ZO1_MOUSE
ID ZO1_MOUSE Reviewed; 1745 AA.
AC P39447; E9QK00;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Tight junction protein ZO-1;
DE AltName: Full=Tight junction protein 1;
DE AltName: Full=Zona occludens protein 1;
DE AltName: Full=Zonula occludens protein 1;
GN Name=Tjp1; Synonyms=Zo1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129;
RX PubMed=8486731; DOI=10.1083/jcb.121.3.491;
RA Itoh M., Nagafuchi A., Yonemura S., Yasuda-Kitani T., Tsukita S.,
RA Tsukita S.;
RT "The 220-kD protein colocalizing with cadherins in non-epithelial cells is
RT identical to ZO-1, a tight junction-associated protein in epithelial cells:
RT cDNA cloning and immunoelectron microscopy.";
RL J. Cell Biol. 121:491-502(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=3528172; DOI=10.1083/jcb.103.3.755;
RA Stevenson B.R., Siliciano J.D., Mooseker M.S., Goodenough D.A.;
RT "Identification of ZO-1: a high molecular weight polypeptide associated
RT with the tight junction (zonula occludens) in a variety of epithelia.";
RL J. Cell Biol. 103:755-766(1986).
RN [4]
RP INTERACTION WITH CLAUDINS, AND SUBCELLULAR LOCATION.
RX PubMed=10601346; DOI=10.1083/jcb.147.6.1351;
RA Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.;
RT "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and
RT ZO-3, with the COOH termini of claudins.";
RL J. Cell Biol. 147:1351-1363(1999).
RN [5]
RP INTERACTION WITH KIRREL1.
RC STRAIN=Swiss Webster; TISSUE=Brain;
RX PubMed=12424224; DOI=10.1096/fj.02-0242fje;
RA Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G.;
RT "NEPH1 defines a novel family of podocin interacting proteins.";
RL FASEB J. 17:115-117(2003).
RN [6]
RP INTERACTION WITH GJA12, AND DOMAIN.
RX PubMed=15183511; DOI=10.1016/j.neuroscience.2004.03.063;
RA Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M.,
RA Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.;
RT "Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes
RT and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain.";
RL Neuroscience 126:611-630(2004).
RN [7]
RP INTERACTION WITH BVES.
RX PubMed=16188940; DOI=10.1242/jcs.02588;
RA Osler M.E., Chang M.S., Bader D.M.;
RT "Bves modulates epithelial integrity through an interaction at the tight
RT junction.";
RL J. Cell Sci. 118:4667-4678(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1139 AND TYR-1353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-241; SER-277;
RP SER-280; SER-284; SER-294; SER-323; SER-353; SER-617; SER-810; SER-821;
RP TYR-822; SER-824; THR-848; THR-868; SER-912; SER-1071; SER-1138 AND
RP SER-1542, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP INTERACTION WITH MYZAP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20093627; DOI=10.1161/circresaha.109.213256;
RA Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R.,
RA Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A.,
RA Olson E.N., Frey N.;
RT "Myozap, a novel intercalated disc protein, activates serum response
RT factor-dependent signaling and is required to maintain cardiac function in
RT vivo.";
RL Circ. Res. 106:880-890(2010).
RN [16]
RP INTERACTION WITH DLL1.
RX PubMed=24715457; DOI=10.1242/dev.102988;
RA Hatakeyama J., Wakamatsu Y., Nagafuchi A., Kageyama R., Shigemoto R.,
RA Shimamura K.;
RT "Cadherin-based adhesions in the apical endfoot are required for active
RT Notch signaling to control neurogenesis in vertebrates.";
RL Development 141:1671-1682(2014).
RN [17]
RP INTERACTION WITH USP53.
RX PubMed=26609154; DOI=10.1523/jneurosci.1965-15.2015;
RA Kazmierczak M., Harris S.L., Kazmierczak P., Shah P., Starovoytov V.,
RA Ohlemiller K.K., Schwander M.;
RT "Progressive hearing loss in mice carrying a mutation in usp53.";
RL J. Neurosci. 35:15582-15598(2015).
RN [18]
RP STRUCTURE BY NMR OF 18-110.
RX PubMed=21431884; DOI=10.1007/s12104-011-9301-x;
RA Umetsu Y., Goda N., Taniguchi R., Satomura K., Ikegami T., Furuse M.,
RA Hiroaki H.;
RT "(1)H, (13)C, and (15)N resonance assignment of the first PDZ domain of
RT mouse ZO-1.";
RL Biomol. NMR. Assign. 5:207-210(2011).
CC -!- FUNCTION: Tjp1, TjpP2, and Tjp3 are closely related scaffolding
CC proteins that link tight junction (TJ) transmembrane proteins such as
CC claudins, junctional adhesion molecules, and occludin to the actin
CC cytoskeleton (By similarity). The tight junction acts to limit movement
CC of substances through the paracellular space and as a boundary between
CC the compositionally distinct apical and basolateral plasma membrane
CC domains of epithelial and endothelial cells. Necessary for
CC lumenogenesis, and particularly efficient epithelial polarization and
CC barrier formation (By similarity). Plays a role in the regulation of
CC cell migration by targeting Cdc42bpb to the leading edge of migrating
CC cells (By similarity). Plays an important role in podosome formation
CC and associated function, thus regulating cell adhesion and matrix
CC remodeling (By similarity). With Tjp2 and TJjp3, participates in the
CC junctional retention and stability of the transcription factor Dbpa,
CC but is not involved in its shuttling to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:O97758, ECO:0000250|UniProtKB:Q07157}.
