ID A0A0V0WUQ5_9BILA Unreviewed; 1224 AA.
AC A0A0V0WUQ5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=AF4/FMR2 family member lilli {ECO:0000256|ARBA:ARBA00021888};
DE AltName: Full=Protein lilliputian {ECO:0000256|ARBA:ARBA00032149};
GN Name=Aff4 {ECO:0000313|EMBL:KRX79230.1};
GN ORFNames=T06_11212 {ECO:0000313|EMBL:KRX79230.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79230.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX79230.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX79230.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX79230.1}.
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DR EMBL; JYDK01000056; KRX79230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WUQ5; -.
DR STRING; 92179.A0A0V0WUQ5; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; 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; PF18876; AFF4_CHD; 1.
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:UP000054673};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 894..1096
FT /note="AF4/FMR2 C-terminal homology"
FT /evidence="ECO:0000259|Pfam:PF18876"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1224 AA; 135042 MW; 66076BACBAF133EF CRC64;
MKKIISSSLQ MQEREALRRQ AEEARRSGVA KVASKPQEHL SCAPVFDPPF RVRDNDEDSL
HVRLKRSLGS FEEVSRYLFN GMRLPGVDCR PVQSGNDSSF VNGIQNSQAE ANSQYACETY
KNGPQRPPKP PSSTSRGKSS TGTSPVVKSL KNSPTKNGSK HHNNHIHQAN PTSSNTTSKH
CTDADPLSGC LDDLSHCPLE VATLIKKVQE MIPAPLTAIS TPRKERKCDF KKNEQQQHLN
GYSSTEEQQH CNGVASKQAT IFASNADYYY DQQAVKTATV IDAFGKKSLS TTTSNNVELV
ENSLKRESSF SVLNRDLELS EDSDSDSEES DDSTSSTKLS DTVLAKVESL SESEQRRCTT
ATTSTITAAA ATTTTNITTA SAAAAAVANT TSTTTTTTIN KKNNNTGSKN MLESSPFSEA
GSETKEESNE APENPWDIDY LISKILFPKV PGSENGQLMN GGLLSPIPPN HHCNGNKAMD
EDDLEEEEVD AIGADVKEKI DSLFEEKKKN VGKVRKKNKA DRTPDKGSLL SPAGKSKKRS
KVAAKVENAD EMVAGEQVKV QEKFDNFQIP SKVKRKSSKC NKLNNEKLSN VKCENDSKQI
TVATTLHNNN NSSNSVVVQS RTTNVVDTIL KEINLPAPLS PIRDLNKHPK QNNKKKSLKC
LLDLQLVRKV PTPVFEKAKQ CGIDLKLEKK SDNVKIKKDP LKHSKLTDHK PTSKEHNCCT
DGFDAKTVEK RNYNHTTTTT TTSINNNNSN TGTVDDFPKI RTELDEKFMK ERVQRTLECL
KRSSSSSVAV VDSKRDTPLT NGIVPVKHSS STTQAKNVVG TEETATTTAT VVKRPTPPVT
SGTVNHQSAK NQVDSPKRKA TSKIEQAEIT PAKKSRTDNF MQNCLAAAPL LPFKLKYDDT
VDPTKYLQEA KTVKHSADAE ATDKSLRIIT YLESICYFML TGNCMLKSLG TESSRPYVMF
KETGDLLKQV YFFINYFASN RRLIDNNINV SEKYLAQSSL STDPYVKFLA PKVEVLTLRI
QAVLCRRLFE LRQPQVFNNY RHINQYQQQM AKDGNRQCCS GNPYTGTGNN SQVSEQHLAP
ACSGASGGAV VMINNNSSRS CQPSPCRPPS ACTHSPTPSP ASSTGSAHSL PPGLVAIPQN
VENLYKQQLS HLHNLMWSHH YWLLIEKKLN TQHGQFFSHV DSVCGALNFT CSIQELCVSV
LTSVHWLRQF HLACQQKTFS NGFN
//
