ID A0A183A5C0_9TREM Unreviewed; 2505 AA.
AC A0A183A5C0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Filamin-A {ECO:0000313|WBParaSite:ECPE_0000215501-mRNA-1};
GN ORFNames=ECPE_LOCUS2155 {ECO:0000313|EMBL:VDP65594.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000215501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000215501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP65594.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP65594.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the filamin family.
CC {ECO:0000256|ARBA:ARBA00009238}.
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DR EMBL; UZAN01039440; VDP65594.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0000215501-mRNA-1; ECPE_0000215501-mRNA-1; ECPE_0000215501.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; 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 Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 20.
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:SF18; FILAMIN-A; 1.
DR PANTHER; PTHR38537; JITTERBUG, ISOFORM N; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 19.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 19.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF81296; E set domains; 20.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 19.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000272942};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 39..145
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 221..324
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REPEAT 431..576
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 577..673
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 673..759
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 763..846
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 847..942
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1004..1096
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1101..1210
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1211..1303
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1304..1402
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1403..1502
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1503..1597
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1633..1707
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1707..1867
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1870..1962
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1986..2052
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2096..2188
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2211..2289
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2289..2381
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 2410..2504
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REGION 182..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2505 AA; 272095 MW; 91F080D72FBD82C7 CRC64;
MYEPSYTDYP DADAGYVDED EEEIPMAERE LAEDAEWKLI QKNTFTRWAN EHLKPKNMIV
DDLQYDFADG LKLIGLVEAL SGQQFKHVNR KPSFRTQKLE NVTMVLRFLE ENEGLRLVNI
DSTDIVDCRS KLILGLIWTL ILHYSITIPL WEGEVDHGVK KKVYRLSATP PTRRRLNQRA
VFEDPKMQDS ENAVKEPTSK ASTLSNKSET PDVTDVQGQG PTPKQRLLSW LNNKLVDRPV
KNFTSDWNDG TAIGALVDAC APGLCPDWRQ WEPKQNLRNA REAMNAAEQW LDVPQLIRPE
EMINPRVDEK AMMTYLSQFP SAKLKEGAPL RPKSTPELVR AYGPAAAFLS QADAEPQQQS
NPPAQKSTQP RGLDVRHGLG VLYALNRQRL SCYLFFFGPK MQKAKTPSKP APTAAGSAAQ
SKNVSPATGK GNAPGTNKTP AKGLERHGNT VGNPARFTID TFSAGRGGVE VIVLNPKGQR
EPCDILSNND RQQTYSCAYV PTQEGEYPAG PGNVDCVILD PHGGRDSIXX SIKPVITKQG
EDNYLVEYTP KDEGLHSVNV FFAGQQIPKS PFGVMVGPTC DPKQAYATGR GIQPQGVRVK
DVADFKVHTE DAGEGPLEVA VIAPDGREIP CTVRKTGAYL FDCNYTPQRA GLHQVHVRYG
GDHIMLSPFN VDVGPYKDSR IRAFGPGLSG GVVNKPAVFV VETNGETGAL GPSEARIDCT
DNGDGSATVA YWPTAPGEYA VHILCNDENI PKSPYMVPIE PDVGRCDPER VKVHGPGVQP
TGNVAGQPTE FTVDIRDAGE PVALKVRDNG DGTFTCNYTP KVPRKHTVLV SYGAVNVPRS
PFRVDVAEPS QPGKVRVFGP GVESVVRGQP THFTVDCKLA GQGNVGISIT DEMGRDVPMD
TQDMRDGTFR VAYTAHTPGP TYTVHVFFNN QEVPRSPFRV PVKPNVDMSR IHVENLSPMA
VDVGGVPVKG SPFRTQATPA PPVQEAVYPI VDTARQHAAI TPMSALEAAG LVRAYGDGLH
QATAGRPAHF TIDSRDAPPA PLSVTIEGPA EAKINYMDNG DGTCGVEYLP VEPGPYVVNV
LYKDTHIKGS PFPVRVVPPG REHVDVSRVH AYGPGLQPTG VLKESFAKFT VDAKPVDPQG
RGLVKAIVVS PTKQRTACIV KNNGDGTWSC SYSPIDEGEL KHMSVLSGLH HVEVTYDGAP
VNGSPFPVNV APGCDPSRVR AYGPGLEGGM THELQRFTVD LDGAGQGALG LALEGPADAQ
IQCHDNKDGT CTVDYLPTKA GMYDVFVKFN DMNIPGSPFA VPIRDKVDPS RVRCYGPGLE
PRGARAQQPA TFTVDASQAG DAPIHVATVD RLGRSTPAQV VPRPGQPNIY DVTYVPATEG
PCQIEVRQGT SHVARSPFTQ HVLPAYEPQR VRVTGEGVHP SRPLGLPATQ PTSFHVDTRE
AGMGDLELSV SDPEAQPLQL EVVDHGDGTY SCHYRPMVVG RHTVRVKFGG QEIPESPYLV
PVAPSGRADL CRIESGNDSR IPVGQECVIT VNTSQAGIGQ VTCRIMTPSG AQADVEIHEA
GNGRVNIYYT PPIRGDYLVE VRFGGDLVPN GRFNQRAVTA DELMPEVVVQ EERIQHVTTQ
SMHSSTLVTG YHPVDFKLPV GPTFSHVDGK EDCLVRTPSG RTMRPTLLDN GDGTVTAQFQ
PTEPGLHELE ITYNGQPIPG SPFRFYVEAV GSGNVTAYGP GLSYGRSGEP ADFTLVTKEA
GADLIQRSAV WPEGFPYITE FRLDVQIPPS KSIESGFINP ETSEPRRFNQ VCVGTTSEMP
LRITEADIYN LVATVRSPSG QEQPSTLKRL PNGHLGISFT PREIGEHYVN VFRNGRHIAN
SPFKIYVGES EIGNASRVRI YGNGLREGTA NQNCQFTVDT RNAGYGSLSL SIEGPSKADI
ECHDNHDGTC LVTYRPTEPG TYIINVRYAD QTVPGSPFVV QIGGEPSLRM MERITRQREL
ADVTHVGSQC ELNLKIPGIN IRDLVATVTS PTGVTQRCDV VALDDVNYTI RFVPQEMGVH
TVSVRNRGAH IPVWVVQFAF TSLYRLAGGD WAHMSGSVGM SFNAAGSPFQ FTVGAITDGG
AHKVHAAGPG LQQGLTYSPN DFSIYTREAG AGGLSIAIEG PSKAEIDFED RKDGSCGVSY
RVTEPGEYQC SIRFNDEHIP GSPYRVVINE SMERTFISPE MRQLSVATVQ DRGLMIGRPT
AFTVNYTGMT GNLRAYVVSP SGAHTDAFVH QVEVDQHAVR FTPSENGPHL VHVLMDERPI
PGSPFRVMVG QDDQGLVTAS GEGLTHGRVG ERNRFFVDTM QAGSGALSVT VDGPSKVQLN
CSERPNGYEF SYLPFLPGEY LINIKYGDMQ HIIGSPFKAY VTGDAMPEAY TVDSTHVVVE
TRASGVQHTM TESRPSRVVC TGTGLQQAYL NQTNTFTVNA TQAGHDVLYV GVSGPVVACE
EVNIKHLGQG QYAVNYVVRD RGRHLIMVKW GDQHVPGSPF VVNVL
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