ID INADL_HUMAN Reviewed; 1801 AA. AC Q8NI35; O15249; O43742; O60833; Q5VUA5; Q5VUA6; Q5VUA7; Q5VUA8; Q5VUA9; AC Q5VUB0; Q8WU78; Q9H3N9; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 185. DE RecName: Full=InaD-like protein {ECO:0000303|PubMed:9280290}; DE Short=Inadl protein {ECO:0000303|PubMed:9280290}; DE Short=hINADL {ECO:0000303|PubMed:11374908}; DE AltName: Full=Channel-interacting PDZ domain-containing protein {ECO:0000250|UniProtKB:Q63ZW7}; DE AltName: Full=Pals1-associated tight junction protein {ECO:0000303|PubMed:11927608}; DE AltName: Full=Protein associated to tight junctions {ECO:0000303|PubMed:11964389}; GN Name=PATJ {ECO:0000303|PubMed:22006950, ECO:0000312|HGNC:HGNC:28881}; GN Synonyms=CIPP {ECO:0000250|UniProtKB:Q63ZW7}, INADL GN {ECO:0000303|PubMed:11964389}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY, AND RP VARIANTS ARG-744; MET-870; HIS-1282 AND LEU-1360. RX PubMed=9280290; DOI=10.1016/s0014-5793(97)00877-6; RA Philipp S., Flockerzi V.; RT "Molecular characterization of a novel PDZ domain protein with homology to RT INAD from Drosophila melanogaster."; RL FEBS Lett. 413:243-248(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANTS MET-870; HIS-1282 AND RP LEU-1360. RX PubMed=11374908; DOI=10.1006/geno.2001.6527; RA Soejima H., Kawamoto S., Akai J., Miyoshi O., Arai Y., Morohka T., RA Matsuo S., Niikawa N., Kimura A., Okubo K., Mukai T.; RT "Isolation of novel heart-specific genes using the BodyMap database."; RL Genomics 74:115-120(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PALS1 AND CRB1, RP SUBCELLULAR LOCATION, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY, RP FUNCTION, AND VARIANTS MET-870 AND SER-1178. RC TISSUE=Kidney; RX PubMed=11927608; DOI=10.1083/jcb.200109010; RA Roh M.H., Makarova O., Liu C.-J., Shin K., Lee S., Laurinec S., Goyal M., RA Wiggins R., Margolis B.; RT "The Maguk protein, Pals1, functions as an adapter, linking mammalian RT homologues of Crumbs and Discs Lost."; RL J. Cell Biol. 157:161-172(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1456-1801 (ISOFORM 1). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND INTERACTION WITH CRB1 RP AND CRB3. RX PubMed=11964389; DOI=10.1074/jbc.m202196200; RA Lemmers C., Medina E., Delgrossi M.-H., Michel D., Arsanto J.-P., RA Le Bivic A.; RT "hINADl/PATJ, a homolog of discs lost, interacts with crumbs and localizes RT to tight junctions in human epithelial cells."; RL J. Biol. Chem. 277:25408-25415(2002). RN [7] RP SUBCELLULAR LOCATION, DOMAINS, AND INTERACTION WITH TJP3 AND CLDN1. RX PubMed=12021270; DOI=10.1074/jbc.m201177200; RA Roh M.H., Liu C.-J., Laurinec S., Margolis B.; RT "The carboxyl terminus of zona occludens-3 binds and recruits a mammalian RT homologue of discs lost to tight junctions."; RL J. Biol. Chem. 277:27501-27509(2002). RN [8] RP INTERACTION WITH PALS1. RX PubMed=12527193; DOI=10.1016/s0378111902010843; RA Makarova O., Roh M.H., Liu C.