L2GL_DROME
ID L2GL_DROME Reviewed; 1161 AA.
AC P08111; A4UZW0; D0IQ91; D0IQJ0; Q0E8V5; Q24377; Q8IPV4; Q8IPV5; Q9VPI1;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Lethal(2) giant larvae protein;
GN Name=l(2)gl; ORFNames=CG2671;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P127).
RX PubMed=16453778; DOI=10.1002/j.1460-2075.1987.tb02432.x;
RA Luetzelschwab R., Klaembt C., Rossa R., Schmidt O.;
RT "A protein product of the Drosophila recessive tumor gene, l(2) gl,
RT potentially has cell adhesion properties.";
RL EMBO J. 6:1791-1797(1987).
RN [2]
RP ERRATUM OF PUBMED:16453778.
RA Luetzelschwab R., Klaembt C., Rossa R., Schmidt O.;
RL EMBO J. 6:2856-2856(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ALTERNATIVE SPLICING
RP (ISOFORMS P127 AND P78).
RC TISSUE=Embryo;
RX PubMed=3036370; DOI=10.1016/0092-8674(87)90217-0;
RA Jacob L., Opper M., Metzroth B., Phannavong B., Mechler B.M.;
RT "Structure of the l(2)gl gene of Drosophila and delimitation of its tumor
RT suppressor domain.";
RL Cell 50:215-225(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., 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.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
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., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P127).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND P127).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12545176; DOI=10.1038/ncb922;
RA Albertson R., Doe C.Q.;
RT "Dlg, Scrib and Lgl regulate neuroblast cell size and mitotic spindle
RT asymmetry.";
RL Nat. Cell Biol. 5:166-170(2003).
RN [9]
RP FUNCTION, INTERACTION WITH APKC, AND PHOSPHORYLATION BY APKC.
RX PubMed=18094021; DOI=10.1242/dev.016253;
RA Tian A.G., Deng W.M.;
RT "Lgl and its phosphorylation by aPKC regulate oocyte polarity formation in
RT Drosophila.";
RL Development 135:463-471(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-484; SER-679;
RP SER-808; SER-869; SER-876; SER-887; SER-889; SER-893 AND SER-1013, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [11]
RP INTERACTION WITH MAHJ.
RX PubMed=20644714; DOI=10.1371/journal.pbio.1000422;
RA Tamori Y., Bialucha C.U., Tian A.G., Kajita M., Huang Y.C., Norman M.,
RA Harrison N., Poulton J., Ivanovitch K., Disch L., Liu T., Deng W.M.,
RA Fujita Y.;
RT "Involvement of Lgl and Mahjong/VprBP in cell competition.";
RL PLoS Biol. 8:E1000422-E1000422(2010).
RN [12]
RP SUBCELLULAR LOCATION, DOMAIN, PHOSPHORYLATION, AND MUTAGENESIS OF
RP 647-ARG--GLN-681; 653-ARG-ARG-654; SER-656; 658-LYS-LYS-659; SER-660;
RP SER-664 AND 666-ARG-ARG-667.
RX PubMed=26481050; DOI=10.1016/j.devcel.2015.09.016;
RA Bailey M.J., Prehoda K.E.;
RT "Establishment of Par-Polarized Cortical Domains via Phosphoregulated
RT Membrane Motifs.";
RL Dev. Cell 35:199-210(2015).
RN [13]
RP INTERACTION WITH BALL.
RX PubMed=31735666; DOI=10.1016/j.devcel.2019.10.009;
RA Link N., Chung H., Jolly A., Withers M., Tepe B., Arenkiel B.R., Shah P.S.,
RA Krogan N.J., Aydin H., Geckinli B.B., Tos T., Isikay S., Tuysuz B.,
RA Mochida G.H., Thomas A.X., Clark R.D., Mirzaa G.M., Lupski J.R.,
RA Bellen H.J.;
RT "Mutations in ANKLE2, a ZIKA Virus Target, Disrupt an Asymmetric Cell
RT Division Pathway in Drosophila Neuroblasts to Cause Microcephaly.";
RL Dev. Cell 51:713-729.e6(2019).
