INADL_MOUSE
ID INADL_MOUSE Reviewed; 1834 AA.
AC Q63ZW7; A2ADS7; O70471; Q5PRG3; Q6P6J1; Q80YR8; Q8BPB9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=InaD-like protein {ECO:0000250|UniProtKB:Q8NI35};
DE Short=Inadl protein {ECO:0000250|UniProtKB:Q8NI35};
DE AltName: Full=Channel-interacting PDZ domain-containing protein {ECO:0000303|PubMed:9647694};
DE AltName: Full=Pals1-associated tight junction protein {ECO:0000303|PubMed:12403818};
DE AltName: Full=Protein associated to tight junctions {ECO:0000250|UniProtKB:Q8NI35};
GN Name=Patj {ECO:0000312|MGI:MGI:1277960};
GN Synonyms=Cipp {ECO:0000303|PubMed:9647694},
GN Inadl {ECO:0000250|UniProtKB:Q8NI35};
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] (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION
RP WITH KCNJ10; KCNJ15; NRXN2; NLGN2; GRIN2A; GRIN2B; GRIN2C AND GRIN2D, AND
RP DOMAINS.
RC STRAIN=BALB/cJ; TISSUE=Cerebellum;
RX PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT neuroligins.";
RL Mol. Cell. Neurosci. 11:161-172(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 493-1834 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 523-1834 (ISOFORM 6).
RC STRAIN=C57BL/6J, FVB/N, and NMRI;
RC TISSUE=Brain, Embryo, Eye, Mammary tumor, and Salivary gland;
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 [5]
RP INTERACTION WITH ASIC3, DOMAIN, AND FUNCTION.
RX PubMed=11872753; DOI=10.1074/jbc.m201087200;
RA Anzai N., Deval E., Schaefer L., Friend V., Lazdunski M., Lingueglia E.;
RT "The multivalent PDZ domain-containing protein CIPP is a partner of acid-
RT sensing ion channel 3 in sensory neurons.";
RL J. Biol. Chem. 277:16655-16661(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12403818; DOI=10.1083/jcb.200207050;
RA Poliak S., Matlis S., Ullmer C., Scherer S.S., Peles E.;
RT "Distinct claudins and associated PDZ proteins form different autotypic
RT tight junctions in myelinating Schwann cells.";
RL J. Cell Biol. 159:361-372(2002).
RN [7]
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 [8]
RP INTERACTION WITH HTR2A, AND SUBCELLULAR LOCATION.
RX PubMed=14988405; DOI=10.1074/jbc.m312106200;
RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A.,
RA Bockaert J., Marin P.;
RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of
RT PDZ proteins.";
RL J. Biol. Chem. 279:20257-20266(2004).
RN [9]
RP INTERACTION WITH HTR4.
RX PubMed=15466885; DOI=10.1242/jcs.01379;
RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA Marin P., Dumuis A., Bockaert J.;
RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT receptor splice variant: roles in receptor targeting.";
RL J. Cell Sci. 117:5367-5379(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647, 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 [11]
RP INTERACTION WITH SLC6A4.
RX PubMed=17452640; DOI=10.1073/pnas.0610964104;
RA Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M.,
RA Freissmuth M., Millan M.J., Bockaert J., Marin P.;
RT "Physical interaction between the serotonin transporter and neuronal nitric
RT oxide synthase underlies reciprocal modulation of their activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-482; SER-524;
RP SER-647 AND SER-1215, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Pancreas;
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 [13]
RP INTERACTION WITH PALS1, AND DEVELOPMENTAL STAGE.
RX PubMed=20399730; DOI=10.1016/j.neuron.2010.03.019;
RA Kim S., Lehtinen M.K., Sessa A., Zappaterra M.W., Cho S.H., Gonzalez D.,
RA Boggan B., Austin C.A., Wijnholds J., Gambello M.J., Malicki J.,
RA LaMantia A.S., Broccoli V., Walsh C.A.;
RT "The apical complex couples cell fate and cell survival to cerebral
RT cortical development.";
RL Neuron 66:69-84(2010).
