ID C3XWT8_BRAFL Unreviewed; 1803 AA.
AC C3XWT8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=AF4/FMR2 family member lilli {ECO:0000256|ARBA:ARBA00021888};
DE AltName: Full=Protein lilliputian {ECO:0000256|ARBA:ARBA00032149};
GN ORFNames=BRAFLDRAFT_88413 {ECO:0000313|EMBL:EEN67198.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN67198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67198.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN67198.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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}.
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DR EMBL; GG666471; EEN67198.1; -; Genomic_DNA.
DR RefSeq; XP_002611188.1; XM_002611142.1.
DR STRING; 7739.C3XWT8; -.
DR eggNOG; KOG0409; Eukaryota.
DR InParanoid; C3XWT8; -.
DR GO; GO:0032783; C:super elongation complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0007366; P:periodic partitioning by pair rule gene; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10528; AF4/FMR2 FAMILY MEMBER; 1.
DR PANTHER; PTHR10528:SF17; AF4_FMR2 FAMILY MEMBER LILLI; 1.
DR Pfam; PF18876; AFF4_CHD; 2.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 11..101
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 104..205
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT DOMAIN 1487..1728
FT /note="AF4/FMR2 C-terminal homology"
FT /evidence="ECO:0000259|Pfam:PF18876"
FT DOMAIN 1746..1802
FT /note="AF4/FMR2 C-terminal homology"
FT /evidence="ECO:0000259|Pfam:PF18876"
FT REGION 326..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1803 AA; 193464 MW; D91019F265940DCB CRC64;
MQKSLTEHPS TNLVFGTSGV LQSIRPGKAY VEMSTIDVET VQDVAESIES RGGRFLEAPV
IGTRKPAEDG MLVIVAGGDR SLFDDCESCF LAMGKKAFYL GEVGSGTRMK LVANMVLGSV
MAGYAEGMSL AERAGLDLQT VLDVFKEGPL NCAAVRSKGD AILHSRFEPS FPLKHQQKDM
RLALALGDEL KQSLPVAAAA NELVVLLNVE KCSVYSAVVV VSGSVDRVEL RRQAQLQRAG
MKVSTETPAV SKPLFDAPVK IDPPPDDHVY RKTQNNFPHV CSRLTPLPTT ICTIDPPPDD
HVYRKTQNNF PHVCSRLNPL LTTLCTPDSS SSASSSIKME ASSTKDDAFQ MPAPLSTAPG
SHRPSHSGGK AGDRPEERPN GLLAAPGHGG KKEGVEKELS REDVKRKLTL TMPDTSEEAR
LNSSGGLKSA GTEKVEIILK GRNCVYHPQS RVRAPVVVGY RRTRLDVSPD EDRMLLSPGE
VVRITLLDFA GVCPPRNENP IISYEDLIAD EVPALGAEAQ EMTEVGPPLT GIHTPIKTDV
SKFPFPANQD VPSAQLSRTK RKTTAESSGG GKTKPMGPSS EPKWGIGSII PRDQWVLVTA
CHPQASRWAG GKAPVPACLR CAFIAVCRVN TLVGGSFGRE PLGLWGRDKA GSSAGGDFSS
RRFTGSSAPW LKKYFLDMSD SEDDDDQARQ TKTAGRNAQK MSVGAVLSFN APEVLTDHRD
LPGHIGRFQS GDLLTVLSAN ESRCPSVNRR SGRSCEKKSG HVSVVGIYHG LLPAWSGDPT
CDEGSSSSDE SVQDAPPPAS PPKCDEGSSS SDESVQDAPP PASPPKCYEG SSSSDESVQD
APPPASPPKC DDGSSSSDES VQDAPPPASP PKQESDTTNW GLASFVNPVK RDSPGNSFPL
LVSAGGGGTP AANATNSAAL PMGLFGGDEG PLSSAGFMTS SDSHGFDVND ILQPLDSSKE
LDPDHKDNYS ATKINGLRMK ISKKGQGGPE PTGCSSNSTS SSNKEVSKKS SVGKSPSTAS
RNSSKTATNR TPRKGADKKP AERPASASNA KAESSEKTKA NSSKAGQTTP SNKTNWAEPS
PKADKTTKTV QGKKSSDKKG KRTPQTSSKV KSKEFIDSDS ESDLEVDVVN ISPEKGGASV
KASPSPRAKL NSSSKPKARD SGKKAAASSS GGGSQEKALS VDVLSSDNSL LSPLNEPLLS
PIEGDLASTV PKITYGNNGI PKSLIVSIDL SLLDRIPARK DSSRQGDSKK SSSSSESKPR
SKVQKRKRDN SQSQADAAGA STAEEVQTKR PKKEKEATSD SKATPTRSLP TPTRTLPIPA
TSLSTPTRNL PTPTRTPSQA TPTRTTPTRT PPSSRQDTEK GRGSARRSSV SSTSSRLSEE
SAKTDRSAKR RKVERQTSQE SSKKKEKKTK KTPKKQQVPS RCQDWDAPPA VVPEHSQNGV
ATEPVAKATN GHAAGSQWGE LASGQHGGKA WERHDPRGDI PYFTSSKTDA EDRPLSADHY
LTEAKNLKHL ADGLADKNQK TLTYVDAVLY FIQCGNAMES DPHLSESKSP STMYLETVDL
IKFILRFNSH HMHNQSQDQT TSDKKLAVLC LRCQSLLYMK LFKLKKDYAM KYSKALTDHF
KNPPKNTQVP SPYQHNWNGA RGTGTPSPMS PTPSPAGSVT SVGSQGSNNG DLTLNTPTQN
KLSNGTSGSS VTIPQRIHSL MQEHLKITNH LLHSQDLWEQ ANTLAQENPG EPRYVTHSHR
RTQVRTNHLL HSQDLWEQAN TLAQENPEFF RRLDQRLGAL TLHSTLIELV RYVRQGLQWL
KES
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