FLNA_DROME
ID FLNA_DROME Reviewed; 2210 AA.
AC Q9VEN1; Q7KJX2; Q7KKC2; Q9GQV1; Q9U4I3; Q9U6C0; Q9U6C1;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Filamin-A;
DE Short=FLN-A;
DE AltName: Full=Actin-binding protein 280;
DE Short=ABP-280;
DE AltName: Full=Filamin-1;
DE AltName: Full=Filamin1;
GN Name=cher; Synonyms=cheerio, sko; ORFNames=CG3937;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=10556087; DOI=10.1016/s0960-9822(99)80502-8;
RA Sokol N.S., Cooley L.;
RT "Drosophila filamin encoded by the cheerio locus is a component of ovarian
RT ring canals.";
RL Curr. Biol. 9:1221-1230(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10477759; DOI=10.1083/jcb.146.5.1061;
RA Li M.G., Serr M., Edwards K., Ludmann S., Yamamoto D., Tilney L.G.,
RA Field C.M., Hays T.S.;
RT "Filamin is required for ring canal assembly and actin organization during
RT Drosophila oogenesis.";
RL J. Cell Biol. 146:1061-1074(1999).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH TEN-M.
RX PubMed=21857973; DOI=10.1371/journal.pone.0022956;
RA Zheng L., Michelson Y., Freger V., Avraham Z., Venken K.J., Bellen H.J.,
RA Justice M.J., Wides R.;
RT "Drosophila Ten-m and filamin affect motor neuron growth cone guidance.";
RL PLoS ONE 6:E22956-E22956(2011).
CC -!- FUNCTION: Involved in the germline ring canal formation. May tether
CC actin microfilament within the ovarian ring canal to the cell membrane.
CC Contributes to actin microfilaments organization.
CC {ECO:0000269|PubMed:10477759, ECO:0000269|PubMed:10556087}.
CC -!- SUBUNIT: Interacts with Ten-m. {ECO:0000269|PubMed:21857973}.
CC -!- INTERACTION:
CC Q9VEN1; O61307: Ten-m; NbExp=4; IntAct=EBI-133626, EBI-118556;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane.
CC Note=Localizes to intercellular bridges corresponding to ring canals
CC that connect cytoplasm of nurse cells to the developing oocyte.
CC Localizes to nurse cell plasma membranes. Detected in both the inner
CC and outer rims of the ring canal.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Filamin A, filamin 240;
CC IsoId=Q9VEN1-1; Sequence=Displayed;
CC Name=2; Synonyms=Filamin B, filamin 90;
CC IsoId=Q9VEN1-2; Sequence=VSP_045205;
CC -!- TISSUE SPECIFICITY: Germline-specific in females (at protein level).
CC Expressed in ovary. {ECO:0000269|PubMed:10477759,
CC ECO:0000269|PubMed:10556087}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the egg-chamber development
CC (at protein level). Expressed in the embryo.
CC {ECO:0000269|PubMed:10477759, ECO:0000269|PubMed:10556087}.
CC -!- DISRUPTION PHENOTYPE: Shows defect in ring canal assembly and female
CC sterility. {ECO:0000269|PubMed:10477759}.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF25614.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF188360; AAF04108.1; -; mRNA.
DR EMBL; AF188361; AAF04109.1; -; mRNA.
DR EMBL; AF174492; AAF25614.1; ALT_INIT; mRNA.
DR EMBL; AE014297; AAF55390.4; -; Genomic_DNA.
DR EMBL; AE014297; AAN13734.1; -; Genomic_DNA.
DR EMBL; AF183182; AAG43432.1; -; Genomic_DNA.
DR RefSeq; NP_001262656.1; NM_001275727.1. [Q9VEN1-2]
DR RefSeq; NP_524383.3; NM_079659.4. [Q9VEN1-1]
DR RefSeq; NP_732207.1; NM_169746.3. [Q9VEN1-2]
DR AlphaFoldDB; Q9VEN1; -.
DR SMR; Q9VEN1; -.
DR BioGRID; 67106; 65.
DR IntAct; Q9VEN1; 45.
DR STRING; 7227.FBpp0304475; -.
DR PRIDE; Q9VEN1; -.
DR DNASU; 42066; -.
DR EnsemblMetazoa; FBtr0089471; FBpp0088478; FBgn0014141. [Q9VEN1-1]
DR EnsemblMetazoa; FBtr0089473; FBpp0088480; FBgn0014141. [Q9VEN1-2]
DR EnsemblMetazoa; FBtr0332167; FBpp0304476; FBgn0014141. [Q9VEN1-2]
DR GeneID; 42066; -.
