ID A0A0V1MNC4_9BILA Unreviewed; 1692 AA.
AC A0A0V1MNC4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Tight junction protein ZO-1 {ECO:0000313|EMBL:KRZ73277.1};
DE Flags: Fragment;
GN Name=TJP1 {ECO:0000313|EMBL:KRZ73277.1};
GN ORFNames=T10_9357 {ECO:0000313|EMBL:KRZ73277.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ73277.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ73277.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ73277.1};
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:KRZ73277.1}.
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DR EMBL; JYDO01000066; KRZ73277.1; -; Genomic_DNA.
DR STRING; 268474.A0A0V1MNC4; -.
DR Proteomes; UP000054843; 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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 195..281
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 293..371
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 534..613
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 811..913
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1551..1692
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 92..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ73277.1"
SQ SEQUENCE 1692 AA; 186646 MW; 825A9951E7DD57D9 CRC64;
LNRSSSGVRT FFFQRCSYCD CCTDNKNCSS SLNVSVLSNR WTILICECLF AWVIILLTPF
FYTVVDCMAN TPSDVISGLA ENRPDGTAAV ELHNDNTSKD RPPSTSNAEL TGSSYEVPMG
KNSSNEILVE PVDEEDCDHT TWIYHSVNLK KKFKAALRAR VVSLTLHICL LAYCDDLFFN
FIFKNIFSPL FSHLVVDFQV QGYGFGIAVS GGRDNPHFKS GDPSIAISDV LRSGPAWGLL
QINDRIVYVN GVNLENADHS TAIQIMKDSE NLNVIVKRRI PFPVLEYDQR TLKFTLTKSR
RKDDFGIVLG CKFFIKDITN RRLAEKDPGL KEGDVVLKIN GENCDQMTLN EARRLLDRSK
DRLSLVIQRD VPRGANWKWS SQATLYERIG GTDTPRQSPT PRHSPMVYVR NADHDTSSAR
SHFPSRYHDR YSRPPSEDRT VSPKRQSTCS QQSFGSRGPS QNQYFYDDGA SNVFPCQSPS
RTISPSCDSS HASVNCATMD QQLLAHQKPP LPSTMQVYYT VPFYYFDHLN EPRLITFRKE
SGSVGVRVIG GNEVGIFVSA VQSDSPAAVR GVRPGDKILR VNNKSMLGVT REEAVLHLLG
LQDHVELFLQ YKKDEYERIR NQNIGDNFFI RTHFTYGKPE NGELSFKKGD IFQVIDTLYG
GTVGSWQAIC VSSPSMASTR SDYVHPKGVI PNSSRAEQLA HAERSQSQSQ VNTEMKSSTL
LRRKVTMGRR SKSLTKSHWD EVVFSHGTVH FAAYERVQLR HPGFLRPVVI YGSLADVARE
KLLRDFPLAF LSSQVENGND ESDPGKTNRI VRLNAIRDVM NKNKHCILDI TPSSVEKLIY
AQYCPIVIFV NVGNRTRLRD LRKRLAKTSA VKSSKKLFEQ SQKIQKLYSH LFTAVIDATH
EEKWFEVLRD LIAHLQSRRV WMSESKPSEL LDDDFLFPMS NGRYGSVGGG DSDVDSIADE
PRCDLSSKRD AAVALTAVDA ASRMDVPYAD NSSSSSYAMA SGTLRSPTKT HAHMCDRQSS
GSNVDMIASM YENRDNIVAL MATMRRKPPP LARKPKPPPP PRIGSSNASL TSDMQCTVDL
AAPSADLPRI AESAVSVAPS AACNGSTTLM QTSFSAATHA DNSRLLTKID EREFVPYSPR
YGRPVADCGL YNVKQILEGT MDNYDSGISA PMASSRLMHS SSSALGHPMT GKPNLTESMS
LSYYENTERA RLDYSASLGL NSHGAAWQNY DHPSSYVSAH SNNSQFQHFF DGHRYSCKNC
LSLSIFCTNK QTDVDCIFRV CPVSPTSSGS MAATMRSVNG GIYGSRSSHD SYAQHVSEGY
LLAGNGSKRP PMVPHRSPVP PPAPRSTYTP STPRHSQSVP PSMSSCGSRV LNSEDDDQQQ
HQFGRINSPS LGRSQPQPIP LARSSLTKAH TTTASVAAST RMSDSSSVHL SKSDAGAGAA
VGCDLQPNNV NRAAAVRCDE ALDMSSGEAV KSKSNNSDDD GNEFETQTCT KQVAVGDDGD
DDDHHDDDHS GHPVSDVSGS KKKQQCGSSF FEEENELGTI ASDADLFICR SSASATVDHS
GATLQLQDAG VRLIIPQAAL SSPVEMFVQL MTRELEPRTS NGAFPSDEAS SFKEKNCFVI
VAGPSGLKFS VPVEICLPKS ALNDGKQWFL AFKSSKNADY FGQRRCLNLL DSCAFPKKNV
DPDQVAFSIS NF
//
