AFFL_DROER
ID AFFL_DROER Reviewed; 1679 AA.
AC B3NAM7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GG24899;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV57550.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV57550.1};
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; CH954177; EDV57550.1; -; Genomic_DNA.
DR RefSeq; XP_001968491.1; XM_001968455.2.
DR AlphaFoldDB; B3NAM7; -.
DR SMR; B3NAM7; -.
DR STRING; 7220.FBpp0143445; -.
DR EnsemblMetazoa; FBtr0144953; FBpp0143445; FBgn0117028.
DR GeneID; 6541908; -.
DR KEGG; der:6541908; -.
DR eggNOG; ENOG502QR32; Eukaryota.
DR HOGENOM; CLU_241798_0_0_1; -.
DR OMA; HESHNIV; -.
DR OrthoDB; 105133at2759; -.
DR PhylomeDB; B3NAM7; -.
DR ChiTaRS; lilli; fly.
DR Proteomes; UP000008711; 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.
DR PROSITE; PS00354; HMGI_Y; 1.
PE 3: Inferred from homology;
KW Developmental protein; DNA-binding; Nucleus; Pair-rule protein;
KW Phosphoprotein; Transcription; Transcription regulation.
FT CHAIN 1..1679
FT /note="AF4/FMR2 family member lilli"
FT /id="PRO_0000394673"
FT DNA_BIND 859..871
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 421
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 1370
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
SQ SEQUENCE 1679 AA; 180421 MW; 6DB64ED889C320DA CRC64;
MAQQQQQQLQ QQQQHHTSSI NNNNNSILLL QQQQPQQQQQ LDQLQQYNNN LYSQNYNMEE
YERRKRRERE KIERQQGIQI DDRETSLFGE PRRVTEGDAE ITAALGEFFE ARVYINNQTV
GISRSAPGAG NPRLQPNMPP QGKSLGHSPS SASASAAAGP TSASATTALP GQQQQHYQQQ
QRPPTYVKQA DNKPPYNGRG GYPGQPMKND IPSSSGMAPP RGPPRSSSSN SNSSSATNNA
SSGGVPASTP LGPPLSTQMP NGREKSFLGP PAPALHNGTG GRFVPPAASK RPGVGQQPPP
PEKDVNKIIS DIANIFTVQP LTLIAATPHA PTRENYNLLA PNKQKYAMDI PSSPPSAEPS
SLMTPLFAPI ASPIAPLVTT PPQASQLPLG GATSGTILAG EALAPLHQLP PTPPKAASGV
TSPGPGKPLK TEKNHSLEKQ DSCLENDLEL SESEDEQRKK EGRSAGNSSN SSESDSSESG
SESSSKNDPQ HHPNHQQHHH QLQQQQQQQQ QQASMQQQQV LQQQQQHRPQ PLTSNGAQNK
KFRHEIIARG SNTITGLLSS SGFGSGGSVG PAGLNSSAAM GAGSGSGGTL SSGGSSSNKT
PSPTESNKWN LSRFFHKPAN QTNSENVSPG NVSMKVPGIL PGGAQIIPES IDVTTAIVKN
EKIHDDHMAM EDGEEEDDDE EQQLRYGGGL SVTPVAVKKE AIDAVSEMAL GAIPKTQIKR
ESAEALLSAR LSDSGTSASG SSSSSSSSSD SAVGGEVVPK LGLGEILQLP GVPAAITTVM
RVQPTQSQKA PPSNSVTLTP ILPLPTSPKQ RQKKPRKKKA VTSAPILDSS DDDEPPPKHP
GLDHTAVSVQ TPPAADTVKK GRGRPRKQQQ SGGSGNLSSA SAGSSSQTKG PTLTAAKKPL
AKTPLAMSRA RKREHSSQSS SNGNTPTKKV ATPQLVAAPL KPTSVTAGSS SSDEDSSSSA
ESSSKSSSSS SSSDDTETQN TNCRIVKLNK TGAVQKKALL GSGSSSPSSS GSEPEDQTTR
SQVGSGQALA QQLPPYKQLP ISQHSQHLSS SECSSSSGGC TAVCSSSSGE EDEGRREKER
ERKPKSDKNK ISTLTRIFNP KEGGAKKQGQ VVIVDLQEEQ QQGKLDAAAQ PPPPQAPPAA
PAAIMAKPRM TPTQQQQLGA GLASPARTTT PHLTSLICKI DLSKLSRERI MRLKKLTPAQ
QNGHLTPKDQ ATNAVHVPNG YAGDTNPATK VKHEHPVKPE PELDAGYEAK FKPGNVKQEF
QLKQERDRDR ERERERERER DREREQPPGR RRKRSSSSSS SPYKEKKRKK EKADQLQIGK
ELLPVPVLLP SNNHERMPNH DRLSYDKLQL LHEDAAAVIG DVSAANGSPT KKMMVMSPLP
PPPTVTVAPA TCNEAVQTTP PSATTASATA PPVPATRLIY RSYFDRDVEH PSDDPRKNNQ
FLQEAISRKH AADLERDSFN QVTLYLEAVV YFLLTADAME RCSSEQATNT MYKDTLSLIK
FISTKFRPYQ QQSTTNIQHE THNKVAILSL RCQSLISLKL YKLRRKDCRA VINSLADFFR
VGRGDIANGN TPSSISPSNS VGSQGSGSNT PPGRIVPPDI HNMLCKENEF LSYLNSAHEL
WDQADRLVRT GNHIDFIREL DHENGPLTLH STMHEVFRYV QAGLKTLRDA VSHPTHQSQ