DR KEGG; dme:Dmel_CG3937; -.
DR UCSC; CG3937-RA; d. melanogaster. [Q9VEN1-1]
DR UCSC; CG3937-RB; d. melanogaster.
DR CTD; 42066; -.
DR FlyBase; FBgn0014141; cher.
DR VEuPathDB; VectorBase:FBgn0014141; -.
DR HOGENOM; CLU_000783_0_0_1; -.
DR InParanoid; Q9VEN1; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-446353; Cell-extracellular matrix interactions.
DR Reactome; R-DME-5627123; RHO GTPases activate PAKs.
DR SignaLink; Q9VEN1; -.
DR BioGRID-ORCS; 42066; 0 hits in 3 CRISPR screens.
DR ChiTaRS; cher; fly.
DR GenomeRNAi; 42066; -.
DR PRO; PR:Q9VEN1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0014141; Expressed in oviduct (Drosophila) and 32 other tissues.
DR ExpressionAtlas; Q9VEN1; baseline and differential.
DR Genevisible; Q9VEN1; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0045179; C:apical cortex; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0035324; C:female germline ring canal; IDA:UniProtKB.
DR GO; GO:0035183; C:female germline ring canal inner rim; IDA:FlyBase.
DR GO; GO:0035182; C:female germline ring canal outer rim; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0051764; P:actin crosslink formation; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0007301; P:female germline ring canal formation; IMP:FlyBase.
DR GO; GO:0008302; P:female germline ring canal formation, actin assembly; IMP:UniProtKB.
DR GO; GO:0030708; P:germarium-derived female germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0030725; P:germline ring canal formation; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IMP:FlyBase.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0110069; P:syncytial embryo cellularization; IMP:FlyBase.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 20.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR044801; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR38537; PTHR38537; 2.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 18.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 20.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF81296; SSF81296; 20.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 20.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome; Repeat.
FT CHAIN 1..2210
FT /note="Filamin-A"
FT /id="PRO_0000421126"
FT DOMAIN 15..120
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 139..242
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 249..347
FT /note="Filamin 1"
FT REPEAT 349..447
FT /note="Filamin 2"
FT REPEAT 448..544
FT /note="Filamin 3"
FT REPEAT 545..635
FT /note="Filamin 4"
FT REPEAT 638..734
FT /note="Filamin 5"
FT REPEAT 735..831
FT /note="Filamin 6"
FT REPEAT 832..929
FT /note="Filamin 7"
FT REPEAT 930..1022
FT /note="Filamin 8"
FT REPEAT 1023..1121
FT /note="Filamin 9"
FT REPEAT 1122..1217
FT /note="Filamin 10"
FT REPEAT 1218..1312
FT /note="Filamin 11"
FT REPEAT 1322..1423
FT /note="Filamin 12"
FT REPEAT 1424..1515
FT /note="Filamin 13"
