AFFL_DROWI
ID AFFL_DROWI Reviewed; 1837 AA.
AC B4MUE1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=GK14864;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW76067.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW76067.1};
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; CH963857; EDW76067.1; -; Genomic_DNA.
DR RefSeq; XP_002065081.2; XM_002065045.2.
DR AlphaFoldDB; B4MUE1; -.
DR SMR; B4MUE1; -.
DR STRING; 7260.FBpp0244007; -.
DR eggNOG; ENOG502QR32; Eukaryota.
DR HOGENOM; CLU_241798_0_0_1; -.
DR InParanoid; B4MUE1; -.
DR OMA; HESHNIV; -.
DR PhylomeDB; B4MUE1; -.
DR ChiTaRS; lilli; fly.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0007366; P:periodic partitioning by pair rule gene; ISS:UniProtKB.
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 InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1837
FT /note="AF4/FMR2 family member lilli"
FT /id="PRO_0000394679"
FT DNA_BIND 952..964
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 1517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
SQ SEQUENCE 1837 AA; 196644 MW; C5D9173836853AA0 CRC64;
MAQQQQQQQH HHHLQHQQQQ QQQQQLQHHS NLLLLQQQQQ QQQQQQQQQQ QLLQQEQQLQ
QYDNNLYSQN YNMEEYERRR RREREKYERQ QGIQSDDRET SLFSEPRRLT EGDAEITAAL
GEFGDARNYI NQYTVGISRH APGGGSGNGS IGNNPRLQAP MIQQQVSSSI SSSASVASSL
LPPGLGQTQQ QQQQQQQQQQ PRPPTYLKQA DNKPPYNGRG GYPGQPMKND IPSSSGMAPP
RGPPKLNSNS SSITNNAAAS SSSSLLGPPI STQVPNGREK SFLGPPTTGT ALHNGGGRFA
QPVSNKRPGV GIQPPPPQEK DVRSMLSEMK NHFQVTPLNP IAATPQAPTR ENYNLNAPNK
FKYAFDIVDP IMPLLNSPPS VTPSSLITPI APMTSPIAPL LTTPPQASQL PLGSGSGNGA
AISATSLSTT TAAAAAAAAV AGVAATVAAT VAPIQQLPPT PPKAMSVTPP TAKPLKIEKN
PILEKQDSCL ENDLELSESE DERKKDGRSP GSSSNGSESD STESGSESSS KGEHNHHHHH
QQQQQQTQQQ QLHGHHPQSH HHQQFLQQQL QRQQQQQQQQ QQLTANGGKK KYSQTIIASG
ANTITGLLTS SGGLGSSSGN NSSGGGGGSG NGGTTSSSSG GSMGGSGGSS SSGGASGGGG
GGGGSGSSSG IGSGSSSNKT PSPTDSNKWN LSRFFHKPTS QTSSESVSPG NVSMKVPGIL
PGGAQIIPES IDVTTAIVKN EKIHHDDHLM DIDECDEDDD DVDEQHQQLR YGAGLSVTPV
AVKKEEDLGL LTAAAIPKSQ IKRESETQIS HQRLSESATS GSSSSSCSSS DSAASASEVV
PMPGPGETLQ IPGVPAAITS VMRVPPINNM QKSQSMSVTV TPIAPLPASP KPRQKKPRKK
KMMSVLTPPL LDSSDEDEPS TKHSSLVVAQ AQAAVVPPPS TNSTTTSATT TKKGRGRPRK
QQQQQSAGSG NLSSASAGSS SQAKGPTLTA AKKTLVKASA SSSTSNTNSS SVLPRKREHS
SQSSSNGNTP TKKMSSIPMM PAAAASAAAT LLQPPAVAAA NAVAASSSSS DEESSSSSCS
TSKSSSSSSS SDDTETQKTN CRIVKLNKTV PVTAAMAPLA KRSSYHRRSG SSSPTSSSSE
TDKPNSNSHN NLGIAAISNS NSNSNNNVIV NNNLQQQAMP QQSPYKVPLS GGSQQLSSSD
SSSSSSGSSS SSGDEDDAKR EKNRERKPKS DKNKISTLTR IFNNKEGGAK KQGQVVIIDQ
SEEQLQQQQQ QQQQVQIRDP LPPPSLLSQS GGVKQRMTPT QQQQLGAGLA SPARTTTPLL
TSLICKIDLS KLSRERILRL KKLAPSSSNQ QNGHLTPNGH VVQGGSSPAG LSKVKHEHHQ
LHHHSQQAHS HPVKPEPELD SLYETKFRPT NVKQEFQLKQ ERDRDRNRER DQQQQPPPRR
RKRSSSSSSS PYKEKKRKKE KTDPMLTNAK DQMLQINPML LPSNNHERLS YDKYQLLQED
AAAAAAAAAA VAVVNSSNGQ KLFQSSIGGG TGATAVGPLS IMAPSTCSEA VQTTPPTSVT
GAGAPASLVS QPPPPPRLIY RSYFDREEEH PSDDLRKSKQ FLQEAVQRKH AADSERDSFN
QVTLYLEAVA YFLLTADAME RCSSETATWT MYKDTLSLIK FISSKFRPYQ QSANCQQETH
NKVAILSLRC QSLISLKLFK LRRVNCRAII NSLTDFFRNG RGDIVNGNTP SSISPSNSVG
SQGSGSNTPP GKIVPQDIHN QLCKQNEYLT YVNSAHELWD QADRLVRTGN HLDFFRELDH
ENGPLTLHST MHEVFRYVQA GLKTLRDAVS HPTHQSQ
