ID A0A0V0VJY8_9BILA Unreviewed; 1587 AA.
AC A0A0V0VJY8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tight junction protein ZO-1 {ECO:0000313|EMBL:KRX63469.1};
DE Flags: Fragment;
GN ORFNames=T09_12913 {ECO:0000313|EMBL:KRX63469.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX63469.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX63469.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX63469.1};
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, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. 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 -!- 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:KRX63469.1}.
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DR EMBL; JYDN01000031; KRX63469.1; -; Genomic_DNA.
DR STRING; 181606.A0A0V0VJY8; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00992; PDZ_signaling; 3.
DR CDD; cd11859; SH3_ZO; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 2.60.220.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR13865:SF28; POLYCHAETOID, ISOFORM O; 1.
DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS51145; ZU5; 1.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Signal {ECO:0000256|SAM:SignalP};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006870907"
FT DOMAIN 107..194
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 206..284
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 446..525
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 723..825
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1447..1565
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 327..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX63469.1"
SQ SEQUENCE 1587 AA; 174096 MW; 66ACE5CB9C0386F0 CRC64;
LKMLMFDVIF NFILFFSRTS PNKVKVDCMA SSPSDVISGL GENRPDGTAA IELHKENSKD
RPPSTSNAEL IRSCSYEVPM GKNSSNEILV EPVDEEDCDH TTWIYHSVNL KKVQGYGFGI
AVSGGRDNPH FKSGDPSIAI SDVLRSGPAW GLLQINDRIV YVNGVNLENA DHSTAIQIMK
DSENLNVIVK RRIPFPVLEY DQRTLKFTLT KSRRKDDFGI VLGCKFFIKD IANRRLAEKD
PGLKEGDVVL KINGENCDQM TLSEARRLLD RSKDRLSLVI QRDVPRGANW KWSSQATLYE
RIGGTDTPRQ SPTPRHSPMV YVRNADHDAS SARSHFPSRY HDRFSRPPSE DRTVSPKRQS
TCSQQSFGSR GPPQNQYFYD DGGSNVFTCQ SPSRTISPSC ESSHASVNCA TMDQQLLAPH
QKPPLPSTMQ VSFHCHLLLV TNEPRLITFR KESGSVGVRV IGGNEVGIFV SAVQSDSPAA
VRGVRPGDKI LRVNNKSMLG VTREEAVLHL LGLQDHVELF LQYKKDEYER IRSQNIGDNF
FIRTHFTYGK PENGELSFKK GDIFQVIDTL YGGTVGSWQA ICVSSPSMSS TRSDYVHPKG
VIPNSSRAEQ LAHAERSQSQ SQATAEMKSS TLLRRKVTMS RRSKSLTKSH WDEVVFSHGT
VHFAAYERVQ LRHPGFLRPV VIYGSLADVA REKLLRDFPL AFLSSQVENG NDDSDPGKTN
RIVRLNAIRD VMNKNKHCIL DITPSSVEKL IYAQYCPIVI FVNVGSRTRL RDMRKRLAKT
SAVKSSKKLF DQSQKIQKLY SHLFTAVIDA THEEKWFEVL RDLIAHLQSR RVWMSESKPS
ELLDDDFLFP MSNGRYGSVG GGDSDVDSLA DESRCDLSSK RDATVALTAV DAASRMDVPY
ADNSSSSSYA MASGTLRSPT KSHAHMCDRQ SSGSNVDMIA SMYENRDNIV ALMATMRRKP
PPLARKPKPP PPPRIGSSNA SLTSDVQCTV DLAAASADLP RIAESTVSVA PSAACNGSTT
LMQTSFSPAT HVDNSRLLTK IDEREFVPYS PRYGRPVADC GLYNVKQILE GTMDNYDSGV
SAPAASSRLM HSSSSALGHP VTGGKPNLTE SMSLSYYDNT ERARLDYSAS LGLNSHGAAW
QNYEHPSSYV SAHSNSQFQH FFDGHRVCPV SPTSSGSMAA AMRSVNGIYG SRSSHDSYAQ
HVSEGYLLAG NASSKRPPLV PHRSPVPPPA PRSTYTPSTP RHSQSMPPSM SSCGSRVLTS
EDEDQQQQQH HHHHQFGRIS SPSLGNRSQP QPIPLARSSL TKAHATTPSA AAARMSDPSS
VHLPKSDAGA AVSSEMQAIG VNRAAAVRCD EGRGRFEISA LDMSSGEAVK SRNNSDDDGN
EFETPQACTK QQAVVIGGGG DDNDDDDNGG QPVSDVSGSK KKQQCGSSEE NGLGTVASDA
DLFICRSSAS ATVDHTGATL QLQDPGVRLT IPQAALSSPV EMFVQLMTRE LEPRTSNGAF
PSEEASSFKE KSRFVIVAGP SGLKFSVPVE LCLPKSALND GKQWFLAFKS KNTDHFGQRR
CLNLLDSCAF PKKNVDPDQV AFFISNF
//
