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Database: UniProt
Entry: A0A0V1BS04_TRISP
LinkDB: A0A0V1BS04_TRISP
Original site: A0A0V1BS04_TRISP 
ID   A0A0V1BS04_TRISP        Unreviewed;      1555 AA.
AC   A0A0V1BS04;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Tight junction protein ZO-1 {ECO:0000313|EMBL:KRY39633.1};
GN   Name=TJP1 {ECO:0000313|EMBL:KRY39633.1};
GN   ORFNames=T01_5153 {ECO:0000313|EMBL:KRY39633.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY39633.1, ECO:0000313|Proteomes:UP000054776};
RN   [1] {ECO:0000313|EMBL:KRY39633.1, ECO:0000313|Proteomes:UP000054776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS3 {ECO:0000313|EMBL:KRY39633.1};
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:KRY39633.1}.
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DR   EMBL; JYDH01000017; KRY39633.1; -; Genomic_DNA.
DR   Proteomes; UP000054776; 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   SMART; SM00218; ZU5; 1.
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:UP000054776};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT   DOMAIN          79..166
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          178..256
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          418..497
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          700..802
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   DOMAIN          1415..1533
FT                   /note="ZU5"
FT                   /evidence="ECO:0000259|PROSITE:PS51145"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1186..1306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1332..1401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1212
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1378..1401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1555 AA;  170330 MW;  6857BCF53AA83F98 CRC64;
     MASSPSDVIS GLGENRPDGT AAIELHKENS KDRPPSTSNA ELIRSCSYEV PMGKNSSNEI
     LVEPVDEEDC DHTTWIYHSV NLTKVQGYGF GIAVSGGRDN PHFKSGDPSI AISDVLRSGP
     AWGLLQINDR IVYVNGVNLE NADHSTAIQI MKDSENLNVI VKRRIPFPVL EYDQRTLKFT
     LTKSRRKDDF GIVLGCKFFI KDIANRRLAE KDPGLKEGDV VLKINGENCD QMTLSEARRL
     LDRSKDRLSL VIQRDVPRGA NWKWSSQATL YERIGGTDTP RQSPTPRHSP MVYVRNADHD
     ASSARSHFPS RYHDRFSRPP SEDRTVSPKR QSTCSQQSFG SRGPPQNQYF YDDGGSNVFT
     CQSPSRTISP SCESSHASVN CATMDQQLLA PHQKPPLPST MQVLFHCHLL LVTNEPRLIT
     FRKESGSVGV RVIGGNEVGI FVSAVQSDSP AAVRGVRPGD KILRVNNKSM LGVTREEAVL
     HLLGLQDHVE LFLQYKKDEY ERIRSQNIGD NFFIRSGLIV THFTYEKPEN GELSFKKGDI
     FQVIDTLYGG TVGSWQAICV SSPSMSSTRS DYVHPKGVIP NSSRAEQLAH AERSQSQSQA
     TAEMKSSTLL RRKVTMSRRS KSLTKSHWDE VVFSHGTVHF AAYERVQLRH PGFLRPVVIY
     GSLADVAREK LLRDFPLAFL SSQVENGNDD SDPGKTNRIV RLNAIRDVMN KNKHCILDIT
     PSSVEKLIYA QYCPIVIFVN VGSRTRLRDM RKRLAKTSAV KSSKKLFDQS QKIQKLYSHL
     FTAVIDATHE EKWFEVLRDL IAHLQSRRVW MSESKPSELL DDDFLFPMSN GRYGSVGGGD
     SDVDSLADES RCDLTSKRDA TVALTTVDAA SRMDVPYADN SSSSSYAMAS GTLRSPTKTH
     AHMCDRQSSG SNVDMIASMY ENRDNIVALM ATMRRKPPPL ARKPKPPPPP RIGSSNASLT
     SDVQCTVDLA AASADLPRIA ESAVSVSPSA ACNGSTTLMQ TSFSPATHVD NSRLLTKIDE
     REFVPYSPRY GRPVADCGLY NVKQILEGTM DNYDSGVSAP TASSRLMHSS SSALGHPVTG
     GKPNLTESMS LSYYDNTERA RLDYSASLGL NSHGAAWQNY EHPSSYASAH SNSQFQHFFD
     GHRVCPVSPT SSGSMAAAMR SVNGIYGSRS SHDSYAQHVS EGYLLAGSAG SKRPPLVPHR
     SPVPPPAPRS TYTPSTPRHS QSMPPSMSSC GSRVLTSEDE DQQQQQQHQH HQFGRISSPS
     LGNRSQPQPI PLARSSLTKA HTTTPSAAAA RMSDPSSVHL PKSDAGAAVS SEMQAIGVNR
     TAAVRCDEAL DMSSGEAVKS RNSSDDDGNE FETPQACTKQ QAVVIGGGDD NDDDDSGGQP
     VSDVSGSKKK QQCGSSEENG LGTVASDADL FICRSSASAT VDHTGATLQL QDPGVRLIIP
     QAALSSPVEM FVQLMTRELE PRTSNGAFPS EEASSFKEKS RFVIVAGPSG LKFSVPVELC
     LPKSALNDGK QWFLAFKSKN TDHFGQRRCL NLLDSCAFPK KNVDPDQVAF FISNF
//
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