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Database: UniProt
Entry: A0A0V1PNC7_9BILA
LinkDB: A0A0V1PNC7_9BILA
Original site: A0A0V1PNC7_9BILA 
ID   A0A0V1PNC7_9BILA        Unreviewed;      1397 AA.
AC   A0A0V1PNC7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=Vinculin {ECO:0000256|ARBA:ARBA00014125};
GN   ORFNames=T08_742 {ECO:0000313|EMBL:KRZ97673.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ97673.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ97673.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ97673.1};
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   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004413}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC       {ECO:0000256|ARBA:ARBA00008376}.
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:KRZ97673.1}.
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DR   EMBL; JYDM01000002; KRZ97673.1; -; Genomic_DNA.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5.
DR   Gene3D; 1.20.120.810; Vinculin, Vh2 four-helix bundle; 2.
DR   InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR   InterPro; IPR017997; Vinculin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   PANTHER; PTHR46180; VINCULIN; 1.
DR   PANTHER; PTHR46180:SF1; VINCULIN; 1.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00806; VINCULIN.
DR   SUPFAM; SSF47220; alpha-catenin/vinculin-like; 6.
DR   PROSITE; PS00664; VINCULIN_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REGION          602..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1143..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          527..554
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        610..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1190
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1397 AA;  155899 MW;  05B6BC4B59E6B467 CRC64;
     MPVFHTKTIE SILEPVAQQL ILLVGFVSNG STTAGRAFRH VFFGIQTCRK LADAHVDMYN
     MQKSTLQQQS SNNRNGIRST LINRKQYPLR QRKYELVILV INLSDRVSRL VILHEEAEDG
     NAMPDLTRPV DAVSRAVENL VQVGYDTIHL SDDDILKQDM PPALQRVETS SRLLEEACYV
     LRDDPYSSQG RKKLIEGSRG ILQGTSALLL CFDESEVRKI VRGCKKVLDY LAVAEVIENM
     EDLVQFVRDI SPWLTKMSRD TEAREKELTH HVHREILIRC IDSVKTLAPI LICAMKIFIQ
     ISAQGGSKGV PEAAENRNYL SSRMIEEVNE VIRVLQLTTY DEDEWNEDDL IVMKKALSAI
     ESLLQAALDW LADPRALRGG VGEKSLRRIL VYAERIADRA LPEDASLIRR ACSDIASMTD
     SLCELRHNKQ GDSPQCQGLA RGIAQKLREL VGGKDIAGLL PHALQGLEQA GIAQPAHTVL
     GRMDQVLKWL DAPYMDDRGV GLNALKALLA EGRKVADLCS PREKYAMNEL CDEIERLSHQ
     LAELQRKGMG YEKRRRVSSS DRAEWAFARP LARRPAPDTF IQPSQSRRWS IKSAGESLSA
     GRPYSSVGAA KKRTTPTCQA GSLPRSSTMP LASEPFQSLN LLLQRLVTEL WRNKRTCAFQ
     TPTTTAKSTA PARPSTTVPH FHVCKAFLYN PYRGAAAGPA ESSSSSPPRR VFFETESLLA
     PLVVRIGDSP QARAIANQLK DKLGELKRMM DRALLDRVVD DFSDITTPLK QFAEAVLAPE
     GTPARDANFA EKAQNLRDHC QRCAKTGRLV GTSGPCKDKK IVEALCSTAN QISNMTPQVI
     NAGKIRFHYP QNVSADEHFE NLRRELSDAL QRLRSLVDDA VDPLEFVKAS ENAIRRHGQE
     CENAISNDEP QKMADHASSI ARLANRVLMA AKGQAENSED PAFSGRMNDA ASRLQGTIPP
     MVNDAKQVAL NPRDQSAAGR WRDSNKKLVD AVGSVRRALE PSQLPEMKNL DINGRVAVLV
     GLCCAGMTVG TKGGARSSSR VCKVSSPLSV DVGYESDTAA PVSWSRPMRS KDVVDFDYPN
     IDFHSMFDMW LYQMPPVNLS SLYDLRRLPT LFHRRSASPR RRRRNRHRRC LTLSFPVDWE
     REQRTGRRRE VRAPPPPPAW YQAASHREGP ASPNRPPPQL MEMRTPPRPP PPQETDDEEE
     MRAFWERVPL PKANQPILSA AHSLHREVQQ WSSRENEIVA AAKRMAILMA RLSQLVRGEG
     GTKKDLIDCA KAIADASEEV TRLAVLLARQ CTDIKMRKAL LQVCERIPTI ATQLKILSTV
     KATMLGSQAP MSVREGSEIS PGTDEDEEAM QQLVLNAQNL MQSVKDTVRA AEAASIKIRT
     DSGLRLRWVR KPVWANY
//
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