|PubMed:15215855,
ECO:0000269|PubMed:16449189}.
-!- TISSUE SPECIFICITY: Ubiquitous. Overexpressed in various
hepatocarcinomas. {ECO:0000269|PubMed:11500051,
ECO:0000269|PubMed:16449189}.
-!- INDUCTION: Up-regulated in response to endoplasmic reticulum stress via
the ERN1-XBP1 pathway of the unfolded protein response (UPR).
{ECO:0000269|PubMed:16449189}.
-!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD34096.1; Type=Frameshift; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AF132289; AAG43049.1; -; mRNA.
EMBL; AF208065; AAL14869.1; -; mRNA.
EMBL; AF151859; AAD34096.1; ALT_FRAME; mRNA.
EMBL; AF242523; AAF99603.1; -; mRNA.
EMBL; CR457202; CAG33483.1; -; mRNA.
EMBL; BC010890; AAH10890.1; -; mRNA.
CCDS; CCDS11073.1; -.
PIR; JC7752; JC7752.
RefSeq; NP_001291708.1; NM_001304779.1.
RefSeq; NP_057125.2; NM_016041.4.
AlphaFoldDB; Q9GZP9; -.
SMR; Q9GZP9; -.
BioGRID; 119216; 141.
CORUM; Q9GZP9; -.
IntAct; Q9GZP9; 57.
MINT; Q9GZP9; -.
STRING; 9606.ENSP00000158771; -.
TCDB; 3.A.16.1.4; the endoplasmic reticular retrotranslocon (er-rt) family.
GlyGen; Q9GZP9; 1 site, 1 O-linked glycan (1 site).
iPTMnet; Q9GZP9; -.
PhosphoSitePlus; Q9GZP9; -.
BioMuta; DERL2; -.
DMDM; 50400648; -.
EPD; Q9GZP9; -.
jPOST; Q9GZP9; -.
MassIVE; Q9GZP9; -.
MaxQB; Q9GZP9; -.
PaxDb; Q9GZP9; -.
PeptideAtlas; Q9GZP9; -.
PRIDE; Q9GZP9; -.
ProteomicsDB; 80110; -.
Antibodypedia; 23707; 140 antibodies from 23 providers.
DNASU; 51009; -.
Ensembl; ENST00000158771.9; ENSP00000158771.4; ENSG00000072849.11.
GeneID; 51009; -.
KEGG; hsa:51009; -.
MANE-Select; ENST00000158771.9; ENSP00000158771.4; NM_016041.5; NP_057125.2.
UCSC; uc002gcc.2; human.
CTD; 51009; -.
DisGeNET; 51009; -.
GeneCards; DERL2; -.
HGNC; HGNC:17943; DERL2.
HPA; ENSG00000072849; Low tissue specificity.
MIM; 610304; gene.
neXtProt; NX_Q9GZP9; -.
OpenTargets; ENSG00000072849; -.
PharmGKB; PA134896343; -.
VEuPathDB; HostDB:ENSG00000072849; -.
eggNOG; KOG0858; Eukaryota.
GeneTree; ENSGT00530000063156; -.
HOGENOM; CLU_051898_5_2_1; -.
InParanoid; Q9GZP9; -.
OMA; WSRKNPD; -.
OrthoDB; 1609512at2759; -.
PhylomeDB; Q9GZP9; -.
TreeFam; TF314715; -.
PathwayCommons; Q9GZP9; -.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
SignaLink; Q9GZP9; -.
BioGRID-ORCS; 51009; 157 hits in 1075 CRISPR screens.
ChiTaRS; DERL2; human.
GeneWiki; Derlin-2; -.
GenomeRNAi; 51009; -.
Pharos; Q9GZP9; Tbio.
PRO; PR:Q9GZP9; -.
Proteomes; UP000005640; Chromosome 17.
RNAct; Q9GZP9; protein.
Bgee; ENSG00000072849; Expressed in right testis and 233 other tissues.
ExpressionAtlas; Q9GZP9; baseline and differential.
Genevisible; Q9GZP9; HS.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
GO; GO:0005047; F:signal recognition particle binding; IDA:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IBA:GO_Central.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:UniProtKB.
GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
InterPro; IPR007599; DER1.
InterPro; IPR035952; Rhomboid-like_sf.
Pfam; PF04511; DER1; 1.
SUPFAM; SSF144091; SSF144091; 1.
1: Evidence at protein level;
Endoplasmic reticulum; Host-virus interaction; Membrane;
Reference proteome; Transmembrane; Transmembrane helix;
Unfolded protein response.
CHAIN 1..239
/note="Derlin-2"
/id="PRO_0000219045"
TOPO_DOM 1..57
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 58..78
/note="Helical; Name=1"
/evidence="ECO:0000255"
TOPO_DOM 79..96
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 97..117
/note="Helical; Name=2"
/evidence="ECO:0000255"
TOPO_DOM 118..150
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 151..171
/note="Helical; Name=3"
/evidence="ECO:0000255"
TOPO_DOM 172
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 173..193
/note="Helical; Name=4"
/evidence="ECO:0000255"
TOPO_DOM 194..239
/note="Cytoplasmic"
/evidence="ECO:0000255"
REGION 215..239
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
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


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