FLII_DROME
ID FLII_DROME Reviewed; 1256 AA.
AC Q24020; Q24088; Q9VRH0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein flightless-1;
DE AltName: Full=Flightless-I;
GN Name=fliI; ORFNames=CG1484;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8248259; DOI=10.1073/pnas.90.23.11386;
RA Campbell H.D., Schimansky T., Claudianos C., Ozsarac N., Kasprzak A.B.,
RA Cotsell J.N., Young I.G., de Couet H.G., Miklos G.L.G.;
RT "The Drosophila melanogaster flightless-I gene involved in gastrulation and
RT muscle degeneration encodes gelsolin-like and leucine-rich repeat domains
RT and is conserved in Caenorhabditis elegans and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11386-11390(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-601.
RC STRAIN=Canton-S;
RX PubMed=8582612; DOI=10.1093/genetics/141.3.1049;
RA de Couet H.G., Fong K.S.K., Weeds A.G., McLaughlin P.J., Miklos G.L.G.;
RT "Molecular and mutational analysis of a gelsolin-family member encoded by
RT the flightless I gene of Drosophila melanogaster.";
RL Genetics 141:1049-1059(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=9520435; DOI=10.1073/pnas.95.7.3731;
RA Maleszka R., de Couet H.G., Miklos G.L.G.;
RT "Data transferability from model organisms to human beings: insights from
RT the functional genomics of the flightless region of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
CC -!- FUNCTION: May play a key role in embryonic cellularization by
CC interacting with both the cytoskeleton and other cellular components.
CC Alternatively, it may play a structural role in indirect flight muscle.
CC Vital for embryonic development.
CC -!- TISSUE SPECIFICITY: Found in ovaries, larval fat bodies, brain and
CC adult thorax.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC -!- DOMAIN: Consists of a leucine-rich N-terminal half, which is likely to
CC be involved in protein-protein interaction, and a C-terminal half which
CC has high sequence similarity to gelsolin and is therefore likely to be
CC involved in actin-binding.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; U01182; AAC03566.1; -; mRNA.
DR EMBL; AF017777; AAC28407.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF50830.2; -; Genomic_DNA.
DR EMBL; AF132184; AAD34772.1; -; mRNA.
DR PIR; S60461; S60461.
DR RefSeq; NP_525097.1; NM_080358.3.
DR AlphaFoldDB; Q24020; -.
DR SMR; Q24020; -.
DR BioGRID; 59388; 6.
DR IntAct; Q24020; 10.
DR STRING; 7227.FBpp0076893; -.
DR PaxDb; Q24020; -.
DR PRIDE; Q24020; -.
DR DNASU; 33110; -.
DR EnsemblMetazoa; FBtr0077192; FBpp0076893; FBgn0000709.
DR GeneID; 33110; -.
DR KEGG; dme:Dmel_CG1484; -.
DR CTD; 2314; -.
DR FlyBase; FBgn0000709; fliI.
DR VEuPathDB; VectorBase:FBgn0000709; -.
DR eggNOG; KOG0443; Eukaryota.
DR eggNOG; KOG0444; Eukaryota.
DR GeneTree; ENSGT00940000156643; -.
DR HOGENOM; CLU_002568_1_0_1; -.
DR InParanoid; Q24020; -.
DR OMA; CFHGWSA; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q24020; -.
DR SignaLink; Q24020; -.
DR BioGRID-ORCS; 33110; 0 hits in 1 CRISPR screen.
DR ChiTaRS; fliI; fly.
DR GenomeRNAi; 33110; -.
DR PRO; PR:Q24020; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000709; Expressed in oocyte and 25 other tissues.
DR Genevisible; Q24020; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; ISS:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:FlyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0010004; P:gastrulation involving germ band extension; IMP:FlyBase.
DR GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
DR Gene3D; 3.40.20.10; -; 6.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR029919; FliI.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF85; PTHR11977:SF85; 1.
DR Pfam; PF00626; Gelsolin; 4.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00369; LRR_TYP; 12.
DR PROSITE; PS51450; LRR; 10.
PE 2: Evidence at transcript level;
KW Actin-binding; Developmental protein; Leucine-rich repeat;
KW Reference proteome; Repeat.