CC -!- FUNCTION: Essential for the development of polarized epithelia, for
CC cell polarity associated with asymmetric cell division of neuroblasts
CC during development, and for oocyte polarity formation. Promotes the
CC formation of actin-rich projections at the oocyte cortex and the
CC posterior enrichment of par-1 which is required for oocyte
CC polarization. Regulates the localization of axis-specifying morphogens
CC such as stau and grk.
CC -!- FUNCTION: [Isoform p78]: Has an essential role in control of cell
CC proliferation and differentiation during development and could act as a
CC tumor suppressor.
CC -!- FUNCTION: [Isoform p127]: Has an accessory function in control of cell
CC proliferation and differentiation during development.
CC -!- SUBUNIT: May form multimeric complexes. Interacts with mahj. Interacts
CC with aPKC; leading to phosphorylation (PubMed:18094021,
CC PubMed:20644714). Interacts with ball (PubMed:31735666).
CC {ECO:0000269|PubMed:18094021, ECO:0000269|PubMed:20644714,
CC ECO:0000269|PubMed:31735666}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:12545176, ECO:0000269|PubMed:26481050}. Cytoplasm
CC {ECO:0000269|PubMed:26481050}. Note=In larval and embryonic
CC neuroblasts, detected in the cortex with apical enrichment from late
CC interphase to metaphase, and uniform cortical localization during
CC anaphase and telophase. {ECO:0000269|PubMed:12545176}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=p127; Synonyms=A, C;
CC IsoId=P08111-1; Sequence=Displayed;
CC Name=p78; Synonyms=EC371;
CC IsoId=P08111-2; Sequence=VSP_004299, VSP_004300;
CC Name=B;
CC IsoId=P08111-3; Sequence=VSP_021794;
CC Name=D; Synonyms=E, F;
CC IsoId=P08111-4; Sequence=VSP_021793;
CC -!- TISSUE SPECIFICITY: Expressed in the epithelial cells of the digestive
CC tract and in gonads.
CC -!- DEVELOPMENTAL STAGE: Expressed abundantly in early embryogenesis.
CC Moderate expression is found in larval and adult stages.
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC necessary and sufficient for interaction with phospholipids permitting
CC cortical localization (PubMed:26481050). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (PubMed:26481050). {ECO:0000269|PubMed:26481050}.
CC -!- PTM: Phosphorylated by aPKC which lowers lipid affinity and promotes
CC dissociation from the cell cortex (PubMed:26481050). In developing
CC oocytes, aPKC-mediated phosphorylation restricts activity to the oocyte
CC posterior and is required for oocyte polarity formation
CC (PubMed:18094021, PubMed:18327897). {ECO:0000269|PubMed:18094021,
CC ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:26481050}.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
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DR EMBL; X05426; CAA29007.1; -; mRNA.
DR EMBL; M17022; AAA28671.1; -; Genomic_DNA.
DR EMBL; M17022; AAA28672.1; -; Genomic_DNA.
DR EMBL; AE014134; AAG22255.1; -; Genomic_DNA.
DR EMBL; AE014134; AAG22256.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10501.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10502.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10503.1; -; Genomic_DNA.
DR EMBL; AY051654; AAK93078.1; -; mRNA.
DR EMBL; BT100129; ACX85650.1; -; mRNA.
DR EMBL; BT100228; ACY56896.1; -; mRNA.
DR PIR; A27069; A27069.
DR PIR; A27868; A27868.