CC -!- FUNCTION: Scaffolding protein that facilitates the localization of
CC proteins to the cell membrane (PubMed:11872753). Required for the
CC correct formation of tight junctions and epithelial apico-basal
CC polarity (By similarity). Positively regulates epithelial cell
CC microtubule elongation and cell migration, possibly via facilitating
CC localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of
CC migrating cells (By similarity). Plays a role in the correct
CC reorientation of the microtubule-organizing center during epithelial
CC migration (By similarity). May regulate the surface expression and/or
CC function of ASIC3 in sensory neurons (PubMed:11872753). May recruit
CC ARHGEF18 to apical cell-cell boundaries (By similarity).
CC {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q8NI35,
CC ECO:0000269|PubMed:11872753}.
CC -!- SUBUNIT: Forms a ternary complex with PALS1 and CRB1 (By similarity).
CC Component of a complex whose core is composed of ARHGAP17, AMOT, PALS1,
CC INADL/PATJ and PARD3/PAR3 (By similarity). Forms a heterotrimeric
CC complex composed of MMP5, LIN7B and PATJ; the N-terminal L27 domain of
CC PALS1 interacts with the L27 domain of PATJ and the C-terminal L27
CC domain of PALS1 interacts with the L27 domain of LIN7B (By similarity).
CC Component of a complex composed of CRB3, PALS1 and PATJ (By
CC similarity). Interacts (via N-terminus) with PALS1/PALS (via PDZ
CC domain) (PubMed:12527193, PubMed:20399730). Interacts with TJP3/ZO-3
CC and CLDN1/claudin-1 (By similarity). Interacts with ASIC3, KCNJ10,
CC KCNJ15, GRIN2A, GRIN2B, GRIN2C, GRIN2D, NLGN2, and HTR2A
CC (PubMed:9647694, PubMed:11872753, PubMed:14988405). Interacts with MPP7
CC (By similarity). Directly interacts with HTR4 (PubMed:15466885).
CC Interacts (via PDZ domain 8) with WWC1 (via the ADDV motif) (By
CC similarity). Interacts with SLC6A4 (PubMed:17452640). Interacts (via C-
CC terminus) with ARHGEF18 (By similarity). Interacts with NPHP1 (By
CC similarity). Interacts with PARD3/PAR3 (By similarity).
CC {ECO:0000250|UniProtKB:A0A5F4CJZ2, ECO:0000250|UniProtKB:E2QYC9,
CC ECO:0000250|UniProtKB:F1MAD2, ECO:0000250|UniProtKB:Q8NI35,
CC ECO:0000269|PubMed:11872753, ECO:0000269|PubMed:12527193,
CC ECO:0000269|PubMed:14988405, ECO:0000269|PubMed:15466885,
CC ECO:0000269|PubMed:17452640, ECO:0000269|PubMed:20399730,
CC ECO:0000269|PubMed:9647694}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with NRXN2.
CC {ECO:0000269|PubMed:9647694}.
CC -!- INTERACTION:
CC Q63ZW7; P35436: Grin2a; NbExp=4; IntAct=EBI-8366894, EBI-400115;
CC Q63ZW7; Q00960: Grin2b; Xeno; NbExp=4; IntAct=EBI-8366894, EBI-396905;
CC Q63ZW7; Q00961: Grin2c; Xeno; NbExp=2; IntAct=EBI-8366894, EBI-631045;
CC Q63ZW7; Q62645: Grin2d; Xeno; NbExp=3; IntAct=EBI-8366894, EBI-631067;
CC Q63ZW7; Q99712: KCNJ15; Xeno; NbExp=4; IntAct=EBI-8366894, EBI-7082607;
CC Q63ZW7-3; O35240: Asic3; Xeno; NbExp=2; IntAct=EBI-8158524, EBI-982374;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q8NI35}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q8NI35}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:14988405}. Note=Localizes to the apical region at
CC the start of epithelial cell polarization then locates to tight
CC junctions as polarization is completed (By similarity). Localized in
CC the paranodal region of myelinating Schwann cells (PubMed:12403818).