FT CHAIN 1..1256
FT /note="Protein flightless-1"
FT /id="PRO_0000218749"
FT REPEAT 4..28
FT /note="LRR 1"
FT REPEAT 29..51
FT /note="LRR 2"
FT REPEAT 52..74
FT /note="LRR 3"
FT REPEAT 75..99
FT /note="LRR 4"
FT REPEAT 100..122
FT /note="LRR 5"
FT REPEAT 124..145
FT /note="LRR 6"
FT REPEAT 147..169
FT /note="LRR 7"
FT REPEAT 171..192
FT /note="LRR 8"
FT REPEAT 218..241
FT /note="LRR 9"
FT REPEAT 243..264
FT /note="LRR 10"
FT REPEAT 265..287
FT /note="LRR 11"
FT REPEAT 289..312
FT /note="LRR 12"
FT REPEAT 313..335
FT /note="LRR 13"
FT REPEAT 336..358
FT /note="LRR 14"
FT REPEAT 360..381
FT /note="LRR 15"
FT REPEAT 499..557
FT /note="Gelsolin-like 1"
FT REPEAT 746..789
FT /note="Gelsolin-like 2"
FT REPEAT 1064..1102
FT /note="Gelsolin-like 3"
FT REPEAT 1165..1206
FT /note="Gelsolin-like 4"
FT REGION 405..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 601
FT /note="G -> S"
FT /evidence="ECO:0000269|PubMed:8582612"
FT CONFLICT 1068
FT /note="T -> A (in Ref. 3; AAC28407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1256 AA; 143682 MW; CF0056EFAA88DB92 CRC64;
MSVLPFVRGV DFTKNDFSAT FPSSMRQMSR VQWLTLDRTQ LAEIPEELGH LQKLEHLSLN
HNRLEKIFGE LTELSCLRSL DLRHNQLKNS GIPPELFHLE ELTTLDLSHN KLKEVPEGLE
RAKNLIVLNL SNNQIESIPT PLFIHLTDLL FLDLSHNRLE TLPPQTRRLI NLKTLDLSHN
PLELFQLRQL PSLQSLEVLK MSGTQRTLLN FPTSIDSLAN LCELDLSHNS LPKLPDCVYN
VVTLVRLNLS DNELTELTAG VELWQRLESL NLSRNQLVAL PAALCKLPKL RRLLVNDNKL
NFEGIPSGIG KLGALEVFSA ANNLLEMVPE GLCRCGALKQ LNLSCNRLIT LPDAIHLLEG
LDQLDLRNNP ELVMPPKPSE ASKATSLEFY NIDFSLQTQL RLAGAAVPPS MPSSATPKDS
TARKIRLRRG PRSEGDQDAA KVLKGMKDVA KDKDNEAGAV PEDGKPESLK PKRWDESLEK
PQLDYSKFFE KDDGQLPGLT IWEIENFLPN KIEEVVHGKF YEGDCYIVLK TKFDDLGLLD
WEIFFWIGNE ATLDKRACAA IHAVNLRNFL GARCRTVREE QGDESEQFLS LFETEVIYIE
GGRTATGFYT IEEMIHITRL YLVHAYGATI HLEPVAPAIT SLDPRHAFVL DLGTHIYIWM
GERSKNTLNS KARLMAEKIS KTERKNKCEI QLERQGEESA EFWQGLGMTS EEADAAEPPK
EHVPEDYQPV QPRLYQVQLG MGYLELPQVE LPEQKLCHTL LNSKHVYILD CYTDLFVWFG
KKSTRLVRAA AVKLSRELFN MMDRPDYALV MRVPEGNEMQ IFRTKFAGWD EVMAVDFTRT
AKSVAKTGAN LTQWARQQET RTDLAALFMP RQSAMPLAEA EQLEEEWNYD LEMMEAFVLE
NKKFVRLPEE ELGRFYTGEC YVFLCRYCIP IEEPENGSED GANPAADVSK SSANNQPEDE
IQCVVYFWQG RNAGNMGWLT FTFTLQKKFK AMFGEELEVV RIFQQQENLK FMSHFKRKFI
IHTGKRKDKA HTAKGKSPVE FFHLRSNGGA LTTRLIQINP DAVHLNSTFC YILHVPFETE
DDSQSGIVYV WIGSKACNEE AKLVQDIAEQ MFNSPWVSLQ ILNEGDEPEN FFWVALGGRK
PYDTDAEYMN YTRLFRCSNE RGYYTVAEKC ADFCQDDLAD DDIMILDNGE HVFLWMGPRC
SEVEVKLAYK SAQVYIQHMR IKQPERPRKL FLTMKNKESR RFTKCFHGWS AFKVYL