-J., Laurinec S., Margolis B.; RT "Mammalian Crumbs3 is a small transmembrane protein linked to protein RT associated with Lin-7 (Pals1)."; RL Gene 302:21-29(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX RP WITH ARHGAP17; AMOT; PALS1 AND PARD3, AND INTERACTION WITH MPP7. RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045; RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., RA Starostine A., Metalnikov P., Pawson T.; RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity RT proteins in epithelial cells."; RL Cell 125:535-548(2006). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH WWC1. RX PubMed=18596123; DOI=10.1681/asn.2007080916; RA Duning K., Schurek E.M., Schlueter M., Bayer M., Reinhardt H.C., Schwab A., RA Schaefer L., Benzing T., Schermer B., Saleem M.A., Huber T.B., Bachmann S., RA Kremerskothen J., Weide T., Pavenstaedt H.; RT "KIBRA modulates directional migration of podocytes."; RL J. Am. Soc. Nephrol. 19:1891-1903(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1209 AND SER-1212, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP INTERACTION WITH NPHP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=19755384; DOI=10.1093/hmg/ddp434; RA Delous M., Hellman N.E., Gaude H.M., Silbermann F., Le Bivic A., RA Salomon R., Antignac C., Saunier S.; RT "Nephrocystin-1 and nephrocystin-4 are required for epithelial RT morphogenesis and associate with PALS1/PATJ and Par6."; RL Hum. Mol. Genet. 18:4711-4723(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-645; SER-1212 AND RP THR-1508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP FUNCTION, INTERACTION WITH ARHGEF18, AND SUBCELLULAR LOCATION. RX PubMed=22006950; DOI=10.1083/jcb.201104118; RA Nakajima H., Tanoue T.; RT "Lulu2 regulates the circumferential actomyosin tensile system in RT epithelial cells through p114RhoGEF."; RL J. Cell Biol. 195:245-261(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; SER-522; SER-645 AND RP THR-1508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-645 AND SER-1212, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 9-67, AND MUTAGENESIS OF LEU-19 RP AND PHE-38. RX PubMed=15241471; DOI=10.1038/sj.emboj.7600294; RA Li Y., Karnak D., Demeler B., Margolis B., Lavie A.; RT "Structural basis for L27 domain-mediated assembly of signaling and cell RT polarity complexes."; RL EMBO J. 23:2723-2733(2004). RN [21] RP STRUCTURE BY NMR OF 114-470; 675-770 AND 1219-1527. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of PDZ domains of INAD-like protein."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Scaffolding protein that facilitates the localization of CC proteins to the cell membrane (PubMed:11927608, PubMed:16678097, CC PubMed:22006950). Required for the correct formation of tight junctions CC and epithelial apico-basal polarity (PubMed:11927608, PubMed:16678097). CC Positively regulates epithelial cell microtubule elongation and cell CC migration, possibly via facilitating localization of PRKCI/aPKC and CC PAR3D/PAR3 at the leading edge of migrating cells (By similarity). CC Plays a role in the correct reorientation of the microtubule-organizing CC center during epithelial migration (By similarity). May regulate the CC surface expression and/or function of ASIC3 in sensory neurons (By CC similarity). May recruit ARHGEF18 to apical cell-cell boundaries CC (PubMed:22006950). {ECO:0000250|UniProtKB:E2QYC9, CC ECO:0000250|UniProtKB:Q63ZW7, ECO:0000269|PubMed:11927608, CC ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:22006950}. CC -!