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AFFL_DROVI
ID   AFFL_DROVI              Reviewed;        1823 AA.
AC   B4LV24;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   25-MAY-2022, entry version 60.
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=GJ13972;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1] {ECO:0000312|EMBL:EDW63273.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW63273.1};
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW63273.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH940649; EDW63273.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002051118.2; XM_002051082.2.
DR   AlphaFoldDB; B4LV24; -.
DR   SMR; B4LV24; -.
DR   STRING; 7244.FBpp0228389; -.
DR   PRIDE; B4LV24; -.
DR   eggNOG; ENOG502QR32; Eukaryota.
DR   InParanoid; B4LV24; -.
DR   ChiTaRS; lilli; fly.
DR   Proteomes; UP000008792; 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; 2.
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..1823
FT                   /note="AF4/FMR2 family member lilli"
FT                   /id="PRO_0000394678"
FT   DNA_BIND        908..920
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000255"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..1057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1322..1350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1413..1448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1480..1531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1547..1567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..701
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1244..1286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1416..1448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         434
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         463
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         859
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         860
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         939
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         941
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         1486
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
SQ   SEQUENCE   1823 AA;  195478 MW;  30F75FD89415C6F2 CRC64;
     MAQQQQQQHQ QQQHHQQQQQ QLQQQQQLLQ YNNNSYNLNY NMEDPERRKR REREKYERQQ
     GIQSDDRETS LFGEPRRLNP NEGDPEITAA LGDFVDARDY MNASTVGIYR QAPGASNARL
     QALPKGFGSA TTSFSSSSSA SASSSASVPG QLPTSQQQQQ QQQQQQQQHY QQQQRAPTYL
     KQADNKPPYN GRGGYPGQPM KNDIPSSSGM APPRGPPRSS SSSSSSNNNS SSVSNNATAA
     PTSASTSSPL GPPMSTQMPN GREKSFLGPP APALPNGGRF VPPSASGKRP SSTAGLQPPP
     PENHINKIIT EMTNNYRVTP LTSIAATPHA PMRENYNLNG PNKFKYAFDA VDPIGPLNSP
     PAAGASSLMT PLLAPIAPIT SPIAPLLTTP PQASQLPLPL PPMAGATTVP PSMAMGAVAP
     MQQLTPTPPK ASPTPPVIKP LKTEKNHSLE KQDSCLENDL ELSESDDERK KDSRSAGNSS
     NSSESDSSES GSEASSKGDP QQQQQQQQQH LLHQQQQHQQ QQLLLQQQQQ QRLAATANGS
     KKKYSQTIIA SGANTISGLL TSSGLGGTGA GPGGAVNSTG SAAGGVGSGS GSTGGGSSSS
     GMGTMSSSNS SNKTPSPTDS NRWHLSRFFP KPANQTAAES VSPGVANAMG NVSMKVPGIL
     PGGAQIIPES IDVTTAIVKN EKLHDDSRHM DDDEDEQADQ QHQQQQQRYG VGLSVTVKKE
     QLEQQQQQQQ QQQLLLQQQQ LTAEQLALAG ALPKNQIKRE SRLSDSGSGS SGSGSSSSDS
     AGGSSEVLPM PGPGETLQIP GVPAAITTVM RVPPATQHKA QPNSVTLTPI GPLPASPKPR
     QKKPRKKKMS AATAPPLDSS DEDEPANSNK KHALELAATA AAAAANAAAA SVMPVAAAAA
     AAAAPAIKKG RGRPRKQAQQ QQQQLQLQQQ QQQSGNLSSA SASSSQAKGP TLTAAKKPLA
     KGTASSSSSS GTAATVAAGS RKREHSSNSS SNGNTPTKKP NAAMAAAAAA AAAAAAAAIA
     VRAASSSDED SSSSSCSSTK SSNSNSSSSG SDTDIPTAAP AVTTAAAVAA AAAQNPAKKR
     IVKINKVGVA SSKAKRRFSL GNSSNSSSSE TEEQQQQFLQ QQQQQQQQKQ QLQQQQQQQP
     QQQQLQQHHQ LQQQQQQQLL QGHFAPELPL QTLKQSAQQR LSSSDCSSSA SSDSSSNSSA
     SSSSDEDDAH RSGKRKSDKK KICTLTRIFN PKEGGAKKQG QVVIIDQSEE QLQQQQQQQQ
     QQQQQQQQQQ QQQQQQQQQQ AKELKPRATP TQLLGATLAS PARTTTPHLT SLMCKIDLSK
     LARQHHHQPE RLKTQQNGHL SSRSAEGART PKELQQIYAP NGYVGGALGG AAGAAAGNKL
     LGGVKHEHGV KPEPELDAGY EAKYKPNSVK QEFMLKQELP ARRRKRSSSS SSSPYKEKKR
     KKEKAEQLSK ELLPVPVLLP ANNHERLSRD KLELLLQQQE NSANASPNKL QQQNARQLPL
     SQSQLQHQHQ HQHQLQQQQS QSTATGHAIA STTSATVATA STQLPTTCSE AVQTTPPPAA
     PPPAPRLIYR SHFDNEEEHA SDDHRKNDLL LQEAIRRKRA ADSERDSFNQ MTLYLEAIVY
     FLLTADAMER CNMEATWTMY KDTLSLIKYI SSKNRPYQQL TNGKHESHNI VAILSLRCQS
     LISLKLYKLR RANCRATIAS CSEFFRSGRG DILNGNTPSS ISPSNSVGSQ GSGSNTPPGK
     IVPQDIHNQL CKQNEYLTYV NSAHELWDQA DRLVRTGNHI DFIRKLDHEN GPLTLHSTMH
     EVFRYVQAGL KTLRDAVSYP QSQ
 
 
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