DERL3_MOUSE
ID DERL3_MOUSE Reviewed; 228 AA.
AC Q9D8K3; Q3T9L7; Q99KC6; Q9D954;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Derlin-3 {ECO:0000303|PubMed:15215855};
DE AltName: Full=Degradation in endoplasmic reticulum protein 3;
DE AltName: Full=Der1-like protein 3 {ECO:0000303|PubMed:15215855};
DE AltName: Full=Protein IZP6 {ECO:0000303|PubMed:11422294};
GN Name=Derl3 {ECO:0000312|MGI:MGI:1917627};
GN Synonyms=Der3, Izp6 {ECO:0000303|PubMed:11422294};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=CNS;
RX PubMed=11422294; DOI=10.1046/j.1440-169x.2001.00569.x;
RA Tsukahara M., Ji Z.-S., Noguchi S., Tsunoo H.;
RT "A novel putative transmembrane protein, IZP6, is expressed in neural cells
RT during embryogenesis.";
RL Dev. Growth Differ. 43:285-293(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pancreas, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-228 (ISOFORM 1).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION.
RX PubMed=15215855; DOI=10.1038/nature02592;
RA Lilley B.N., Ploegh H.L.;
RT "A membrane protein required for dislocation of misfolded proteins from the
RT ER.";
RL Nature 429:834-840(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH SELENOK AND SELENOS.
RX PubMed=22016385; DOI=10.1074/jbc.m111.310920;
RA Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Selenoprotein K binds multiprotein complexes and is involved in the
RT regulation of endoplasmic reticulum homeostasis.";
RL J. Biol. Chem. 286:42937-42948(2011).
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 (By similarity). Interacts with VCP and EDEM1 (By
CC similarity). Interacts with SELENOK and SELENOS (PubMed:22016385).
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 (By similarity). {ECO:0000250|UniProtKB:Q96Q80,
CC ECO:0000269|PubMed:22016385}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96Q80}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96Q80}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8K3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8K3-2; Sequence=VSP_011090;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, lung, liver, spleen and
CC testis. Expressed at intermediate level in kidney. Weakly or not
CC expressed in brain, heart and skeletal muscle.
CC {ECO:0000269|PubMed:11422294}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neural cells during enbryogenesis.
CC From 11.5 dpc until 14.5 dpc, it is mainly expressed in the forebrain.
CC From 15.5 dpc until birth, expression in the forebrain becomes weaker
CC but is still observed in the olfactory bulb and the skin around the
CC eyes, nose, limbs and tail, showing that its pattern of expression
CC changes from the central nervous system to the peripheral tissues
CC during development. {ECO:0000269|PubMed:11422294}.
CC -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04729.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB047555; BAB32788.1; -; mRNA.
DR EMBL; AK007348; BAB24977.1; -; mRNA.
DR EMBL; AK007948; BAB25367.1; -; mRNA.
DR EMBL; AK172429; BAE43003.1; -; mRNA.
DR EMBL; BC004729; AAH04729.1; ALT_INIT; mRNA.
DR CCDS; CCDS23935.1; -. [Q9D8K3-1]
DR RefSeq; NP_077760.1; NM_024440.2. [Q9D8K3-1]
DR AlphaFoldDB; Q9D8K3; -.
DR SMR; Q9D8K3; -.
DR STRING; 10090.ENSMUSP00000009236; -.
DR MaxQB; Q9D8K3; -.
DR PaxDb; Q9D8K3; -.
DR PRIDE; Q9D8K3; -.
DR ProteomicsDB; 279402; -. [Q9D8K3-1]
DR ProteomicsDB; 279403; -. [Q9D8K3-2]
DR Antibodypedia; 23832; 74 antibodies from 21 providers.
DR Ensembl; ENSMUST00000009236; ENSMUSP00000009236; ENSMUSG00000009092. [Q9D8K3-1]
DR GeneID; 70377; -.
DR KEGG; mmu:70377; -.
DR UCSC; uc007ftj.1; mouse. [Q9D8K3-1]
DR UCSC; uc007ftk.1; mouse. [Q9D8K3-2]
DR CTD; 91319; -.
DR MGI; MGI:1917627; Derl3.
DR VEuPathDB; HostDB:ENSMUSG00000009092; -.
DR eggNOG; KOG0858; Eukaryota.
DR GeneTree; ENSGT00530000063156; -.
DR HOGENOM; CLU_051898_5_2_1; -.
DR InParanoid; Q9D8K3; -.
DR OMA; WSKRNPL; -.
DR PhylomeDB; Q9D8K3; -.
DR TreeFam; TF314715; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 70377; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Derl3; mouse.
DR PRO; PR:Q9D8K3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D8K3; protein.
DR Bgee; ENSMUSG00000009092; Expressed in saliva-secreting gland and 111 other tissues.
DR ExpressionAtlas; Q9D8K3; baseline and differential.
DR Genevisible; Q9D8K3; MM.
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; ISO:MGI.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005047; F:signal recognition particle binding; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:MGI.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:MGI.
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 Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR007599; DER1.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF04511; DER1; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..228
FT /note="Derlin-3"
FT /id="PRO_0000219049"
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..57
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..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..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 110..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011090"
FT CONFLICT 15
FT /note="A -> T (in Ref. 3; AAH04729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 25978 MW; C60D830C83D42D0D CRC64;
MAGQRLAAGF LQVPAVTRAY TAACVLTTAA VQLELLSPFQ LYFNPHLVFR KFQVWRLITT
FLFFGPLGFG FFFNMLFVFR YCRMLEEGSF RGRKADFVFM FLFGGVLMTL LGFLGSLFFL
GQALMAMLVY VWSRRSPHVR VNFFGLLNFQ APFLPWALMG FSLLLGNSVV TDLLGILVGH
IYYFLEDVFP NQPGGKRLLL TPSVLKLLLD DPQEDPDYLP LPEEQPEL