- SUBUNIT: Forms a ternary complex with PALS1, CRB1 and CRB3 CC (PubMed:11927608, PubMed:11964389). Component of a complex whose core CC is composed of ARHGAP17, AMOT, PALS1, INADL/PATJ and PARD3/PAR3 CC (PubMed:16678097). Forms a heterotrimeric complex composed of MMP5, CC LIN7B and PATJ; the N-terminal L27 domain of PALS1 interacts with the CC L27 domain of PATJ and the C-terminal L27 domain of PALS1 interacts CC with the L27 domain of LIN7B (By similarity). Component of a complex CC composed of CRB3, PALS1 and PATJ (By similarity). Interacts (via N- CC terminus) with PALS1/PALS (via PDZ domain) (PubMed:11927608, CC PubMed:12527193). Interacts with TJP3/ZO-3 and CLDN1/claudin-1 CC (PubMed:12021270). Interacts with ASIC3, KCNJ10, KCNJ15, GRIN2A, CC GRIN2B, GRIN2C, GRIN2D, NLGN2, HTR2A and SLC6A4 (By similarity). CC Interacts with MPP7 (PubMed:12021270). Directly interacts with HTR4 (By CC similarity). Interacts (via PDZ domain 8) with WWC1 (via the ADDV CC motif) (PubMed:18596123). Interacts with SLC6A4 (By similarity). CC Interacts (via C-terminus) with ARHGEF18 (PubMed:22006950). Interacts CC with NPHP1 (PubMed:19755384). Interacts with PARD3/PAR3 (By CC similarity). {ECO:0000250|UniProtKB:A0A5F4CJZ2, CC ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, CC ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:11964389, CC ECO:0000269|PubMed:12021270, ECO:0000269|PubMed:12527193, CC ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:18596123, CC ECO:0000269|PubMed:19755384, ECO:0000269|PubMed:22006950}. CC -!- INTERACTION: CC Q8NI35; P82279: CRB1; NbExp=2; IntAct=EBI-724390, EBI-1048648; CC Q8NI35; P35240: NF2; NbExp=2; IntAct=EBI-724390, EBI-1014472; CC Q8NI35; Q8N3R9: PALS1; NbExp=4; IntAct=EBI-724390, EBI-2513978; CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction CC {ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:11964389, CC ECO:0000269|PubMed:12021270, ECO:0000269|PubMed:19755384, CC ECO:0000269|PubMed:22006950}. Apical cell membrane CC {ECO:0000269|PubMed:11964389}; Peripheral membrane protein CC {ECO:0000269|PubMed:11964389}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:18596123}. Note=Localizes to the apical region at CC the start of epithelial cell polarization then locates to tight CC junctions as polarization is completed (PubMed:11964389). Localized in CC the paranodal region of myelinating Schwann cells (By similarity). CC Localized to the leading edge of the actin cortex of migrating CC epithelia cells (By similarity). {ECO:0000250|UniProtKB:E2QYC9, CC ECO:0000250|UniProtKB:Q63ZW7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q8NI35-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NI35-2; Sequence=VSP_014205, VSP_014207; CC Name=3; CC IsoId=Q8NI35-3; Sequence=VSP_014207; CC Name=4; CC IsoId=Q8NI35-4; Sequence=VSP_014206, VSP_014207; CC Name=5; CC IsoId=Q8NI35-5; Sequence=VSP_014204, VSP_014208, VSP_014209; CC -!