ID A0A3Q0G763_ALLSI Unreviewed; 1781 AA.
AC A0A3Q0G763;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tight junction protein ZO-1 isoform X9 {ECO:0000313|RefSeq:XP_025055262.1};
GN Name=TJP1 {ECO:0000313|RefSeq:XP_025055262.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025055262.1};
RN [1] {ECO:0000313|RefSeq:XP_025055262.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_025055262.1; XM_025199477.1.
DR Proteomes; UP000189705; Unplaced.
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; cd12026; SH3_ZO-1; 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; IPR005417; ZO.
DR InterPro; IPR005418; ZO-1.
DR InterPro; IPR035597; ZO-1_SH3.
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 PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01598; ZONOCCLUDNS1.
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; PS50002; SH3; 1.
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:UP000189705};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 11..98
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 175..253
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 410..491
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 505..573
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 679..780
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1647..1781
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 102..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..853
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1781 AA; 199835 MW; F35B4D56E1F48E7F CRC64;
MEETAIWEQH TVTLHRAPGF GFGIAISGGR DNPHFQSGET SIVISDVLKG GPAEGLLQEN
DRVAMVNGVS MDNVEHAFAV QQLRKSGKNA KITIRRMKKV QIPVARPEPE PVSENEEDSF
DEEIQDPRSA RGGPGANRKH EKSWVRDRSA SRERSLSPRS DRRSIASSQP AKPTKVTLVK
SRKNEEYGLR LASHIFVKEI SQDSLAARDG NIQEGDVVLK INGTVTENMS LADAKTLIER
SKGKLKMVVQ RDERATLLNV PDLSDSIHSA NASERDDISE IQSLASDHSN RSHDRPRRSR
SRSPDQRSEP SDHSRHSPQQ PSNGSLRSRE DERVSKPGAI STPVKNADDI PLSKTMEEVV
VERNEKQTPP LPEPKPVYAQ AGQPDVDLPV SPSDGPLPSS THEDGMLRPS MKLVKFKKGD
SVGLRLAGGN DVGIFVAGVL EDSPAAKEGL EEGDQILRVN NVDFTNIIRE EAVLFLLDLP
KGEEVTILAQ KKKDVYRRIV ESDVGDSFYI RTHFEYEKES PYGLSFNKGE VFRVVDTLYN
GKLGSWLAIR IGKNHKEVER GIIPNKNRAE QLASVQYTLP KTAGGDRADF WRFRGLRSSK
RNLRKSREDL SAQPVQTKFP AYERVVLREA GFLRPVTIFG PIADVAREKL AREEPDIFQI
AKSEPRDAGT DQRSSGIIRL HTIKQIIDRD KHALLDVTPN AVDRLNYAQW YPIVVFLNPD
SKQGVKTMRT RLCPESRKSA RKLYERAHKL RKNNHHLFTT TINLNSMNDG WYGALKEAIQ
QQQNQLVWVS EGKADGATSD DLDLHDDRLS YLSAPGSEYS MYSTDSRHTS DYEDTDTEGG
AYTDQELDET LNDEVGTPPE SAITRSSEPV REDSSGMHHE AQAYPYVSQA QPQPNLRMDS
PGFKITASQP KAEASPAVPY LSPSPETNPA ISSTSVVNPN VNLTNVRLEE PTPPPYNSYQ
PQAGPLRTSS TEGAHIMLRD QEPSSLSPHI DPTKVYRKDP YINEEAAPRQ NYILKQPAVN
HPVHRQERES NLIYESQTQY TEKQPSREYE QSTYRYDSAN YSDQFARSYD PHLHYEDRVP
SYEDQWSYYD EKQPYQPRPP YDNQPPKDFD PRQNAEESTE RSYYPAQPRF EEPPPMTYDS
RPRYEHAPKN FIPQVRYEDQ PTTAYDIHGR YKPEAQTYPP VISRSPEPKQ YFEPHTRGYE
PGPPQGFNAK VGQYEPSHTT ANVPPPPPPS QTKPEILPSN SKPLPTPPTL TEEEEDPAMK
PQSVLTRVKM FENKRSLSVE KIKDSNDTPA VKPPELAPKP TLATVAKPAS QYEHDKTTYR
APEPQRPQAK PPEDIVRSNH YDPEEDEEYY RKQLSYFDRR SFENKPSAQI PASHHPEPAK
PVHPQLNFTN YSSKFLGSYT SYDYLKRNIK WGKPTDTEPM DRPVGEKRYE PVPQVTSAVP
PPPPVQYTQP QSINNPALSL QAHHKPALSE VNSVSVDFQN STVSKPDPPP PQNKPAILRS
SNREDTVQST FYPQKSFPDK GPLNGSEQTQ KPVTPAYNRF TTKPYTSAAR PFERKFESPK
FNHNLLPNET QHKPELPSKS PNSPQPILKA HGSLQPSEFD SGMDTFSIQA DKPKYQPNNV
NAVPKAIPVS PSALEDDEEE DGHTVVATAR GVFNSNGGVL SSIETGVSII IPQGAIPEGI
EQEIYFKVCR DNSILPPLDK EKGETLLSPL VMCGPHGLKF LKPVELRLPH CASMTPDGWS
FALKSSDSSS GDPKTWQNKS LPGDPNYLVG ANCVSVLIDH F
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