ID A0A0V1N126_9BILA Unreviewed; 1092 AA.
AC A0A0V1N126;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Filamin-A {ECO:0000313|EMBL:KRZ77599.1};
DE Flags: Fragment;
GN Name=cher {ECO:0000313|EMBL:KRZ77599.1};
GN ORFNames=T10_3355 {ECO:0000313|EMBL:KRZ77599.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77599.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ77599.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77599.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the filamin family.
CC {ECO:0000256|ARBA:ARBA00009238}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ77599.1}.
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DR EMBL; JYDO01000018; KRZ77599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1N126; -.
DR STRING; 268474.A0A0V1N126; -.
DR Proteomes; UP000054843; 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; cd21230; CH_FLN_rpt2; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
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; 8.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 8.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF81296; E set domains; 8.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 8.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1092
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006883029"
FT DOMAIN 49..155
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 178..281
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REPEAT 312..403
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 405..505
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 505..596
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 605..696
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 697..793
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 794..891
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 892..984
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 985..1083
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ77599.1"
SQ SEQUENCE 1092 AA; 121122 MW; 5351DFE6B41B331D CRC64;
LLLLITNFFF HFCIFVHISN VNIIKYHIMV YEEMDFVAIQ SRDKAKWKTI QQNTFTRWVN
ERLKAVDCSV NNLETDLTNG LLLIRLLEVL SKKKLPRYNK KPNFRSQRLE NVSVALTFLE
TVEGIKLVNI DSSDIVDGRL KLILGLIWTL ILHYSIDAQI WDNERNRQNQ ENKHKLQLPP
KQRLLDWLNS KIPGFHLTNL TTQWSDGRPL GALVDSLAPG LCPEWSMWKA ANALKNTTIA
MDLAEKWLVI PKLIEPEEFI NPNVDEMSMM TYLSQYPNAK LQPGAPIGSS VIEKSDSNKL
EYPVAKMKRI LQIKASGPGL QSGVISGKTT HFDIYMAGGD EKKFAIQILN PSGKSDSVNQ
RFRRLSGDML RCEYTPEMVG MHTINIFYDD HSVLNNNPYE VWVASGSFDP TEWKVFGRGI
QNSGIRVGDK VDVRILCNGG DADASLVEMI VKHSDGTIVP IHRKNSSIRP LKVEGIYQPT
HAGVHIVHIK YDGKDFPSSP FEVMVDSEMT SKIRAFGPGL QSGVVNRPCK FTVETNGERC
GLGFSVDGPS KAELTCHDNG DGSAEICYIP KACGEYAIHV LSNDVNISGS PYMVEIGESH
LGCIPELVKC SGAGISEYGH VCGQRSTFTV DASRAGDSAV KIFAMDSDGM EMNIQQKTIA
NNVYSCSFVP ESCKRHWIMV TFDGQSVPGS PFKIHVSEQT NPNLVRMYGP GLEESVRTKD
RNHFFVDCAD AGPGKVEVCM KNHADGMPVD VQISDCGNGS YTVYYKVNKP GQYDIYVRFA
GSLIPGMPYK VQVKPHIDLS NVVIRGLEER VFINSISEFI VDTTALTKKI GDAEVSCTIR
SPDGNMARCH IINEKDGTYR IFYSTIVEGK HELQVSYDDI PLTAQPLLVH AVDGHDETRC
KVQGAGLKSG LVGIPCRFRV DTKGAGSGKL NIAIEGPSES TISTADNLDG SCTVEYVVSK
AGVYKISVTF AEKHIPGSPF TALIEPPLDP NLVRAWGPGL EPKNCRFDLP LQFLVDTTRS
GPAQLQVLVD SECGAAPKQP EIVEQAHGVY KVTYYAPAVD SNCKVHILYG GKEIPNRLAN
IYTYIYIHLC IY
//
