ID G3V8X2_RAT Unreviewed; 228 AA. AC G3V8X2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Derlin {ECO:0000256|RuleBase:RU363059}; GN Name=Derl3 {ECO:0000313|Ensembl:ENSRNOP00000029737.4, GN ECO:0000313|RGD:1597373}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000029737.4, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000029737.4, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000029737.4, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000029737.4} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000029737.4}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Functional component of endoplasmic reticulum-associated CC degradation (ERAD) for misfolded lumenal proteins. May act by forming a CC channel that allows the retrotranslocation of misfolded proteins into CC the cytosol where they are ubiquitinated and degraded by the CC proteasome. {ECO:0000256|RuleBase:RU363059}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363059}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477, CC ECO:0000256|RuleBase:RU363059}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the derlin family. CC {ECO:0000256|ARBA:ARBA00008917, ECO:0000256|RuleBase:RU363059}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; NP_001103047.2; NM_001109577.1. DR RefSeq; XP_006256387.1; XM_006256325.3. DR RefSeq; XP_008772062.1; XM_008773840.2. DR RefSeq; XP_008772063.1; XM_008773841.2. DR AlphaFoldDB; G3V8X2; -. DR SMR; G3V8X2; -. DR STRING; 10116.ENSRNOP00000029737; -. DR PaxDb; 10116-ENSRNOP00000029737; -. DR Ensembl; ENSRNOT00000038623.6; ENSRNOP00000029737.4; ENSRNOG00000028243.6. DR GeneID; 690315; -. DR KEGG; rno:690315; -. DR AGR; RGD:1597373; -. DR CTD; 91319; -. DR RGD; 1597373; Derl3. DR eggNOG; KOG0858; Eukaryota. DR GeneTree; ENSGT00530000063156; -. DR HOGENOM; CLU_051898_5_2_1; -. DR OMA; RWLETPM; -. DR OrthoDB; 5475101at2759; -. DR TreeFam; TF314715; -. DR Reactome; R-RNO-382556; ABC-family proteins mediated transport. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000028243; Expressed in pancreas and 17 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD. DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central. DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD. DR GO; GO:0005047; F:signal recognition particle binding; ISO:RGD. DR GO; GO:1990381; F:ubiquitin-specific protease binding; IBA:GO_Central. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD. DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:RGD. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:RGD. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD. DR Gene3D; 1.20.1540.10; Rhomboid-like; 1. DR InterPro; IPR007599; DER1. DR InterPro; IPR035952; Rhomboid-like_sf. DR PANTHER; PTHR11009; DER1-LIKE PROTEIN, DERLIN; 1. DR PANTHER; PTHR11009:SF4; DERLIN-3; 1. DR Pfam; PF04511; DER1; 1. DR SUPFAM; SSF144091; Rhomboid-like; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, KW ECO:0000256|RuleBase:RU363059}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363059}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU363059}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU363059}. FT TRANSMEM 20..42 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363059" FT TRANSMEM 54..79 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363059" FT TRANSMEM 99..132 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363059" FT TRANSMEM 153..183 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363059" SQ SEQUENCE 228 AA; 26082 MW; 86C3F8FD4037DF2C CRC64; MAGQRLAADF LQVPAVTRAY TAACVLTTAA VQLELLSPFQ LYFNPHLVFR KFQVWRLITT FLFFGPLGFG FFFNMLFVFR YCRMLEEGSF RGRKADFVFM FLFGGVLMTL LGFLGSMFFL GQALMAMLVY VWSRRSPHVR VNFFGLLNFQ APFLPWALMG FSLLLGNSVI TDLLGIIVGH IYYFLEDVFP NQPGGKRLLL TPSFLKLLLD DPQEDPNYLP LPEEHPEA //