DR RefSeq; NP_001245801.1; NM_001258872.2. [P08111-1]
DR RefSeq; NP_001245802.1; NM_001258873.2. [P08111-1]
DR RefSeq; NP_001245803.1; NM_001258874.2. [P08111-1]
DR RefSeq; NP_001245804.1; NM_001258875.2. [P08111-1]
DR RefSeq; NP_523439.2; NM_078715.4. [P08111-1]
DR RefSeq; NP_722583.1; NM_164348.3. [P08111-3]
DR RefSeq; NP_722584.1; NM_164349.3. [P08111-1]
DR RefSeq; NP_722585.1; NM_164350.3. [P08111-4]
DR RefSeq; NP_722586.1; NM_164351.3. [P08111-4]
DR RefSeq; NP_722587.1; NM_164352.3. [P08111-4]
DR AlphaFoldDB; P08111; -.
DR SMR; P08111; -.
DR BioGRID; 59421; 40.
DR DIP; DIP-22687N; -.
DR IntAct; P08111; 6.
DR STRING; 7227.FBpp0297544; -.
DR iPTMnet; P08111; -.
DR PaxDb; P08111; -.
DR PRIDE; P08111; -.
DR DNASU; 33156; -.
DR EnsemblMetazoa; FBtr0078166; FBpp0077824; FBgn0002121. [P08111-3]
DR EnsemblMetazoa; FBtr0078167; FBpp0077825; FBgn0002121. [P08111-4]
DR EnsemblMetazoa; FBtr0078168; FBpp0077826; FBgn0002121. [P08111-4]
DR EnsemblMetazoa; FBtr0078169; FBpp0077827; FBgn0002121. [P08111-4]
DR EnsemblMetazoa; FBtr0078170; FBpp0077828; FBgn0002121. [P08111-1]
DR EnsemblMetazoa; FBtr0078171; FBpp0077829; FBgn0002121. [P08111-1]
DR EnsemblMetazoa; FBtr0306589; FBpp0297544; FBgn0002121. [P08111-1]
DR EnsemblMetazoa; FBtr0306590; FBpp0297545; FBgn0002121. [P08111-1]
DR EnsemblMetazoa; FBtr0306591; FBpp0297546; FBgn0002121. [P08111-1]
DR EnsemblMetazoa; FBtr0306592; FBpp0297547; FBgn0002121. [P08111-1]
DR GeneID; 33156; -.
DR KEGG; dme:Dmel_CG2671; -.
DR UCSC; CG2671-RE; d. melanogaster.
DR FlyBase; FBgn0002121; l(2)gl.
DR VEuPathDB; VectorBase:FBgn0002121; -.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00950000182906; -.
DR InParanoid; P08111; -.
DR PhylomeDB; P08111; -.
DR SignaLink; P08111; -.
DR BioGRID-ORCS; 33156; 0 hits in 3 CRISPR screens.
DR ChiTaRS; l(2)gl; fly.
DR GenomeRNAi; 33156; -.
DR PRO; PR:P08111; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002121; Expressed in wing disc and 27 other tissues.
DR ExpressionAtlas; P08111; baseline and differential.
DR Genevisible; P08111; DM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0031012; C:extracellular matrix; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IDA:FlyBase.
DR GO; GO:0031256; C:leading edge membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0042734; C:presynaptic membrane; IDA:FlyBase.
DR GO; GO:0005920; C:smooth septate junction; IDA:FlyBase.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; IGI:FlyBase.
DR GO; GO:0045159; F:myosin II binding; IGI:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IPI:FlyBase.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IGI:FlyBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
DR GO; GO:0045175; P:basal protein localization; IMP:FlyBase.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0035072; P:ecdysone-mediated induction of salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:FlyBase.
DR GO; GO:0090163; P:establishment of epithelial cell planar polarity; IMP:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
DR GO; GO:0045184; P:establishment of protein localization; IMP:FlyBase.
DR GO; GO:0051294; P:establishment of spindle orientation; IBA:GO_Central.
DR GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; IGI:FlyBase.
DR GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IGI:FlyBase.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0051668; P:localization within membrane; IMP:FlyBase.
DR GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase.
