AFFL_DROGR
ID AFFL_DROGR Reviewed; 1883 AA.
AC B4JQ42;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-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=GH13637;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV99022.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV99022.1};
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; CH916372; EDV99022.1; -; Genomic_DNA.
DR RefSeq; XP_001993097.1; XM_001993061.1.
DR AlphaFoldDB; B4JQ42; -.
DR SMR; B4JQ42; -.
DR STRING; 7222.FBpp0147543; -.
DR PRIDE; B4JQ42; -.
DR eggNOG; ENOG502QR32; Eukaryota.
DR HOGENOM; CLU_241798_0_0_1; -.
DR InParanoid; B4JQ42; -.
DR OMA; HESHNIV; -.
DR PhylomeDB; B4JQ42; -.
DR ChiTaRS; lilli; fly.
DR Proteomes; UP000001070; 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..1883
FT /note="AF4/FMR2 family member lilli"
FT /id="PRO_0000394674"
FT DNA_BIND 930..942
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1783..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 1546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT MOD_RES 1548
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9VQI9"
SQ SEQUENCE 1883 AA; 202795 MW; 3E1CABEFD85FD9ED CRC64;
MAQQQQQQHL QQQQQQHHQQ QQLQQLQQQQ QLPQYNNNLY NLNYNMEDPE RRKRREREKY
ERQQGIQSDD RETSLFEAPR RLNPSEGDNM ITAALGEFVD AKEHMCMNMV GIHRQAPGGG
SNARLQGQAT TPIINSLSSI NSTTTTSSSA SLLPGQLPTS QQQQQQQQQQ QQHYQQQQRA
PTYLKQADNK PPYNGRGGYP GQPMKNDIPS SSGMAPPRGP PRSASSSSSA SNNNSSSATN
NATAAAATSA STAPLLGPPM STQMPNGREK SYLGPPAPAL SNGGRFVPPA ASGKRTSNTA
GLQPPPPEKD ISKIINEMTN SYRVTPLTSI AATPHAPTRE NYNLNGPNKN KYAFDDVEPI
GPLNSPPAAS GASSSSLSCT TNSSSSLLMT PLLAPIAPIT SPIAPLLTTP PQASQLPLPL
PLLPPLAGAT TVLPPALGMA AVAPIQQLMP TPPKASPTPP TAIRPLKSEK NHSLEKQDSC
LENDLELSES DDDRKRDICS AGNSSNSSET DSSESGSEAS SKGEAQQQQQ QQQQLLHHQH
QQQLLLQQQQ QQQQQQRATA TTANGGNKKK CQTIIASGAN TISGLLTSSG LGGSGGAVNA
TSNTNSGLLG GGGGSGSTGG GGGSSSSGMG NMSSSSSSNK TPSPTDSNRW HLSRFFPKPT
NQATAESVSP GNVACGNVSM KVPGILPGGA QIIPESIDVT TAIVKNEKLH DDTRRITDDE
DEDEQQQQRY AAGLSVTVKK EQQEQQQQQQ QQQQQQQQQQ QQQQQQQQLS AEQLALAGAL
PNNQIKREVR LSDSASISSG SASGSSSSDS AAGEVVPLPG PGETLQIPGV PAAITTVLRV
PPAMQQKVPP NSVTLTPIGP LPASPKPRQK KPRKKKMSAA TAPPLDSSDE DEPASSNKKH
ALELAATTAA AAAAIAAAPA ATAAALPAVK KGRGRPRKQQ QQLQQTQSGN LSSASAGSLA
KGPTLTAAKK PLAKSTAAAA AAAALAATAL TVAGSRKREH SSNSSSNGNT PTKKLHAAPA
TVAAAAAAAA AATTLLPPTA AAGSSSDEDS TSSSCSSTKS SNSSSSGSDS EATATTAAAA
TTAAAAAAAT TTTTQNPAKK RIVKINKLGV VSSSKNNRLY GAGSSSNSSS SETEEQQQQQ
QQHKQQQQLL LMQQQQQQQQ QQQQKQQLQQ HQQQQPLQPQ QQQQQQSHFT PDAKQARQRS
SSSDGSSSSS TDSSSTNSSS SSDEVDVHHG GGKRKSDKKK ICTLTRIFNP KEGGAKKQGQ
VVIIDQSEEQ LQQQQQQLQQ QQQQQQQHQQ QQQQQQQQEQ QQSKEWKPRA TPTQLLGATL
ASPARTTTPH LTSLMCKIDL SKLARVPPEW YQKSYRQYAA EQQQQQQQHL HTQQLHHPPH
HQHQHYQQQH QPHQQKAQQN GHLSSRSAEG ARTPKELQQA YGMPNGYVTS GGAAGAAGAA
SKLLGGVKHE HGVKPEPELD AGYEAKYKPN SVKQEFMPKQ EMPTRRRKRS SSSSPYKEKK
RKKEKADQVS KELLPVPVLL PANNHERLSR DKLELLQQEI SSANGSPTKR SFPLAHAQQQ
QHQQQQQQQQ HQPQHQQQLK ATTTTSTTAT VAAVQTSTTA TQQPTTCSEA VQTTPPPVAP
PPPPRLIYRS HFDNEEEPPS DDLRKNEILL QEAIRRKRAA DSERDSFKQM TLYLEAIVYF
LLTADAMERS NMEATWTMYK DTLTLIKFIS SKNRPYQQST NGKHESHNIV AILSLRCQSL
ISLKLYKLRR ANCRAIIASC SEFFRTGGRG DILNGNTLSS ISPSNSVGSQ GSGSNTPPGR
IVPQDIHNQL CRQNEYLTYV NSAHDLWDQA DRLVRTGNHI DFIRKLDHEN GPMTLHSTMH
EVFRYVQAGL KTLRDSVSYP QSQ
