ID A0A151WMC5_9HYME Unreviewed; 2423 AA.
AC A0A151WMC5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Filamin-A {ECO:0000313|EMBL:KYQ48951.1};
GN ORFNames=ALC60_12006 {ECO:0000313|EMBL:KYQ48951.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ48951.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ48951.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ48951.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ48951.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the filamin family.
CC {ECO:0000256|ARBA:ARBA00009238}.
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DR EMBL; KQ982944; KYQ48951.1; -; Genomic_DNA.
DR STRING; 64791.A0A151WMC5; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR CDD; cd21311; CH_dFLNA-like_rpt1; 1.
DR CDD; cd21315; CH_dFLNA-like_rpt2; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 22.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
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; JITTERBUG, ISOFORM N; 1.
DR PANTHER; PTHR38537:SF17; JITTERBUG, ISOFORM N; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 22.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 22.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF81296; E set domains; 22.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 22.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 35..140
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 156..259
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REPEAT 266..364
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 366..462
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 463..559
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 559..632
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 635..731
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 732..827
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 877..956
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 957..1049
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1052..1131
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1132..1224
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1223..1316
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1317..1412
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1425..1508
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1578..1636
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1636..1728
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1726..1817
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1820..1912
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1910..2010
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2013..2105
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2107..2200
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2202..2293
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2329..2423
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2423 AA; 262175 MW; 07AE98EB8061B691 CRC64;
MNENDKSVKC ENSAGEEEED EMFERELAED AQWKRIQQNT FTRWANERLK VANKHIGDLE
CDLSDGLQLV SLIEVLSQKR LPKHNQRPTF RSQKLENVSV ALKFLEDEGI RLVNIDSSDI
VDCKLKLILG LIWTLILHYS ISMPMWEGDD GEDKGATPKQ RLMHWIQSKV PDLPISNFTS
DWNDGRAVGA LVDAVAPGLC PDWREWNPKD AVQNASEAMG LADDWLNIPQ LIKPEEMVNP
NIDEMSMMTY LSQYPSAKLK PGAPLRARTN PNRVRAYGPG IEPTGSIVGA PANFTVETFS
AGKGNVDVIV DDPKGNKLPV DIRFNKDRNL TYSVSYTPKM EGPHKVKVLF AGREIPKSPY
TVNVEGHAGD PSKVTASGPG LQPEGVVVNR PTFFDIFTKD AGRGVPEIII LDPQGNKTTV
KLRQTSPDVW RCEYVSPVTG LHSVNIFFAG KPIPRSPIGV NIAPVSDAKK CRAYGRGLLP
TGVRVQDIAD FVVLTKDAGE GVPDIRVIGP GGVNQPIRMS KTDATTYKCH YTPVKEGRHV
VMITYGGKEI PKSPFEVNVG PYKESNIKAF GPGLHTGVVG HPAKFTVNTN ECNDNGDDPA
DVSYLPTAPG QYAVHILCDN EDIPKSPYIA TILPKTDFDP EKVEVYGPGI QPEGVAKDEP
TNFTIDAREA GQAALEVAIQ DALGKEVPLR LGDNRNGTVQ AHYTPISSSP HVVMVNYGGV
ATKKSPYRVK IASPLNPAMV SAFGPGLEKG VKSNVPTHFN VDCREAGPGK LDVKMLNPEG
RELPISLTDN EDGTYVVDYM PPQPGNYTVN LNYGGLKVPQ CPIKVNVQPH VDVSKIKVDG
LAPIGATSVR CSRAVVPSRK HKRKMHRGSP REPANVLAAA PVNSLQQFRV ITQEAGRAAD
FQVAITTPSG NRVKAHVVPT HEGYLVNFTP TELGEYLLGI SFGGEPISNQ PYRLTCVHGS
DPGKVRASGP GLSHGVVNKP AEFVIDTRGA GQGGLGVTVE GPCEAAINCR DNGDGTCSVA
YLPTETGDYG INITFNEQHV PGSPFQAIGL FVNKQTTFTI DARDITKSKT DDGKVSCIIN
NPSGGKTEKL IIPQGDGTYC VSYTPFEEGY YTIDILYDNV PIPGSPFSVN VQRTSDPSKC
RAYGPGLEQG VTEKTNYFTV ETEGAGNGGL GVSITGDGEV SAEAREKWDG SCDVEYVTSE
PGDYEIDIKF AEQSIPGSPF KIKVISPKKD VIAYGPGLHM VREGVPAKFT VDASKCIEAP
VKVRLSPDMG QQPQVKSKGD GLYEVTYQPP PAGNNIRLDV TFDDEYINGS PFEVKVLPFV
EPNKVTLSGP GVSPFCTASF PIDFIVDTSN AGYGDLEVQV VGPDQVPRKV VVQDLGDGKY
KATYLPDDCG RYKVNVKYGG KEVPNSPVTV QSTSIGSANN CKIKEGIQHT LAQGEEYCIT
VDTENAGRGA VTCRIRSTTG SEVVDIDIED NGDGTVNIYY TVADAGDYTL SIKFGGQPVP
DGFYTFTASE EYREHSTHKT QRARKTRQKQ NQHVEQRSTT LQESSTVTTK RSSQQELSKK
NFNVIRLNSI PLPLPSGGTV TSEVKMPSGN VDKPVIEDNH DGTVSIKYEP REEGLHEIYV
KFNGEHVQGS PYKFHVDSLA SGYVTAYGPG LVYGVCGEPG NFTISTKGAG AGGLSLAVEG
PSKAEISCHD NKDGTVSVSY LPTAPGEYKI TVKFGDKHIR GSPFVAKITG EGRKRNQISV
GSSSEVQLPG KVSDADIKSL NASITAPSGL EEPCFLKKMP GSGNMCVSFT PREAGEHTVS
VKRMGKHIPN SPFKIDVKDR EVGDAKKVKV SGPGLKEGKT HVENKFSIDT RNAGFGGLSL
SMEGPSKAEI QCKDNEDGTL NISYKPTEPG YYIMNLKFAD HHVEGSPFTV KVSGEGSNRQ
REKIQRQREA VPITEVGNQC KLTFKMPGIT SFDLAATVTS PGGVTEDAEI KEAEDGIYAV
AFVPKELGVH TVSVRYKSMH IPGSPFQFTV GPLRDGGAHR VHAGGPGLER GEQGEPCEFN
IWTREAGAGT LAVSVEGPSK AQIDFKDRKD GSCYVSYVVS EPGEYRVGIK FNDQHIPDSP
HKVYISPAMG DAHKLEVAQF PESGVQPDKP CTFLVRKNGA KGELDGKLVS PSGTQDDCFI
QSIDADTYSV RFMPTENGIH QIHLKFNGVH ISGSPYRVKV GKVDADPAAL HAYGNGLKEI
KTGQKTDFII DTCNAGSGAL GVTVDGPSKV AMDCTEVEEG YKVRYTPLVP GDYYISIKYN
GYHIVGSPYK VPCTGADLAE RGAQETSSIV VETVQKISKS KQTGPILPLF KSDAGKVTSK
GMGLKKAYLG KQNQFTVHAG DAGNNILYVG VYGPKGPCEE VFVKHTGRNN YNVSYLVRER
GEYIVIVKWG DDHIPGSPYK VEV
//