- TISSUE SPECIFICITY: Expressed in renal tubules (at protein level) CC (PubMed:19755384). Expressed in bladder, testis, ovary, small CC intestine, colon, heart, skeletal muscle, pancreas and cerebellum in CC the brain. {ECO:0000269|PubMed:11964389, ECO:0000269|PubMed:19755384, CC ECO:0000269|PubMed:9280290}. CC -!- DOMAIN: The L27 domain (also called Maguk recruitment domain) is CC required for interaction with PALS1 and CRB3, and PALS1 localization to CC tight junctions. {ECO:0000269|PubMed:11927608}. CC -!- DOMAIN: The PDZ domain 6 mediates interaction with the C-terminus of CC TJP3 and is crucial for localization to the tight junctions CC (PubMed:12021270). The PDZ domain 8 interacts with CLDN1 but is not CC required for proper localization (PubMed:12021270). CC {ECO:0000269|PubMed:12021270}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ001306; CAA04666.1; -; mRNA. DR EMBL; AJ224747; CAA12112.1; -; mRNA. DR EMBL; AJ224748; CAA12113.1; -; mRNA. DR EMBL; AB044807; BAB19683.1; -; mRNA. DR EMBL; AF397170; AAM28433.1; -; mRNA. DR EMBL; AC097064; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136458; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353802; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL449143; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590374; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC021135; AAH21135.1; -; mRNA. DR CCDS; CCDS617.2; -. [Q8NI35-1] DR PDB; 1VF6; X-ray; 2.10 A; A/B=9-67. DR PDB; 2D92; NMR; -; A=676-770. DR PDB; 2DAZ; NMR; -; A=1219-1329. DR PDB; 2DB5; NMR; -; A=114-228. DR PDB; 2DLU; NMR; -; A=238-335. DR PDB; 2DM8; NMR; -; A=1425-1527. DR PDB; 2DMZ; NMR; -; A=355-470. DR PDB; 2EHR; NMR; -; A=1058-1167. DR PDB; 4Q2N; X-ray; 2.00 A; A/B/C/D/E/F=362-452. DR PDB; 6IRD; X-ray; 2.81 A; C=1421-1625. DR PDBsum; 1VF6; -. DR PDBsum; 2D92; -. DR PDBsum; 2DAZ; -. DR PDBsum; 2DB5; -. DR PDBsum; 2DLU; -. DR PDBsum; 2DM8; -. DR PDBsum; 2DMZ; -. DR PDBsum; 2EHR; -. DR PDBsum; 4Q2N; -. DR PDBsum; 6IRD; -. DR AlphaFoldDB; Q8NI35; -. DR SMR; Q8NI35; -. DR BioGRID; 115502; 92. DR ComplexPortal; CPX-6166; CRUMBS3-PALS1-PATJ cell polarity complex. DR ComplexPortal; CPX-6167; CRUMBS1-PALS1-PATJ cell polarity complex. DR ComplexPortal; CPX-6180; CRUMBS2-PALS1-PATJ cell polarity complex. DR CORUM; Q8NI35; -. DR IntAct; Q8NI35; 71. DR MINT; Q8NI35; -. DR STRING; 9606.ENSP00000494277; -. DR GlyGen; Q8NI35; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NI35; -. DR PhosphoSitePlus; Q8NI35; -. DR SwissPalm; Q8NI35; -. DR BioMuta; PATJ; -. DR DMDM; 116242542; -. DR EPD; Q8NI35; -. DR jPOST; Q8NI35; -. DR MassIVE; Q8NI35; -. DR MaxQB; Q8NI35; -. DR PaxDb; 9606-ENSP00000360200; -. DR PeptideAtlas; Q8NI35; -. DR ProteomicsDB; 73822; -. [Q8NI35-1] DR ProteomicsDB; 73823; -. [Q8NI35-2] DR ProteomicsDB; 73824; -. [Q8NI35-3] DR ProteomicsDB; 73825; -. [Q8NI35-4] DR ProteomicsDB; 73826; -. [Q8NI35-5] DR Pumba; Q8NI35; -. DR Antibodypedia; 33304; 187 antibodies from 30 providers. DR Ensembl; ENST00000371158.6; ENSP00000360200.2; ENSG00000132849.22. [Q8NI35-1] DR