INADL_HUMAN
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 03-AUG-2022, entry version 176.
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},
GN INADL {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 Q8NI35; P46937: YAP1; NbExp=5; IntAct=EBI-724390, EBI-1044059;
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}.
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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; 80.
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; 67.
DR MINT; Q8NI35; -.
DR STRING; 9606.ENSP00000360200; -.
DR iPTMnet; Q8NI35; -.
DR PhosphoSitePlus; Q8NI35; -.
DR BioMuta; PATJ; -.
DR DMDM; 116242542; -.
DR EPD; Q8NI35; -.
DR jPOST; Q8NI35; -.
DR MassIVE; Q8NI35; -.
DR MaxQB; Q8NI35; -.
DR PaxDb; Q8NI35; -.
DR PeptideAtlas; Q8NI35; -.
DR PRIDE; 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 Antibodypedia; 33304; 159 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 GeneCards; PATJ; -.
DR HGNC; HGNC:28881; PATJ.
DR HPA; ENSG00000132849; Tissue enhanced (brain).
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 OrthoDB; 1419918at2759; -.
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 1065 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 186 other tissues.
DR ExpressionAtlas; Q8NI35; baseline and differential.
DR Genevisible; Q8NI35; HS.
DR GO; GO:0043296; C:apical junction complex; IC:ComplexPortal.
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; TAS:Reactome.
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; IC:ComplexPortal.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0120192; P:tight junction assembly; ISS:UniProtKB.
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 Pfam; PF09045; L27_2; 1.
DR Pfam; PF00595; PDZ; 10.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 10.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50156; SSF50156; 10.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 10.
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