DR GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:FlyBase.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0072697; P:protein localization to cell cortex; IMP:FlyBase.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:1904580; P:regulation of intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; TAS:FlyBase.
DR GO; GO:0098725; P:symmetric cell division; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR000664; Lethal2_giant.
DR InterPro; IPR013905; Lgl_C_dom.
DR InterPro; IPR013577; LLGL2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08596; Lgl_C; 1.
DR Pfam; PF08366; LLGL; 1.
DR PRINTS; PR00962; LETHAL2GIANT.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cytoplasm; Developmental protein;
KW Exocytosis; Phosphoprotein; Reference proteome; Repeat; Tumor suppressor;
KW WD repeat.
FT CHAIN 1..1161
FT /note="Lethal(2) giant larvae protein"
FT /id="PRO_0000084345"
FT REPEAT 39..72
FT /note="WD 1"
FT REPEAT 82..128
FT /note="WD 2"
FT REPEAT 131..167
FT /note="WD 3"
FT REPEAT 189..223
FT /note="WD 4"
FT REPEAT 231..263
FT /note="WD 5"
FT REPEAT 278..320
FT /note="WD 6"
FT REPEAT 328..358
FT /note="WD 7"
FT REPEAT 380..464
FT /note="WD 8"
FT REPEAT 513..594
FT /note="WD 9"
FT REPEAT 603..664
FT /note="WD 10"
FT REPEAT 708..778
FT /note="WD 11"
FT REPEAT 787..832
FT /note="WD 12"
FT REPEAT 837..927
FT /note="WD 13"
FT REPEAT 941..964
FT /note="WD 14"
FT REGION 15..86
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000269|PubMed:26481050"
FT REGION 1141..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_021793"
FT VAR_SEQ 17..28
FT /note="HRLQKDLFAYRK -> QRYI (in isoform B)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_021794"
FT VAR_SEQ 708
FT /note="V -> F (in isoform p78)"
FT /evidence="ECO:0000305"
FT /id="VSP_004299"
FT VAR_SEQ 709..1161
FT /note="Missing (in isoform p78)"
FT /evidence="ECO:0000305"
FT /id="VSP_004300"
FT MUTAGEN 647..681
FT /note="Missing: Reduced cortical localization and increased
FT cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 653..654
FT /note="RR->DD: Reduced cortical localization and increased
FT cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 656
FT /note="S->A: In 3A; loss of phosphorylation. In the
FT presence of aPKC remains localized to the cell cortex and
FT does not display any decrease in phospholipid binding; when
FT associated with A-660 and A-664."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 656
FT /note="S->D: In 3D; phosphomimetic mutant that displays a
FT slight decrease in phospholipid binding and reduced
FT cortical localization; when associated with D-660 and D-
FT 664."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 658..659
FT /note="KK->DD: In 4k/R-D; phosphomimetic mutant that
FT displays decreased phospholipid binding and reduced
FT cortical localization; when associated with D-666 and D-
FT 667."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 660
FT /note="S->A: In 3A; loss of phosphorylation. In the
FT presence of aPKC remains localized to the cell cortex and
FT does not display any decrease in phospholipid binding; when
FT associated with A-656 and A-664."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 660
FT /note="S->D: In 3D; phosphomimetic mutant that displays a
FT slight decrease in phospholipid binding and reduced
FT cortical localization; when associated with D-656 and D-
FT 664."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 664
FT /note="S->A: In 3A; loss of phosphorylation. In the
FT presence of aPKC remains localized to the cell cortex and
FT does not display any decrease in phospholipid binding; when
FT associated with A-656 and A-660."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 664
FT /note="S->D: In 3D; phosphomimetic mutant that displays a
FT slight decrease in phospholipid binding and reduced
FT cortical localization; when associated with D-656 and D-
FT 660."
FT /evidence="ECO:0000269|PubMed:26481050"
FT MUTAGEN 666..667
FT /note="RK->DD: In 4k/R-D; phosphomimetic mutant that
FT displays decreased phospholipid binding and reduced
FT cortical localization; when associated with 658-D--D-659."