Ensembl; ENST00000484937.5; ENSP00000433669.1; ENSG00000132849.22. [Q8NI35-5] DR UCSC; uc001dab.4; human. [Q8NI35-1] DR AGR; HGNC:28881; -. DR GeneCards; PATJ; -. DR HGNC; HGNC:28881; PATJ. DR HPA; ENSG00000132849; Low tissue specificity. DR MIM; 603199; gene. DR neXtProt; NX_Q8NI35; -. DR OpenTargets; ENSG00000132849; -. DR PharmGKB; PA134919267; -. DR VEuPathDB; HostDB:ENSG00000132849; -. DR eggNOG; KOG0708; Eukaryota. DR eggNOG; KOG3528; Eukaryota. DR GeneTree; ENSGT00940000155136; -. DR HOGENOM; CLU_002378_1_0_1; -. DR InParanoid; Q8NI35; -. DR PhylomeDB; Q8NI35; -. DR TreeFam; TF330709; -. DR PathwayCommons; Q8NI35; -. DR Reactome; R-HSA-420029; Tight junction interactions. DR Reactome; R-HSA-9705677; SARS-CoV-2 targets PDZ proteins in cell-cell junction. DR SignaLink; Q8NI35; -. DR SIGNOR; Q8NI35; -. DR BioGRID-ORCS; 10207; 19 hits in 1136 CRISPR screens. DR ChiTaRS; PATJ; human. DR EvolutionaryTrace; Q8NI35; -. DR GeneWiki; INADL; -. DR Pharos; Q8NI35; Tbio. DR PRO; PR:Q8NI35; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8NI35; Protein. DR Bgee; ENSG00000132849; Expressed in heart right ventricle and 188 other cell types or tissues. DR ExpressionAtlas; Q8NI35; baseline and differential. DR GO; GO:0043296; C:apical junction complex; NAS:ComplexPortal. DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS:UniProtKB. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; NAS:ComplexPortal. DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB. DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central. DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0120192; P:tight junction assembly; ISS:UniProtKB. DR CDD; cd00992; PDZ_signaling; 10. DR Gene3D; 1.20.1440.360; -; 1. DR Gene3D; 2.30.42.10; -; 10. DR InterPro; IPR015132; L27_2. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR036892; L27_dom_sf. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR19964; MULTIPLE PDZ DOMAIN PROTEIN; 1. DR PANTHER; PTHR19964:SF44; PATJ HOMOLOG; 1. DR Pfam; PF09045; L27_2; 1. DR Pfam; PF00595; PDZ; 10. DR SMART; SM00569; L27; 1. DR SMART; SM00228; PDZ; 10. DR SUPFAM; SSF101288; L27 domain; 1. DR SUPFAM; SSF50156; PDZ domain-like; 10. DR PROSITE; PS51022; L27; 1. DR PROSITE; PS50106; PDZ; 10. DR Genevisible; Q8NI35; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat; KW Tight junction. FT CHAIN 1..1801 FT /note="InaD-like protein" FT /id="PRO_0000094592" FT DOMAIN 1..65 FT /note="L27" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 134..221 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 248..328 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 365..453 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 553..639 FT /note="PDZ 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 686..772 FT /note="PDZ 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1068..1160 FT /note="PDZ 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1239..1322 FT /note="PDZ 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1437..1520 FT /note="PDZ 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1533..1615 FT /note="PDZ 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1676..1762 FT /note="PDZ 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 452..