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:Q8NI35, ECO:0000269|PubMed:12403818}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Cytoplasm, perinuclear
CC region. Note=Concentrates around the nucleus upon HTR2A coexpression.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q63ZW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63ZW7-2; Sequence=VSP_014211;
CC Name=3;
CC IsoId=Q63ZW7-3; Sequence=VSP_014210, VSP_014216;
CC Name=4;
CC IsoId=Q63ZW7-4; Sequence=VSP_014210, VSP_014216, VSP_014217,
CC VSP_014218;
CC Name=5;
CC IsoId=Q63ZW7-5; Sequence=VSP_014212, VSP_014213;
CC Name=6;
CC IsoId=Q63ZW7-6; Sequence=VSP_014214, VSP_014215;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in the kidney.
CC {ECO:0000269|PubMed:9647694}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in the brain, high levels
CC are detected in the cerebellum, inferior colliculus, vestibular
CC nucleus, facial nucleus and thalamus (PubMed:9647694). Also detected in
CC deep cerebellar nuclei, superior colliculus, dorsal transition zone,
CC brain stem, as well as the glomerular and mitral cell layers of the
CC olfactory bulb (PubMed:9647694). Within the cerebellum it is expressed
CC in both Purkinje and granule cell layers (PubMed:9647694).
CC {ECO:0000269|PubMed:9647694}.
CC -!- DEVELOPMENTAL STAGE: Expressed apically in the cortical neuroepithelium
CC along the ventricular surface at 14.5 dpc.
CC {ECO:0000269|PubMed:20399730}.
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:0000250}.
CC -!- DOMAIN: The PDZ domain 6 mediates interaction with the C-terminus of
CC TJP3 and is crucial for localization to the tight junctions. The PDZ
CC domain 8 interacts with CLDN1 but is not required for proper
CC localization (By similarity). The PDZ domain 2 of isoform 3 mediates
CC interactions with KCNJ10, KCNJ15, GRIN2B and NLGN2. The PDZ domain 3 of
CC isoform 3 mediates interactions with KCNJ15, GRIN2A, GRIN2B, GRIN2C,
CC GRIN2D and NRXN2. The PDZ domain 4 of isoform 3 mediates interaction
CC with ASIC3. {ECO:0000250, ECO:0000269|PubMed:11872753,
CC ECO:0000269|PubMed:9647694}.
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DR EMBL; AF060539; AAC40148.1; -; mRNA.
DR EMBL; AK077268; BAC36720.1; -; mRNA.
DR EMBL; AL671229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037607; AAH37607.1; -; mRNA.
DR EMBL; BC050846; AAH50846.1; -; mRNA.
DR EMBL; BC057124; AAH57124.1; -; mRNA.
DR EMBL; BC062194; AAH62194.1; -; mRNA.
DR EMBL; BC082787; AAH82787.1; -; mRNA.
DR CCDS; CCDS18375.1; -. [Q63ZW7-1]
DR CCDS; CCDS18376.1; -. [Q63ZW7-3]
DR CCDS; CCDS18377.1; -. [Q63ZW7-4]
DR RefSeq; NP_001005784.1; NM_001005784.1. [Q63ZW7-6]
DR RefSeq; NP_001005787.1; NM_001005787.1. [Q63ZW7-4]
DR RefSeq; NP_031730.1; NM_007704.2. [Q63ZW7-3]
DR RefSeq; NP_766284.2; NM_172696.2. [Q63ZW7-1]
DR RefSeq; XP_006502762.1; XM_006502699.2. [Q63ZW7-1]
DR RefSeq; XP_006502763.1; XM_006502700.2. [Q63ZW7-1]
DR RefSeq; XP_006502764.1; XM_006502701.1. [Q63ZW7-1]
DR AlphaFoldDB; Q63ZW7; -.
DR SMR; Q63ZW7; -.
DR BioGRID; 198715; 28.
DR DIP; DIP-41238N; -.
DR ELM; Q63ZW7; -.
DR IntAct; Q63ZW7; 14.
DR MINT; Q63ZW7; -.
DR STRING; 10090.ENSMUSP00000049176; -.
DR iPTMnet; Q63ZW7; -.
DR PhosphoSitePlus; Q63ZW7; -.
DR jPOST; Q63ZW7; -.
DR MaxQB; Q63ZW7; -.
DR PaxDb; Q63ZW7; -.
DR PeptideAtlas; Q63ZW7; -.
DR PRIDE; Q63ZW7; -.