FT REPEAT 1516..1603
FT /note="Filamin 14"
FT REPEAT 1606..1698
FT /note="Filamin 15"
FT REPEAT 1699..1796
FT /note="Filamin 16"
FT REPEAT 1799..1891
FT /note="Filamin 17"
FT REPEAT 1893..1986
FT /note="Filamin 18"
FT REPEAT 1988..2079
FT /note="Filamin 19"
FT REPEAT 2116..2210
FT /note="Filamin 20"
FT VAR_SEQ 1..1372
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10556087"
FT /id="VSP_045205"
SQ SEQUENCE 2210 AA; 239181 MW; A600974971A3FD84 CRC64;
MEAERDLAED AQWKKIQQNT FTRWANEHLK TIDRSINNLE TDLSDGLRLI ALIEVLSQKR
MPKYNKRPTF RSQKLENVSV ALKFLQDEGI KIVNIDSSDI VDCKLKLILG LIWTLILHYS
ISMPMWDGED DKQLNGSGHT PKQRLLNWIH AKIPDLPINN FTNDWTTGKA VGALVDACAP
GLCPDWELWD PKDAVQNASE AMGLADDWLN VRQLIKPEEL VNPNVDEQSM MTYLSQYPNS
KLKTGAPLRP KTNPNRVRAY GPGIEPIGPV VGAPANFTVE TFSAGKGSVD VDIQGPNGEI
EKADVRFNND KNLTYTVSYI PKSEGSHKVA VKFSGRDIPK SPFPVKVEGH AGDASKVKVT
GPGIQPNGVT IKKPTFFDIL AKDAGRGVPE VIIIDPANHK TSVAAKVRQL ENDTWRCEYV
TALQGLHSVN VFYAGTPIPN SPFPVKVAPL SDARKVRASG RGLQATGVRV GDDADFKIYT
EGAGEGEPEV RVIGPGGMNQ NVMQSKVDGN TYECHYYPTK EGRYVIMVTF AGQEVAKSPF
EVKVGPKKES SIVAYGPGLS SGVIGYPAAF VVETNGETGA LGFTVAGPSQ AEIECHDNGD
GSALVKYHPT AVGEYAVHIL CDNEDIPKSP FIAQILPRTD FHPELVKASG PGLEKNGVTI
NQPTSFTVDP SKAGNAPLDV VVQDVFGTKL PVELKNNPDG TKKVTYTPTS GVPHTVEVNY
GGVSTPNSPH RVYVGVPVDA AKVQAFGPWL QPGVRPNAAT HFNVDAREAG DAELKVKIIH
EETKIEVPCR IIDNEDNTYS VEVIPPSKGA YTTTMTYGGQ RVPLGEKVVV EQTVDVSKIK
VDGLEPSVIM NAATDFMVDM SKVGSNIDSG KLSCAIFDPM GHVLPSKIVQ GPTDDIFRIM
YTPFEAGRHT IELMYDNIPV PGSPFVVNVK SGCDPARCKA YGPGLEKGLT NQKNKFTVET
KGAGNGGLSL AIEGPSEAKM TCTDNRDGSC DVDYLATDPG EYDITIRFAD KHIPGSPFRV
LVEETVDPSK VKVYGPGIEH GQVRESVPTF FNVDVGEAGP GRIAVKLTNS EGIPVDNLRV
EDKGNCIYAV HYVPPKAGSV LTCQVKFSEV EVPCSPFVMT VFPKSEPTKV KVKGVNEKKK
TPASLPAEFE IDTKQAGQAD INVAIKNPKG KAMQPRLEEV STGTYVVSFV PDECGTYQCS
IKYGDKEIEG SPFKLEAFPT GEAKKCKLVE QAPKIQTSGS QSHLKVDARE AGDGAVTCKI
TNKAGSEIVD IDVIEKDGFF DILYALNDPG DYDINVKFGG KDIPNGSFSI KAVESIEQYS
HSEYIEEHTT KVVQQTTQSE LVNGKSEITY RSVAFEKLPL PTTGGNVTAE VRMPSGKVDK
PVIQDNRDGT VSVKYDPREE GSHELVVKYN GEPVQGSPFK FHVDSITSGY VTAYGPGLTH
GVTGEPANFT ISTKGASAGG LTMAVEGPSK ADINYHDNKD GTVSVQYLPT APGEYQVSVR
FGDKHIKGSP YFAKITGEGR KRNQISVGSC SEVTMPGDIT DDDLRALNAS IQAPSGLEEP
CFLKRMPTGN IGISFTPREI GEHLVSVKRL GKHINNSPFK VTVCEREVGD AKKVKVSGTG
LKEGQTHADN IFSVDTRNAG FGGLSVSIEG PSKAEIQCTD KDDGTLNISY KPTEPGYYIV
NLKFADHHVE GSPFTVKVAG EGSNRKREKI QRERDAVPIT EIGSQCKLTF KMPGITSFDL
AACVTSPSNV TEDAEIQEVE DGLYAVHFVP KELGVHTVSV RYSEMHIPGS PFQFTVGPLR
DSGSHLVKAG GSGLERGVVG EAAEFNVWTR EAGGGSLAIS VEGPSKADIE FKDRKDGSCD
VSYKVTEPGE YRVGLKFNDR HIPDSPFKVY VSPDAGDAHK LEVQQFPQGN IQADAPYQFM
VRKNGAKGEL DAKIVAPSGT DDDCFIQVID GEMYSVRFYP RENGIHAIHV KFNGVHIPDS
PFRIKVGKDV ADPAAVHASG NGLDEVKTGH KADFIINTCN AGVGTLAVSI DGPSKVAMDC
TEVEEGYKVR YTPLLPGEHY ITVKYNNMHI VGSPFKVNAT GDKLADEGAQ ETSTVIVETV
QKVAKGGKNT GVHLPTFKSD ASKVVSKGMG LKKAYIGKQN QFSISATDAG NNILYVGMYG
PKGPCEEFHV KHAGHNNYNV QYLVRDRGQY VLLIKWGEEH IPGSPFQIDV