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1169..1221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1332..1360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1622..1642 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1781..1801 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1332..1354 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 455 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 522 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 645 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1209 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1212 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1508 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..541 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11374908" FT /id="VSP_014204" FT VAR_SEQ 1459 FT /note="L -> LFWRLGSPRAWSQHLVRAFMLHHPVTEVEGQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9280290" FT /id="VSP_014205" FT VAR_SEQ 1460..1487 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:9280290" FT /id="VSP_014206" FT VAR_SEQ 1553..1801 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:9280290" FT /id="VSP_014207" FT VAR_SEQ 1631..1675 FT /note="GSQQSAHSSCHPSFAPVITGLQNLVGTKRVSDPSQKNSGTDMEPR -> SAE FT CTQQLSSLLRSCHHWPAKPGWHKKSFRSFPEKFRHRYGTKDC (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11374908" FT /id="VSP_014208" FT VAR_SEQ 1676..1801 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11374908" FT /id="VSP_014209" FT VARIANT 303 FT /note="G -> R (in dbSNP:rs3762321)" FT /id="VAR_027988" FT VARIANT 362 FT /note="E -> A (in dbSNP:rs1286823)" FT /id="VAR_027989" FT VARIANT 400 FT /note="I -> V (in dbSNP:rs7516332)" FT /id="VAR_027990" FT VARIANT 599 FT /note="Q -> H (in dbSNP:rs1286812)" FT /id="VAR_027991" FT VARIANT 744 FT /note="C -> R (in dbSNP:rs1134764)" FT /evidence="ECO:0000269|PubMed:9280290" FT /id="VAR_022695" FT VARIANT 779 FT /note="E -> K (in dbSNP:rs12141598)" FT /id="VAR_027992" FT VARIANT 780 FT /note="E -> K (in dbSNP:rs12141599)" FT /id="VAR_027993" FT VARIANT 870 FT /note="I -> M (in dbSNP:rs2799627)" FT /evidence="ECO:0000269|PubMed:11374908, FT ECO:0000269|PubMed:11927608, ECO:0000269|PubMed:9280290" FT /id="VAR_027994" FT VARIANT 1178 FT /note="G -> S (in dbSNP:rs1056513)" FT /evidence="ECO:0000269|PubMed:11927608" FT /id="VAR_027995" FT VARIANT 1282 FT /note="R -> H (in dbSNP:rs1134767)" FT /evidence="ECO:0000269|PubMed:11374908, FT ECO:0000269|PubMed:9280290" FT /id="VAR_027996" FT VARIANT 1360 FT /note="V -> L (in dbSNP:rs2498982)" FT /evidence="ECO:0000269|PubMed:11374908, FT ECO:0000269|PubMed:9280290" FT /id="VAR_027997" FT VARIANT 1504 FT /note="A -> P (in dbSNP:rs13376115)" FT /id="VAR_027998" FT MUTAGEN 19 FT /note="L->W: Reduces L27 domain binding affinity to PALS1 FT L27 domain." FT /evidence="ECO:0000269|PubMed:15241471" FT MUTAGEN 38 FT /note="F->W: Reduces L27 domain binding affinity to PALS1 FT L27 domain." FT /evidence="ECO:0000269|PubMed:15241471" FT CONFLICT 1443 FT /note="G -> R (in Ref. 