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AFFL_DROYA
ID   AFFL_DROYA              Reviewed;        1671 AA.
AC   B4NXA8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-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=GE18192;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:EDW87465.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW87465.1};
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; CM000157; EDW87465.1; -; Genomic_DNA.
DR   RefSeq; XP_002087753.1; XM_002087717.2.
DR   AlphaFoldDB; B4NXA8; -.
DR   SMR; B4NXA8; -.
DR   STRING; 7245.FBpp0263202; -.
DR   EnsemblMetazoa; FBtr0264710; FBpp0263202; FBgn0235623.
DR   GeneID; 6526645; -.
DR   eggNOG; ENOG502QR32; Eukaryota.
DR   HOGENOM; CLU_241798_0_0_1; -.
DR   OMA; HESHNIV; -.
DR   PhylomeDB; B4NXA8; -.
DR   ChiTaRS; lilli; fly.
DR   Proteomes; UP000002282; Chromosome 2L.
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..1671
FT                   /note="AF4/FMR2 family member lilli"
FT                   /id="PRO_0000394680"
FT   DNA_BIND        849..861
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000255"
FT   REGION          53..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..1162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1185..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1562..1586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..796
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1059..1080
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         416
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         446
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         448
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         819
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         869
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         871
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         1360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
FT   MOD_RES         1362
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VQI9"
SQ   SEQUENCE   1671 AA;  179779 MW;  9A37490A342B69BD CRC64;
     MAQQQQQQLQ QQQQHHTSSI NNNNSILLLH QQQPQQQQQQ QLDQLQQYNN NLYSQNYNME
     EYERRKRRER EKIERQQGIQ IDDRETSLFG EPRRLTEGDA EITAALGEFF EARVYINNQT
     VGISRSAPGA GNPRLQPNLP PQAKSLGHSP SSASSAAGPT SASATTALPG QQQHYQQQQR
     PPTYVKQADN KPPYNGRGGY PGQPMKNDIP SSSGMAPPRG PPRSSSSNSN SSSATNNASS
     GGVPANTPLG PPLSTQMPNG REKSFLGPPA PALHNGTGGG RFVPPAASKR PGVGQQPPPP
     EKDVNKIISD IANIFSVQPL TSIAATPHAP TRENYNLLAP NKQKYAMDIP SSPPSAEPSS
     LMTPLFTPIA PLVTTPPQAS QLPLGAATSG TILAGEPLAP LHQLPPTPPK AASGVTSPGP
     TKPLKTEKNH SLEKQDSCLE NDLELSESED EQRKKEGRSA GNSSNSSESD SSESGSESSS
     KNDLQHHPNH QQHHHQLQQQ QQASMQQQQV LQQQQQHRPQ PLTSNGAQNK KFRHEIIARG
     SNTITGLLSS SGFGSGGSVG PAGVNSSAVM GAGSVSGGTL SSGGSSSNKT PSPTESNKWN
     LSRFFHKPAN QTNSESVSPG NVSMKVPGIL PGGAQIIPES IDVTTAIVKN EKIHDDHMAM
     EEGEEEDDDE EQQMRYGGGL SVTPVAVKKE AIDAVSEMAL GAIPKTQIKR ESAEALLSAR
     LSDSGTSASG SSSSSSSSSD SAVGGEVVPM PGPGETFQLP GVPADITTVV RVPPTQSQKA
     PPSNSVTLTP ILPLPTSPKQ RQKKPRKKKA VTSAPILDSS DDDEPPPKHP GLDHSAVSVQ
     AQPATDTVKK GRGRPRKQQQ SGGSGNLSSA SAGSSSQTKG PTLTAAKKPL AKTPLAMSRA
     RKREHSSQSS SNGNTPTKKV ATPVLVAAPL KPTSVTAGSS SSDEDSSSSA ESSSKSSSSS
     SSSDDTETQN TNCRIVKLNK TGAVQKKALL GSGSSSASSS GSEPEDQTSR SQVGSGQALA
     QQLPPYKQLP ISQHSQHLSS SECSSSSGGC TAVCSSSSGE EDEGRREKER ERKPKSDKNK
     ISTLTRIFNP KEGGAKKQGQ VVIVDLQEEQ QQGKLDAAAQ PPPPHAPPAA PAAIMAKPRM
     TPTQQQQLGA GLASPARTTT PHLTSLICKI DLSKLSRERI MRLKKLTPAQ QNGHLTPKDQ
     ATNAVHVPNG YAGDTNPAAK VKHEHPVKPE PELDAGYEAK FKPGNVKQEF QLKQERDRDR
     ERERERERER ERDREREQPP GRRRKRSSSS SSSPYKEKKR KKEKADQLQI GKELLPVPVL
     LPSNNHERMP NHDRLSYDKL QLLHEDAAAV IGDVSAANGS PTKKLLVMSP LPPPPTVTVA
     PATCNEAVQT TPPSATTTTA TAPPVPATRL IYRSYFDRDV EHPSDDLRKN NQFLQEAINR
     KHAADLERDS FNQVTLYLEA VVYFLLTADA MERCSSEQAT NTMYKDTLSL IKFISTKFRP
     YQQQSTTNIQ HETHNKVAIL SLRCQSLISL KLYKLRRKDC RAIINGLTDF FRVGRGDIAN
     GNTPSSISPS NSVGSQGSGS NTPPGRIVSP DIHNMLCKQN EFLSYLNSAH ELWDQADRLV
     RTGNHIDFIR ELDHENGPLT LHSTMHEVFR YVQAGLKTLR DAVSHPTHQS Q
 
 
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