ID Q8MLW7_DROME Unreviewed; 498 AA. AC Q8MLW7; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 4. DT 22-FEB-2023, entry version 171. DE SubName: Full=X box binding protein-1, isoform E {ECO:0000313|EMBL:AAM70855.4}; GN Name=Xbp1 {ECO:0000313|EMBL:AAM70855.4, GN ECO:0000313|FlyBase:FBgn0021872}; GN Synonyms=138/3 {ECO:0000313|EMBL:AAM70855.4}, anon-EST:Liang-1.41 GN {ECO:0000313|EMBL:AAM70855.4}, CG 9415 {ECO:0000313|EMBL:AAM70855.4}, GN clone 1.41 {ECO:0000313|EMBL:AAM70855.4}, DM18 GN {ECO:0000313|EMBL:AAM70855.4}, Dmel\CG9415 GN {ECO:0000313|EMBL:AAM70855.4}, dmXBP1 {ECO:0000313|EMBL:AAM70855.4}, GN Dxbp-1 {ECO:0000313|EMBL:AAM70855.4}, dXbp-1 GN {ECO:0000313|EMBL:AAM70855.4}, l(2)k13803 GN {ECO:0000313|EMBL:AAM70855.4}, sXbp1 {ECO:0000313|EMBL:AAM70855.4}, GN XBP-1 {ECO:0000313|EMBL:AAM70855.4}, Xbp-1 GN {ECO:0000313|EMBL:AAM70855.4}, xbp-1 {ECO:0000313|EMBL:AAM70855.4}, GN XBP1 {ECO:0000313|EMBL:AAM70855.4}, xbp1 GN {ECO:0000313|EMBL:AAM70855.4}, XbpI {ECO:0000313|EMBL:AAM70855.4}; GN ORFNames=CG9415 {ECO:0000313|EMBL:AAM70855.4, GN ECO:0000313|FlyBase:FBgn0021872}, Dmel_CG9415 GN {ECO:0000313|EMBL:AAM70855.4}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AAM70855.4, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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 EMBL; AE013599; AAM70855.4; -; Genomic_DNA. DR RefSeq; NP_726032.4; NM_166427.4. DR AlphaFoldDB; Q8MLW7; -. DR SMR; Q8MLW7; -. DR IntAct; Q8MLW7; 5. DR STRING; 7227.FBpp0301746; -. DR PaxDb; Q8MLW7; -. DR DNASU; 44226; -. DR EnsemblMetazoa; FBtr0310045; FBpp0301746; FBgn0021872. DR GeneID; 44226; -. DR AGR; FB:FBgn0021872; -. DR CTD; 7494; -. DR FlyBase; FBgn0021872; Xbp1. DR VEuPathDB; VectorBase:FBgn0021872; -. DR eggNOG; KOG4005; Eukaryota. DR HOGENOM; CLU_880746_0_0_1; -. DR InParanoid; Q8MLW7; -. DR OrthoDB; 5406889at2759; -. DR BioGRID-ORCS; 44226; 0 hits in 1 CRISPR screen. DR ChiTaRS; Xbp1; fly. DR GenomeRNAi; 44226; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0021872; Expressed in spermathecum and 61 other tissues. DR ExpressionAtlas; Q8MLW7; baseline and differential. DR Genevisible; Q8MLW7; DM. DR GO; GO:0005634; C:nucleus; ISS:FlyBase. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:FlyBase. DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase. DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:FlyBase. DR GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IDA:FlyBase. DR GO; GO:0036490; P:regulation of translation in response to endoplasmic reticulum stress; IMP:FlyBase. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:FlyBase. DR GO; GO:0006642; P:triglyceride mobilization; IGI:FlyBase. DR CDD; cd14691; bZIP_XBP1; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR PANTHER; PTHR46542:SF1; BZIP DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR46542; X-BOX BINDING PROTEIN 1; 1. DR Pfam; PF07716; bZIP_2; 1. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 81..144 FT /note="BZIP" FT /evidence="ECO:0000259|PROSITE:PS50217" FT REGION 38..77 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 203..223 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 99..161 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 38..63 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 498 AA; 53106 MW; 3C8C92896C93CAD8 CRC64; MAPTANTVLI TVPRTAITSN NLPKLRPAPL TAALLKVSAT PSASPTPSSS GYASSSNMDD DNMAASQPKA KKRRLDHLTW EEKVQRKKLK NRVAAQTSRD RKKARMEEMD YEIKELTDRT EILQNKCDSL QAINESLLAK NHKLDSELEL LRQELAELKQ QQQHNTRCIS QSNASAGAEG CASTNLGSAA GYTTGGHTVV SASAGGAAEE QQEPGLTLES CGPLPTLQDM LGVDEEFDVK RLEELAESLL ADITADLETG AGASSPAAAQ DAGNAERLPG PMVGPAAERL ESDGHRANGL NVEQEQETEH KVSLNVQMLK INGNPQHTTA APASRTATIT ATAAASQLQA TPDTVYGTYD AKTNSITIVM DGDAVPVNEA VEEIYCDGVS AGDDSTDVIM KCPPPATSPS QVYLNVMNAV DNSDDEESFD PIDRFLRPRV KAISPLAKSP ALSLHSATSD HGYESILGSP TSVALTLPAD EDDFPWESNF DELFPSLI //