ID   AFFL_DROAN              Reviewed;        1587 AA.
AC   B3MLB7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=AF4/FMR2 family member lilli {ECO:0000250|UniProtKB:Q9VQI9};
DE   AltName: Full=Protein lilliputian {ECO:0000250|UniProtKB:Q9VQI9};
GN   Name=lilli {ECO:0000250|UniProtKB:Q9VQI9}; ORFNames=GF14991;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1] {ECO:0000312|EMBL:EDV30706.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV30706.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Has a role in transcriptional regulation. Acts in parallel
CC       with the Ras/MAPK and the PI3K/PKB pathways in the control of cell
CC       identity and cellular growth. Essential for regulation of the
CC       cytoskeleton and cell growth but not for cell proliferation or growth
CC       rate. Required specifically for the microtubule-based basal transport
CC       of lipid droplets. Plays a partially redundant function downstream of
CC       Raf in cell fate specification in the developing eye. Pair-rule protein
CC       that regulates embryonic cellularization, gastrulation and segmentation
CC       (By similarity). {ECO:0000250|UniProtKB:Q9VQI9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9VQI9}.
CC   -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000255}.
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DR   EMBL; CH902620; EDV30706.1; -; Genomic_DNA.
DR   RefSeq; XP_001961485.1; XM_001961449.2.
DR   AlphaFoldDB; B3MLB7; -.
DR   SMR; B3MLB7; -.
DR   STRING; 7217.FBpp0118183; -.
DR   EnsemblMetazoa; FBtr0119691; FBpp0118183; FBgn0092016.
DR   eggNOG; ENOG502QR32; Eukaryota.
DR   HOGENOM; CLU_241798_0_0_1; -.
DR   InParanoid; B3MLB7; -.
DR   OMA; HESHNIV; -.
DR   OrthoDB; 105133at2759; -.
DR   PhylomeDB; B3MLB7; -.
DR   ChiTaRS; lilli; fly.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0000791; C:euchromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032783; C:super elongation complex; IEA:EnsemblMetazoa.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblMetazoa.
DR   GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR   GO; GO:0007611; P:learning or memory; IEA:EnsemblMetazoa.
DR   GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:EnsemblMetazoa.
DR   GO; GO:0007366; P:periodic partitioning by pair rule gene; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0032368; P:regulation of lipid transport; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IEA:EnsemblMetazoa.
DR   InterPro; IPR007797; AF4/FMR2.
DR   InterPro; IPR043640; AF4/FMR2_CHD.
DR   PANTHER; PTHR10528; PTHR10528; 1.
DR   Pfam; PF18876; AF-4_C; 1.
PE   3: Inferred from homology;
KW   Developmental protein; DNA-binding; Nucleus; Pair-rule protein;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1587
FT                   /note="AF4/FMR2 family member lilli"
FT                   /id="PRO_0000394672"
FT   DNA_BIND        754..766
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1130..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1477..1506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..577
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..842
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1135..1213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1477..1499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         311
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         724
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         777
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         1261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
SQ   SEQUENCE   1587 AA;  170486 MW;  AC558719F2C0302A CRC64;
     MAQQQQQQHN HQTSNNNNNN SSILLLQQQQ LHQEQLQQYN NNLYSQNYNM EEYERRKRRE
     REKIERQQGI QIDDRETSLF GEPRRLTEAD ADITAALGEF GDARVYINQS TVGISRHTPG
     AGNPRLQAPL QPPPKSLGHS PSYTGSTGSA SASANSAVPS QQQQQQHYNG TGGRFLPPAA
     SKRSSSGAGQ QPLPQEKDIS KMISEMADNF RVTPLTSIAA TPHAPVRENY NLNGPNKNKY
     MDDIISSPLS QPSSLMTPLF APIAPIASPP QTSQLPLGGA TSLTGSSEAV LGLAPLQQLP
     PTPPKAASAI TSPAAAKPLK TEKNHTLEKQ DSCLENDLEL SESEDEQPKK EGRSAGNSSN
     SSESDSSESG SESSSKNDAQ PLPNHKLHHQ QQQQLQQQPL QQQQHQQQQQ QQILLQQQQQ
     QRPQQLTANG KSEKKKYKHA IIAGGSNTIT GLLTSSGFGS GGNGGPGGNS CGPGSGASAS
     AGTMSSGGSS SNKTPSPTES NKWTLSRFFP KPANQTNTES ATPGNVSMKV PGILPGGAQI
     IPEPIEVSTA IVKNEKIHDD PMDMDDGEED DDDEDQQQQQ QQQLHYRADL SVTPVSVKKE
     AIDGVSELGL AAIPKNQIKR ESSEALHASR LSDSGTSGSS SSSSSSSESA PGGEVVPMPG
     PGETLQIPGG AAITSVMRVP PTLTQKAPSS TSVTLMPILP LPMSPKQRQK KQRKKKTSTP
     IVNSSDEDEP APKHPGLDYT AVSAHSQSTA TAPAKKRGRP RKQQQQSGGS GNLSSASAGS
     SSQTKGPTLT AAKKPLCKAL PAMGGARKRD HSSQSSSNGN TPTKKMATPM SVSAPPKTAS
     VHRDSSSSDD DSSSSGGSSS KSSSSSSSSD DTEEAQNTNC RIVKLNKTGA GAVAAKVLLG
     SGSSSALSSG SEAEDQARSQ AGSGKALAQQ MPPYKPQVMS QHSQQLSSSE CSSSSGDRGG
     TGAGSSSSGE EDEARHEKER ERKPKSDKNK ISTLTRIFNP KEGGAKKQGQ VVIMDLQEEQ
     QQGKLDAATQ SSQIPATAPA VKPRMTPTQQ LQQQHAQSQQ MLGTSLASPA RTTTPHLTSL
     ICKIDLSKLS RERIMRLKKL TPAQQNGHLT PKGQAASAVQ MPNGYANDAV PAAKVKPEHP
     VKPEPDADYE AKFKPGSVKQ EFQLKQERDR DRERERERDR EQPPGRRRKR SSSSSSSPYK
     EKKRKKEKTD QLQICKELLP SNNHERIPNH DRLSYDKLQL LHEDAAAAAA ASGVGAAPNG
     SPRKNLLAMS PLPPPPISTA IAIVPPITCN EAVQTTPPLT TSTSPQAASA VTEPAPPAVA
     VPPAPVTRLI YRSYFDREEA HPSADLRRNN QFLQEAVNRK HAADAEPDSF NQVTLYLEAV
     VYFLLTADAM ERCSSEATYT MYKDTLSLIK FISFKFRPQH SANGQTKTHM AKVAILSLRC
     QSLISLKLYN LRRANCRDII ASLTDFFRTG RGDIVNGNTP SSISPSNSVG SQGSGSNTPP
     GRIVPRDIHN QLSKQNEYLS YVHSAHELWD QADHSVRKGN HTDFFRELDH ENGPLTLHST
     MHEVFRYVQA GLKTLRDAVS HTAHPTQ