DR ProteomicsDB; 266980; -. [Q63ZW7-1]
DR ProteomicsDB; 266981; -. [Q63ZW7-2]
DR ProteomicsDB; 266982; -. [Q63ZW7-3]
DR ProteomicsDB; 266983; -. [Q63ZW7-4]
DR ProteomicsDB; 266984; -. [Q63ZW7-5]
DR ProteomicsDB; 266985; -. [Q63ZW7-6]
DR Antibodypedia; 33304; 159 antibodies from 30 providers.
DR DNASU; 12695; -.
DR Ensembl; ENSMUST00000030290; ENSMUSP00000030290; ENSMUSG00000061859. [Q63ZW7-4]
DR Ensembl; ENSMUST00000041284; ENSMUSP00000049176; ENSMUSG00000061859. [Q63ZW7-1]
DR Ensembl; ENSMUST00000102792; ENSMUSP00000099854; ENSMUSG00000061859. [Q63ZW7-3]
DR Ensembl; ENSMUST00000107029; ENSMUSP00000102644; ENSMUSG00000061859. [Q63ZW7-2]
DR Ensembl; ENSMUST00000107030; ENSMUSP00000102645; ENSMUSG00000061859. [Q63ZW7-5]
DR GeneID; 12695; -.
DR KEGG; mmu:12695; -.
DR UCSC; uc008tub.1; mouse. [Q63ZW7-6]
DR UCSC; uc008tuc.1; mouse. [Q63ZW7-1]
DR UCSC; uc008tug.1; mouse. [Q63ZW7-4]
DR UCSC; uc008tuh.1; mouse. [Q63ZW7-3]
DR CTD; 10207; -.
DR MGI; MGI:1277960; Patj.
DR VEuPathDB; HostDB:ENSMUSG00000061859; -.
DR eggNOG; KOG0708; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155136; -.
DR HOGENOM; CLU_002378_1_0_1; -.
DR InParanoid; Q63ZW7; -.
DR OMA; ESHYILH; -.
DR PhylomeDB; Q63ZW7; -.
DR TreeFam; TF330709; -.
DR BioGRID-ORCS; 12695; 3 hits in 68 CRISPR screens.
DR ChiTaRS; Patj; mouse.
DR PRO; PR:Q63ZW7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q63ZW7; protein.
DR Bgee; ENSMUSG00000061859; Expressed in cerebellar vermis and 222 other tissues.
DR ExpressionAtlas; Q63ZW7; baseline and differential.
DR Genevisible; Q63ZW7; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035003; C:subapical complex; IDA:MGI.
DR GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS: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 Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1834
FT /note="InaD-like protein"
FT /id="PRO_0000094593"
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 555..641
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 688..774
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1074..1166
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1245..1328
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1472..1555
FT /note="PDZ 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1568..1650
FT /note="PDZ 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1709..1795
FT /note="PDZ 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 456..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1819..1834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI35"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI35"
FT VAR_SEQ 1..1222
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9647694"
FT /id="VSP_014210"
FT VAR_SEQ 1..573
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014211"
FT VAR_SEQ 564..598
FT /note="LLPIHTLRLGMEVDSFDGHHYISSVAPGGPVDTLN -> WMLVLKAKAVPPS
FT ALHVVGSRAHIRRYKMALTAVF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014212"