CC -!- SUBUNIT: Homodimer, and heterodimer with TJP2 and TJP3. Interacts with
CC OCLN, CALM, claudins, CGN/cingulin, CXADR, GJD3 and UBN1
CC (PubMed:10601346). Interacts (via ZU5 domain) with CDC42BPB (By
CC similarity). Interacts (via PDZ domain) with GJA1 (By similarity).
CC Interacts (via PDZ domains) with ANKRD2 (By similarity). Interacts with
CC BVES (via the C-terminus cytoplasmic tail) (PubMed:16188940). Interacts
CC with GJA12 and KIRREL1 (PubMed:12424224, PubMed:15183511). Interacts
CC with HSPA4 (By similarity). Interacts (via ZU5 domain) with MYZAP
CC (PubMed:20093627). Interacts with DLL1 (PubMed:24715457). Interacts
CC with USP53 (via the C-terminal region) (PubMed:26609154). Interacts
CC with DNMBP (via C-terminal domain); required for the apical cell-cell
CC junction localization of DNMBP (By similarity). Interacts with SPEF1
CC (By similarity). {ECO:0000250|UniProtKB:O97758,
CC ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:10601346,
CC ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:15183511,
CC ECO:0000269|PubMed:16188940, ECO:0000269|PubMed:20093627,
CC ECO:0000269|PubMed:24715457, ECO:0000269|PubMed:26609154}.
CC -!- INTERACTION:
CC P39447; P57780: Actn4; NbExp=6; IntAct=EBI-79508, EBI-445071;
CC P39447; P23242: Gja1; NbExp=4; IntAct=EBI-79508, EBI-298630;
CC P39447; P70689: Gjb6; NbExp=3; IntAct=EBI-79508, EBI-2615416;
CC P39447; Q64727: Vcl; NbExp=8; IntAct=EBI-79508, EBI-432047;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07157};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q07157}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q07157}. Cell junction, tight junction
CC {ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:3528172}. Cell
CC junction, gap junction {ECO:0000269|PubMed:20093627}. Cytoplasm,
CC myofibril, sarcomere, I band {ECO:0000269|PubMed:20093627}. Note=Moves
CC from the cytoplasm to the cell membrane concurrently with cell-cell
CC contact (By similarity). Detected at the leading edge of migrating and
CC wounded cells (By similarity). Colocalizes with SPEF1 at sites of cell-
CC cell contact in intestinal epithelial cells (By similarity).
CC {ECO:0000250|UniProtKB:Q07157}.
CC -!- DOMAIN: The 244-aa domain between residues 633 and 876 is the primary
CC occludin (Ocln)-binding site and is required for stable association
CC with the tight junction (By similarity).
CC {ECO:0000250|UniProtKB:Q07157}.
CC -!- DOMAIN: The C-terminal region (residues 1151-1372) is an actin-binding
CC region (ABR) that interacts directly with F-actin and plays an
CC important role in the localization of Tjp1 at junctions (By
CC similarity). The ABR is also required for the localization to puncta at
CC the free edge of cells before initiation of cell-cell contact (By
CC similarity). The ABR is also necessary for Tjp1 recruitment to
CC podosomes (By similarity). {ECO:0000250|UniProtKB:Q07157}.
CC -!- DOMAIN: The second PDZ domain (PDZ2) mediates homodimerization and
CC heterodimerization with Tjp2 and Tjp3 (By similarity). PDZ2 domain also
CC mediates interaction with Gja12 (PubMed:15183511).
CC {ECO:0000250|UniProtKB:Q07157, ECO:0000269|PubMed:15183511}.
CC -!- PTM: Phosphorylated at tyrosine redidues in response to epidermal
CC growth factor (EGF) (By similarity). This response is dependent on an
CC intact actin microfilament system (By similarity). Dephosphorylated by
CC PTPRJ (By similarity). {ECO:0000250|UniProtKB:Q07157}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; D14340; BAA03274.1; -; mRNA.
DR EMBL; AC122222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS21338.1; -.
DR PIR; A46431; A46431.
DR RefSeq; NP_033412.2; NM_009386.2.
DR PDB; 2RRM; NMR; -; A=18-110.
DR PDBsum; 2RRM; -.
DR AlphaFoldDB; P39447; -.
DR BMRB; P39447; -.
DR SMR; P39447; -.
DR BioGRID; 204209; 29.
DR DIP; DIP-30946N; -.
DR IntAct; P39447; 20.
DR MINT; P39447; -.
DR STRING; 10090.ENSMUSP00000099652; -.
DR iPTMnet; P39447; -.
DR PhosphoSitePlus; P39447; -.
