ID A0A3S3PM85_9ACAR Unreviewed; 784 AA.
AC A0A3S3PM85;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=AF4/FMR2 family member lilli {ECO:0000256|ARBA:ARBA00021888};
DE AltName: Full=Protein lilliputian {ECO:0000256|ARBA:ARBA00032149};
GN ORFNames=B4U79_00295 {ECO:0000313|EMBL:RWS15478.1}, B4U79_01892
GN {ECO:0000313|EMBL:RWS15493.1}, B4U79_15290
GN {ECO:0000313|EMBL:RWS15503.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS15493.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS15493.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS15493.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:RWS15493.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS15493.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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
CC segmentation. {ECO:0000256|ARBA:ARBA00024653}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000256|ARBA:ARBA00007354}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS15493.1}.
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DR EMBL; NCKU01000444; RWS15478.1; -; Genomic_DNA.
DR EMBL; NCKU01000443; RWS15493.1; -; Genomic_DNA.
DR EMBL; NCKU01000442; RWS15503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3PM85; -.
DR STRING; 1965070.A0A3S3PM85; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0007366; P:periodic partitioning by pair rule gene; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR Gene3D; 6.10.250.2670; -; 1.
DR InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR PANTHER; PTHR10528; AF4/FMR2 FAMILY MEMBER; 1.
DR PANTHER; PTHR10528:SF17; AF4/FMR2 FAMILY MEMBER LILLI; 1.
DR Pfam; PF05110; AF-4; 1.
DR Pfam; PF18876; AFF4_CHD; 2.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Pair-rule protein {ECO:0000256|ARBA:ARBA00022788};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 571..686
FT /note="AF4/FMR2 C-terminal homology"
FT /evidence="ECO:0000259|Pfam:PF18876"
FT DOMAIN 696..784
FT /note="AF4/FMR2 C-terminal homology"
FT /evidence="ECO:0000259|Pfam:PF18876"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 87368 MW; DF751A5E20671F42 CRC64;
MTSTSSQQQQ RSLQREREKY QRERCQQISS GTPLLSSAVH GSNSLFGEPI KQQHEDETTK
RIKSTLGDFD QVQLLLITDH KPLIGISTRE ITRIKGNKLK KCKLEQILSE MKAIQPISGF
DDGDNEEDAS DGESSNDNGK QSEDELSLDE ISDDDNEVKS SRSDDKSTQR KRKLSDSRDN
VQNGDKKRRG SSSSESSDSS SSSSSSSSSS SSSSSEGEDE DGGYPEDSGD ESKVNCARGI
ENENAIKKDL VEPSSKATQP QQPEIATWNL ESFMDQKTTS SSLTTTSSSF TSKTNEKLKT
VDTDNLSTVI DRVAKGELGE DVCFSSPPLS PLISKTKRKS VHQQQRQEKQ SYRQNEQPYL
KPQDPPKTIE KQKSSHQVYA NQHQFLQSIH CETPKESLCR SLSPCETQNY HEKSNSVQIH
SETHQIPRNL VVSINLTYLK RVPRKEKSEL NSISSDKNNN FSKESKSKAS VKEEKKVKSE
DTGSKSKSKI KDFANSTKSK SKSASKKESK ALSQVPEIVK TEVTASAPHY PVKEEPTSFP
SSPTLPPPPL LVPPSHPVKS ASLLQQSSTP EQQGLAADDY LSAAKELKHA ADKECDRTLQ
VCKYLEAVLY FILTGNAMEQ RSGNDLEKVC VMYKETLNLI RHISSKFAKS RSSHQGDVPT
TDHKLTALSY RCQSLLVLKL SRLKGKEIRD NFKAIQSQSQ EIPMSGNTVT LPTSTYSLMQ
KQILLLQQLN NAHDLWQQAD NLVERDPSCK AFFNTIDKEC NCLSLNSSFD QLVRYVKTGL
TLLK
//