1; CAA04666)" FT /evidence="ECO:0000305" FT CONFLICT 1699 FT /note="L -> I (in Ref. 3; AAM28433)" FT /evidence="ECO:0000305" FT HELIX 13..26 FT /evidence="ECO:0007829|PDB:1VF6" FT HELIX 32..43 FT /evidence="ECO:0007829|PDB:1VF6" FT HELIX 45..67 FT /evidence="ECO:0007829|PDB:1VF6" FT HELIX 119..127 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 131..138 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:2DB5" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 184..190 FT /evidence="ECO:0007829|PDB:2DB5" FT HELIX 199..208 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 211..219 FT /evidence="ECO:0007829|PDB:2DB5" FT STRAND 244..252 FT /evidence="ECO:0007829|PDB:2DLU" FT STRAND 260..263 FT /evidence="ECO:0007829|PDB:2DLU" FT STRAND 266..275 FT /evidence="ECO:0007829|PDB:2DLU" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:2DLU" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:2DLU" FT HELIX 306..316 FT /evidence="ECO:0007829|PDB:2DLU" FT STRAND 318..327 FT /evidence="ECO:0007829|PDB:2DLU" FT STRAND 362..369 FT /evidence="ECO:0007829|PDB:4Q2N" FT STRAND 378..382 FT /evidence="ECO:0007829|PDB:4Q2N" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:2DMZ" FT STRAND 395..400 FT /evidence="ECO:0007829|PDB:4Q2N" FT HELIX 405..409 FT /evidence="ECO:0007829|PDB:4Q2N" FT STRAND 417..421 FT /evidence="ECO:0007829|PDB:4Q2N" FT HELIX 431..439 FT /evidence="ECO:0007829|PDB:4Q2N" FT STRAND 443..452 FT /evidence="ECO:0007829|PDB:4Q2N" FT STRAND 685..691 FT /evidence="ECO:0007829|PDB:2D92" FT STRAND 697..704 FT /evidence="ECO:0007829|PDB:2D92" FT STRAND 712..719 FT /evidence="ECO:0007829|PDB:2D92" FT HELIX 724..728 FT /evidence="ECO:0007829|PDB:2D92" FT STRAND 736..742 FT /evidence="ECO:0007829|PDB:2D92" FT HELIX 750..759 FT /evidence="ECO:0007829|PDB:2D92" FT STRAND 762..770 FT /evidence="ECO:0007829|PDB:2D92" FT STRAND 1058..1061 FT /evidence="ECO:0007829|PDB:2EHR" FT STRAND 1067..1071 FT /evidence="ECO:0007829|PDB:2EHR" FT STRAND 1075..1077 FT /evidence="ECO:0007829|PDB:2EHR" FT STRAND 1081..1083 FT /evidence="ECO:0007829|PDB:2EHR" FT STRAND 1101..1107 FT /evidence="ECO:0007829|PDB:2EHR" FT STRAND 1109..1111 FT /evidence="ECO:0007829|PDB:2EHR" FT TURN 1112..1114 FT /evidence="ECO:0007829|PDB:2EHR" FT STRAND 1124..1130 FT /evidence="ECO:0007829|PDB:2EHR" FT HELIX 1138..1146 FT /evidence="ECO:0007829|PDB:2EHR" FT STRAND 1150..1156 FT /evidence="ECO:0007829|PDB:2EHR" FT HELIX 1219..1221 FT /evidence="ECO:0007829|PDB:2DAZ" FT HELIX 1223..1229 FT /evidence="ECO:0007829|PDB:2DAZ" FT STRAND 1233..1243 FT /evidence="ECO:0007829|PDB:2DAZ" FT STRAND 1251..1254 FT /evidence="ECO:0007829|PDB:2DAZ" FT STRAND 1256..1258 FT /evidence="ECO:0007829|PDB:2DAZ" FT STRAND 1264..1269 FT /evidence="ECO:0007829|PDB:2DAZ" FT HELIX 1274..1278 FT /evidence="ECO:0007829|PDB:2DAZ" FT STRAND 1289..1292 FT /evidence="ECO:0007829|PDB:2DAZ" FT HELIX 1300..1309 FT /evidence="ECO:0007829|PDB:2DAZ" FT STRAND 1312..1320 FT /evidence="ECO:0007829|PDB:2DAZ" FT HELIX 1324..1327 FT /evidence="ECO:0007829|PDB:2DAZ" FT STRAND 1425..1427 FT /evidence="ECO:0007829|PDB:2DM8" FT STRAND 1436..1441 