FT VAR_SEQ 599..1834
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014213"
FT VAR_SEQ 951..975
FT /note="MEETFGLDSRAPIPSSEGNGQHGRF -> VRLCDTATTCSPLCPHTPRSCYF
FT HS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014214"
FT VAR_SEQ 976..1834
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014215"
FT VAR_SEQ 1223..1230
FT /note="EDCALTDK -> MVHGGFPE (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9647694"
FT /id="VSP_014216"
FT VAR_SEQ 1792..1804
FT /note="VADTNISAIATQL -> FRSMENQLAEADK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014217"
FT VAR_SEQ 1805..1834
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014218"
FT CONFLICT 740
FT /note="V -> L (in Ref. 2; BAC36720)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="S -> R (in Ref. 2; BAC36720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1834 AA; 198517 MW; 177ADF8E12B82A30 CRC64;
MPENPAAEKM QVLQVLDRLR GKLQEKGDTT QNEKLSAFYE TLKSPLFNQI LTLQQSIKQL
KGQLSHIPSD CSANFDFSRK GLLVFTDGSI TNGNAQRPCS NVTASELLPW TQKSASEDFN
SVIQQMAQGR HVEYIDIERP STGGLGFSVV ALRSQSLGLI DIFVKEVHPG SVADRDHRLK
ENDQILAIND TPLDQNISHQ QAIALLQQAT GSLRLVVARE VGHTQGRAST SSADTTLPET
VCWGHTEEVE LINDGSGLGF GIVGGKSSGV VVRTIVPGGL ADRDGRLQTG DHILKIGGTN
VQGMTSEQVA QVLRNCGNSV RMLVARDPVG EIAVTPPTPV SLPVALPAVA TRTLDSDRSP
FETYSVELVK KDGQSLGIRI VGYVGTAHPG EASGIYVKSI IPGSAAYHNG QIQVNDKIVA
VDGVNIQGFA NQDVVEVLRN AGQVVHLTLV RRKTSLSASP FEHSSSRETV AEPPKVPERA
GSPKPEANLS VEAEEIGERL DNLKNNTVQA LEKPDVYPEK VPGSPENELK SRWENLLGPD
YEVMVATLDA QIADDEELQK YSKLLPIHTL RLGMEVDSFD GHHYISSVAP GGPVDTLNLL
QPEDELLEVN GMQLYGKSRR EAVSFLKEVP PPFTLVCCRR LFDDEASVDE PRTMEPALLE
AEVDHSVDVN IEDDDDGELA LWSPEVKTVE LVKDCKGLGF SILDYQDPLD PTRSVIVIRS
LVADGVAERS GELLPGDRLV SVNEFSLDNA TLAEAVEVLK AVPPGVVHLG ICKPLVEDEK
EERFSLHSNN NGDSSEPADA VHEIHSSLIL EAPQGFRDEP YLEELVDEPF LDLGKSLQFQ
QKDVDSSSEA WEMHEFLSPP LDGRGEEREM LVDEEYELYQ DHLRAMESNP PPPHIREAAP
ASPVLELQAG TQWLHANLSG GERLECHDAE SMMSAYPQEM QQYSYSTADM MEETFGLDSR
APIPSSEGNG QHGRFDDMGH LHSLTSSSLD LGMMIPSDLQ GPGVLVDLPA VAQRREQEDL
PLYRLPSARV VTKPSSHMGL VSSRHANAAC ELPEREEGEG EETPNFSHWG PPRIVEIFRE
PNVSLGISIV GGQTVIKRLK NGEELKGIFI KQVLEDSPAG KTNALKTGDK ILEVSGVDLQ
NASHAEAVEA IKSAGNPVVF VVQSLSSTPR VIPTVNNKGK TPAPNQDQNT QERKAKRHGT
APPPMKLPPP YRAPSADMEG SEEDCALTDK KIRQRYADLP GELHIIELEK DKNGLGLSLA
GNKDRSRMSI FVVGINPEGP AAADGRMRIG DELLEINNQI LYGRSHQNAS AIIKTAPTRV
KLVFIRNEDA VSQMAVAPFP ELSHSPSPVE DLGGTELVSS EEESSVDAKH LPEPESSKPE
DLSQVVDDNM VAEQQKESES PDSAACQIKQ QTYSTQVSSS SQDSPSSPAP LCQSAHADVT
GSGNFQAPLP VDPAPLSVDP ATCPIVPGQE MIIEISKGRS GLGLSIVGGK DTPLDAIVIH
EVYEEGAAAR DGRLWAGDQI LEVNGVDLRS SSHEEAITAL RQTPQKVRLV VYRDEAQYRD
EENLEVFLVD LQKKTGRGLG LSIVGKRSGS GVFISDIVKG GAADLDGRLI RGDQILSVNG
EDMRHASQET VATILKCVQG LVQLEIGRLR AGSWAASRKT SQNSQGDQHS AHSSCRPSFA
PVITSLQNLV GTKRSSDPPQ KCTEEEPRTV EIIRELSDAL GISIAGGKGS PLGDIPIFIA
MIQANGVAAR TQKLKVGDRI VSINGQPLDG LSHTDAVNLL KNAFGRIILQ VVADTNISAI
ATQLEIMSAG SQLGSPTADR HPEDTEEQMQ RTAD