FT /evidence="ECO:0000269|PubMed:26481050"
FT CONFLICT 2
FT /note="L -> F (in Ref. 3; AAA28671/AAA28672)"
FT /evidence="ECO:0000305"
FT CONFLICT 37..38
FT /note="KP -> A (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="A -> V (in Ref. 7; ACY56896)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="G -> S (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="G -> R (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..245
FT /note="FTW -> RYL (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="Y -> N (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="F -> I (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="N -> S (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="I -> T (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="V -> L (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..515
FT /note="VKKI -> SEEN (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 667..675
FT /note="KLRKGRSTR -> SFARVDQTK (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="T -> S (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
FT CONFLICT 857
FT /note="I -> V (in Ref. 7; ACY56896)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="R -> G (in Ref. 3; AAA28671)"
FT /evidence="ECO:0000305"
FT CONFLICT 1095
FT /note="A -> G (in Ref. 1; CAA29007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1161 AA; 126892 MW; 979F73A01DA62A1A CRC64;
MLKFIRGKGQ QPSADRHRLQ KDLFAYRKTA QHGFPHKPSA LAYDPVLKLM AIGTQTGALK
VFGQPGVELY GQHTLLNNSA SELNVQLLEW VYGTGRILSL TAANQLILWE PVGATLLPIK
TLPFDGKLKK VSSLCCSLSK DLLWIGTEGG NIYQLDLHTF TIKEPVIYHD VVLEQVPPAY
KLNPGAIESI RQLPNSPSKL LVAYNRGLCV LWDFESASVQ RAYIAPGHGQ SVGLTVNFEG
SEFTWYHADG SYATWSIDNP EPPSNVNYVP YGPDPCKSIN RLYKGKRRSN DVIVFSGGMP
RSAYGDHNCV SVHASDGHKV CLDFTSKVID FFVTFENNRD VAEVLVVLLE EELCAYDLTD
PNICAIKAPY LHSVHASAVT CNYLASEVVQ SVYESILRAG DEQDIDYSNI SWPITGGTLP
DNLEESVEED ATKLYEILLT GHEDGSVKFW DCTGVLLKPI YNFKTSSIFG SESDFRDDAA
ADMSAEQVDE GEPPFRKSGL FDPYSDDPRL AVKKIAFCPK TGQLIVGGTA GQIVIADFID
LPEKVSLKYI SMNLVSDRDG FVWKGHDQLN VRSNLLDGEA IPTTERGVNI SGVLQVLPPA
SITCMALEAS WGLVSGGTAH GLVLFDFKNF VPVFHRCTLN PNDLTGAGEQ LSRRKSFKKS
LRESFRKLRK GRSTRTNQSN QVPTTLEARP VERQIEARCA DDGLGSMVRC LLFAKTYVTN
VNITSPTLWS ATNASTVSVF LLHLPPAQTA ATAVPSASGN APPHMPRRIS AQLAKEIQLK
HRAPVVGISI FDQAGSPVDQ LNAGENGSPP HRVLIASEEQ FKVFSLPQLK PINKYKLTAN
EGARIRRIHF GSFSCRISPE TLQSMHGCSP TKSTRSHGDG EADPNISGSL AVSRGDVYNE
TALICLTNMG DIMVLSVPEL KRQLNAAAVR REDINGVSSL CFTNSGEALY MMSSSELQRI
ALATSRVVQP TGVVPVEPLE NEESVLEEND AENNKETYAC DEVVNTYEIK NPSGISICTR
PAEENVGRNS VQQVNGVNIS NSPNQANETI SSSIGDITVD SVRDHLNMTT TTLCSINTEE
TIGRLSVLST QTNKASTTVN MSEIPNINIS NLEDLESKRN TTETSTSSVV IKSIITNISH
EKTNGDNKIG TPKTAPEESQ F
