ID   Q5RKH9_RAT              Unreviewed;       251 AA.
AC   Q5RKH9; F7FNS3;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Derlin {ECO:0000256|RuleBase:RU363059};
GN   Name=Derl1 {ECO:0000313|Ensembl:ENSRNOP00000007484.5,
GN   ECO:0000313|RGD:1311835};
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:ENSRNOP00000007484.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000007484.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007484.5,
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:ENSRNOP00000007484.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007484.5};
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}.
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DR   RefSeq; NP_001014224.1; NM_001014202.1.
DR   AlphaFoldDB; Q5RKH9; -.
DR   SMR; Q5RKH9; -.
DR   PhosphoSitePlus; Q5RKH9; -.
DR   Ensembl; ENSRNOT00000007484.6; ENSRNOP00000007484.5; ENSRNOG00000005551.7.
DR   GeneID; 362912; -.
DR   KEGG; rno:362912; -.
DR   UCSC; RGD:1311835; rat.
DR   AGR; RGD:1311835; -.
DR   CTD; 79139; -.
DR   RGD; 1311835; Derl1.
DR   eggNOG; KOG0858; Eukaryota.
DR   GeneTree; ENSGT00530000063156; -.
DR   HOGENOM; CLU_051898_3_1_1; -.
DR   OMA; LWRCVTS; -.
DR   OrthoDB; 1123482at2759; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:RGD.
DR   GO; GO:0036502; C:Derlin-1-VIMP complex; ISO:RGD.
DR   GO; GO:0005769; C:early endosome; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:RGD.
DR   GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0042288; F:MHC class I protein binding; ISO:RGD.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0002020; F:protease binding; ISO:RGD.
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:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR   GO; GO:0034620; P:cellular response to unfolded protein; ISO:RGD.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR   GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:RGD.
DR   GO; GO:0036503; P:ERAD pathway; ISO:RGD.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR   GO; GO:0006986; P:response to unfolded protein; ISO:RGD.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
DR   InterPro; IPR007599; DER1.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   PANTHER; PTHR11009; DER1-LIKE PROTEIN, DERLIN; 1.
DR   PANTHER; PTHR11009:SF1; DERLIN-1; 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        17..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363059"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363059"
FT   TRANSMEM        101..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363059"
FT   TRANSMEM        154..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363059"
FT   REGION          229..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  28835 MW;  2E1B79DEAFD3FDC8 CRC64;
     MSDIGDWFRS IPAITRYWFA ATVAVPLIGK LGIISPAYFF LWPEAFLYRF QIWRPFTATF
     YFPVGPGTGF LYLVNLYFLY QYSTRLEAGA FDGRPADYLF MLLFNWICIV ITGLAMDMQL
     LMIPLIMSVL YVWAQLNRDL IVSFWFGTRF KACYLPWVIL GFNYIIGGSV INELIGNLVG
     HLYFFLMFRY PMDLGGRNFL STPQFLYRWL PSRRGGVSGF GVPPASMRRA ADQNGGGGRH
     NWGQGFRLGD Q
//