DR jPOST; P39447; -.
DR MaxQB; P39447; -.
DR PaxDb; P39447; -.
DR PeptideAtlas; P39447; -.
DR PRIDE; P39447; -.
DR ProteomicsDB; 275155; -.
DR Antibodypedia; 783; 448 antibodies from 41 providers.
DR DNASU; 21872; -.
DR Ensembl; ENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.
DR GeneID; 21872; -.
DR KEGG; mmu:21872; -.
DR UCSC; uc009hgp.2; mouse.
DR CTD; 7082; -.
DR MGI; MGI:98759; Tjp1.
DR VEuPathDB; HostDB:ENSMUSG00000030516; -.
DR eggNOG; KOG3580; Eukaryota.
DR GeneTree; ENSGT00940000155164; -.
DR InParanoid; P39447; -.
DR OMA; DQILRXY; -.
DR OrthoDB; 1175136at2759; -.
DR PhylomeDB; P39447; -.
DR TreeFam; TF315957; -.
DR Reactome; R-MMU-191650; Regulation of gap junction activity.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR BioGRID-ORCS; 21872; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Tjp1; mouse.
DR EvolutionaryTrace; P39447; -.
DR PRO; PR:P39447; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P39447; protein.
DR Bgee; ENSMUSG00000030516; Expressed in brain blood vessel and 270 other tissues.
DR ExpressionAtlas; P39447; baseline and differential.
DR Genevisible; P39447; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005921; C:gap junction; ISS:UniProtKB.
DR GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0071253; F:connexin binding; IPI:CAFA.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0034334; P:adherens junction maintenance; ISO:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:MGI.
DR GO; GO:2000250; P:negative regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:ARUK-UCL.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:ARUK-UCL.
DR GO; GO:0071896; P:protein localization to adherens junction; ISO:MGI.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:MGI.
DR GO; GO:0150105; P:protein localization to cell-cell junction; IMP:ARUK-UCL.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:1901888; P:regulation of cell junction assembly; ISO:MGI.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071000; P:response to magnetism; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR CDD; cd12026; SH3_ZO-1; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 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:SF25; PTHR13865:SF25; 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Cell junction; Cell membrane; Cytoplasm;
KW Gap junction; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain; Tight junction.
FT CHAIN 1..1745
FT /note="Tight junction protein ZO-1"
FT /id="PRO_0000094541"
FT DOMAIN 23..110
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 186..264
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 421..502
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 516..584
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 610..791
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 1631..1745
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT REGION 102..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..876
FT /note="Occludin (OCLN)-binding region"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT REGION 825..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1370
FT /note="Actin-binding region (ABR)"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT COMPBIAS 134..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..864
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 809
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 846
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0A0G2K2P5"
FT MOD_RES 848
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 854
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 868
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 1164
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 1353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07157"
FT CONFLICT 202
FT /note="L -> P (in Ref. 1; BAA03274)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="N -> D (in Ref. 1; BAA03274)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="P -> L (in Ref. 1; BAA03274)"
FT /evidence="ECO:0000305"
FT CONFLICT 985
FT /note="V -> G (in Ref. 1; BAA03274)"
FT /evidence="ECO:0000305"
FT CONFLICT 1237
FT /note="P -> R (in Ref. 1; BAA03274)"
FT /evidence="ECO:0000305"
FT CONFLICT 1395
FT /note="S -> P (in Ref. 1; BAA03274)"
FT /evidence="ECO:0000305"
FT CONFLICT 1584
FT /note="D -> G (in Ref. 1; BAA03274)"
FT /evidence="ECO:0000305"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:2RRM"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2RRM"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2RRM"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2RRM"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2RRM"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2RRM"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:2RRM"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2RRM"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2RRM"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:2RRM"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2RRM"
SQ SEQUENCE 1745 AA; 194742 MW; 002B96F5A998B5CD CRC64;
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD
PEPVSDNEDD SYDEEVHDPR AGRGALANRR SEKSWARDRS ASRERSLSPR SDRRSVASSQ
PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS
GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG AISTPVKHVD
DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP VSPSDGALPN SAHEDGILRP
SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR
EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG
EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK
LAREEPDIYQ IAKSEPRDAG TDHRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ
WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND
GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT
SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP
QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS VTNVSLEEPA
PAPPTSHASQ PGCLGAPSAE AAHVVLRGEG PPLPPHADPA KVYRKEPYSE EMMRQNHILK
QPALGHPGQR PDKEPNLAYE PQLPYIEKQA SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF
EDRIPTYEDQ WSYYDDKQPY QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD
SRTRYEQLPR TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ
VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT EEEEDPAMKP
QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP GASLAGPKPV PQSQFSEHDK
TLYRLPEPQK PQVKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFESKP SAHLPAGHHS
EPAKPVHSQS QPNFSSYSSK GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL
SSSSLHIHSK GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS
FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL
SSKTPTSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ MNNISTMPKA VPVSPSAVEE
DEDEDGHTVV ATARGIFNSN GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP
PLDKEKGETL LSPLVMCGPH GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV
LIDHF