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1449..1452 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1455..1459 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1461..1467 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1469..1471 FT /evidence="ECO:0007829|PDB:2DM8" FT HELIX 1472..1476 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1484..1488 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1494..1496 FT /evidence="ECO:0007829|PDB:2DM8" FT HELIX 1498..1506 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1510..1517 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1530..1537 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1540..1542 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1547..1549 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1552..1555 FT /evidence="ECO:0007829|PDB:6IRD" FT HELIX 1567..1571 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1579..1583 FT /evidence="ECO:0007829|PDB:6IRD" FT HELIX 1593..1602 FT /evidence="ECO:0007829|PDB:6IRD" FT STRAND 1605..1613 FT /evidence="ECO:0007829|PDB:6IRD" SQ SEQUENCE 1801 AA; 196368 MW; 313DD1F12B6AD80A CRC64; MPENPATDKL QVLQVLDRLK MKLQEKGDTS QNEKLSMFYE TLKSPLFNQI LTLQQSIKQL KGQLNHIPSD CSANFDFSRK GLLVFTDGSI TNGNVHRPSN NSTVSGLFPW TPKLGNEDFN SVIQQMAQGR QIEYIDIERP STGGLGFSVV ALRSQNLGKV DIFVKDVQPG SVADRDQRLK ENDQILAINH TPLDQNISHQ QAIALLQQTT GSLRLIVARE PVHTKSSTSS SLNDTTLPET VCWGHVEEVE LINDGSGLGF GIVGGKTSGV VVRTIVPGGL ADRDGRLQTG DHILKIGGTN VQGMTSEQVA QVLRNCGNSV RMLVARDPAG DISVTPPAPA ALPVALPTVA SKGPGSDSSL FETYNVELVR KDGQSLGIRI VGYVGTSHTG EASGIYVKSI IPGSAAYHNG HIQVNDKIVA VDGVNIQGFA NHDVVEVLRN AGQVVHLTLV RRKTSSSTSP LEPPSDRGTV VEPLKPPALF LTGAVETETN VDGEDEEIKE RIDTLKNDNI QALEKLEKVP DSPENELKSR WENLLGPDYE VMVATLDTQI ADDAELQKYS KLLPIHTLRL GVEVDSFDGH HYISSIVSGG PVDTLGLLQP EDELLEVNGM QLYGKSRREA VSFLKEVPPP FTLVCCRRLF DDEASVDEPR RTETSLPETE VDHNMDVNTE EDDDGELALW SPEVKIVELV KDCKGLGFSI LDYQDPLDPT RSVIVIRSLV ADGVAERSGG LLPGDRLVSV NEYCLDNTSL AEAVEILKAV PPGLVHLGIC KPLVEDNEEE SCYILHSSSN EDKTEFSGTI HDINSSLILE APKGFRDEPY FKEELVDEPF LDLGKSFHSQ QKEIEQSKEA WEMHEFLTPR LQEMDEEREI LVDEEYELYQ DPSPSMELYP LSHIQEATPV PSVNELHFGT QWLHDNEPSE SQEARTGRTV YSQEAQPYGY CPENVMKENF VMESLPSVPS TEGNSQQGRF DDLENLNSLA KTSLDLGMIP NDVQGPSLLI DLPVVAQRRE QEDLPLYQHQ ATRVISKASA YTGMLSSRYA TDTCELPERE EGEGEETPNF SHWGPPRIVE IFREPNVSLG ISIVGGQTVI KRLKNGEELK GIFIKQVLED SPAGKTNALK TGDKILEVSG VDLQNASHSE AVEAIKNAGN PVVFIVQSLS STPRVIPNVH NKANKITGNQ NQDTQEKKEK RQGTAPPPMK LPPPYKALTD DSDENEEEDA FTDQKIRQRY ADLPGELHII ELEKDKNGLG LSLAGNKDRS RMSIFVVGIN PEGPAAADGR MRIGDELLEI NNQILYGRSH QNASAIIKTA PSKVKLVFIR NEDAVNQMAV TPFPVPSSSP SSIEDQSGTE PISSEEDGSV EVGIKQLPES ESFKLAVSQM KQQKYPTKVS FSSQEIPLAP ASSYHSTDAD FTGYGGFQAP LSVDPATCPI VPGQEMIIEI SKGRSGLGLS IVGGKDTPLN AIVIHEVYEE GAAARDGRLW AGDQILEVNG VDLRNSSHEE AITALRQTPQ KVRLVVYRDE AHYRDEENLE IFPVDLQKKA GRGLGLSIVG KRNGSGVFIS DIVKGGAADL DGRLIQGDQI LSVNGEDMRN ASQETVATIL KCAQGLVQLE IGRLRAGSWT SARTTSQNSQ GSQQSAHSSC HPSFAPVITG LQNLVGTKRV SDPSQKNSGT DMEPRTVEIN RELSDALGIS IAGGRGSPLG DIPVFIAMIQ ASGVAARTQK LKVGDRIVSI NGQPLDGLSH ADVVNLLKNA YGRIILQVVA DTNISAIAAQ LENMSTGYHL GSPTAEHHPE DTEEQLQMTA D //