ID   PALS1_HUMAN             Reviewed;         675 AA.
AC   Q8N3R9; A1L380; Q7Z631; Q86T98; Q8N7I5; Q9H9Q0;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   28-JUN-2023, entry version 203.
DE   RecName: Full=Protein PALS1 {ECO:0000305};
DE   AltName: Full=MAGUK p55 subfamily member 5;
DE   AltName: Full=Membrane protein, palmitoylated 5 {ECO:0000303|PubMed:16519681};
DE   AltName: Full=Protein associated with Lin-7 1 {ECO:0000303|PubMed:12527193, ECO:0000312|HGNC:HGNC:18669};
GN   Name=PALS1 {ECO:0000303|PubMed:21479189, ECO:0000312|HGNC:HGNC:18669};
GN   Synonyms=MPP5 {ECO:0000303|PubMed:15914641};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skeletal muscle, and Spinal cord;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-441 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 155-675.
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   INTERACTION WITH CRB3 AND PATJ.
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   [6]
RP   COMPLEX FORMATION WITH CRB1 AND MPP4, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15914641; DOI=10.1167/iovs.04-1417;
RA   Kantardzhieva A., Gosens I., Alexeeva S., Punte I.M., Versteeg I.,
RA   Krieger E., Neefjes-Mol C.A., den Hollander A.I., Letteboer S.J.F.,
RA   Klooster J., Cremers F.P.M., Roepman R., Wijnholds J.;
RT   "MPP5 recruits MPP4 to the CRB1 complex in photoreceptors.";
RL   Invest. Ophthalmol. Vis. Sci. 46:2192-2201(2005).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=15558731; DOI=10.1002/cne.20367;
RA   Stoehr H., Molday L.L., Molday R.S., Weber B.H.F., Biedermann B.,
RA   Reichenbach A., Kraemer F.;
RT   "Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with
RT   Veli3 at distinct intercellular junctions of the neurosensory retina.";
RL   J. Comp. Neurol. 481:31-41(2005).
RN   [8]
RP   INTERACTION WITH MPP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17584769; DOI=10.1093/hmg/ddm147;
RA   Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
RA   Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
RA   Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
RT   "MPP1 links the Usher protein network and the Crumbs protein complex in the
RT   retina.";
RL   Hum. Mol. Genet. 16:1993-2003(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX
RP   WITH ARHGAP17; AMOT; PATJ 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   IDENTIFICATION IN A COMPLEX WITH MPP3 AND CRB1, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=16519681; DOI=10.1111/j.1742-4658.2006.05140.x;
RA   Kantardzhieva A., Alexeeva S., Versteeg I., Wijnholds J.;
RT   "MPP3 is recruited to the MPP5 protein scaffold at the retinal outer
RT   limiting membrane.";
RL   FEBS J. 273:1152-1165(2006).
RN   [11]
RP   IDENTIFICATION IN A COMPLEX WITH CRB1 AND EPB41L5, AND INTERACTION WITH
RP   CRB1 AND EPB41L5.
RX   PubMed=17920587; DOI=10.1016/j.yexcr.2007.08.025;
RA   Gosens I., Sessa A., den Hollander A.I., Letteboer S.J.F., Belloni V.,
RA   Arends M.L., Le Bivic A., Cremers F.P.M., Broccoli V., Roepman R.;
RT   "FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity
RT   complex.";
RL   Exp. Cell Res. 313:3959-3970(2007).
RN   [12]
RP   INTERACTION WITH MPP7.
RX   PubMed=17332497; DOI=10.1091/mbc.e06-11-0980;
RA   Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.;
RT   "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates
RT   epithelial tight junction formation.";
RL   Mol. Biol. Cell 18:1744-1755(2007).
RN   [13]
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   [14]
RP   INTERACTION WITH NPHP1 AND NPHP4.
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   [15]
RP   INTERACTION WITH WWTR1.
RX   PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012;
RA   Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K.,
RA   Larsen B.G., Rossant J., Wrana J.L.;
RT   "The Crumbs complex couples cell density sensing to Hippo-dependent control
RT   of the TGF-beta-SMAD pathway.";
RL   Dev. Cell 19:831-844(2010).
RN   [16]
RP   FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV E, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20861307; DOI=10.1091/mbc.e10-04-0338;
RA   Teoh K.T., Siu Y.L., Chan W.L., Schlueter M.A., Liu C.J., Peiris J.S.,
RA   Bruzzone R., Margolis B., Nal B.;
RT   "The SARS coronavirus E protein interacts with PALS1 and alters tight
RT   junction formation and epithelial morphogenesis.";
RL   Mol. Biol. Cell 21:3838-3852(2010).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP   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   [18]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21479189; DOI=10.1371/journal.pone.0018159;
RA   Carvalho G., Poalas K., Demian C., Hatchi E., Vazquez A., Bidere N.;
RT   "Participation of the cell polarity protein PALS1 to T-cell receptor-
RT   mediated NF-kappaB activation.";
RL   PLoS ONE 6:E18159-E18159(2011).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-25 AND SER-83, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
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   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP   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   [21]
RP   FUNCTION, INTERACTION WITH CADH5, AND TISSUE SPECIFICITY.
RX   PubMed=27466317; DOI=10.1091/mbc.e16-02-0127;
RA   Brinkmann B.F., Steinbacher T., Hartmann C., Kummer D., Pajonczyk D.,
RA   Mirzapourshafiyi F., Nakayama M., Weide T., Gerke V., Ebnet K.;
RT   "VE-cadherin interacts with cell polarity protein Pals1 to regulate
RT   vascular lumen formation.";
RL   Mol. Biol. Cell 27:2811-2821(2016).
RN   [22]
RP   INTERACTION WITH SARS-COV-2 E PROTEIN (MICROBIAL INFECTION), AND FUNCTION
RP   (MICROBIAL INFECTION).
RX   PubMed=32891874; DOI=10.1016/j.micinf.2020.08.006;
RA   De Maio F., Lo Cascio E., Babini G., Sali M., Della Longa S., Tilocca B.,
RA   Roncada P., Arcovito A., Sanguinetti M., Scambia G., Urbani A.;
RT   "Improved binding of SARS-CoV-2 Envelope protein to tight junction-
RT   associated PALS1 could play a key role in COVID-19 pathogenesis.";
RL   Microbes Infect. 22:592-597(2020).
RN   [23]
RP   STRUCTURE BY NMR OF 118-177, AND INTERACTION WITH MPDZ.
RX   PubMed=15863617; DOI=10.1073/pnas.0409346102;
RA   Feng W., Long J.-F., Zhang M.;
RT   "A unified assembly mode revealed by the structures of tetrameric L27
RT   domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 119-232 IN COMPLEX WITH MOUSE
RP   LIN7B AND RAT PATJ.
RX   PubMed=22337881; DOI=10.1074/jbc.m111.321216;
RA   Zhang J., Yang X., Wang Z., Zhou H., Xie X., Shen Y., Long J.;
RT   "Structure of an L27 domain heterotrimer from cell polarity complex
RT   Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly mode.";
RL   J. Biol. Chem. 287:11132-11140(2012).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 236-675 IN COMPLEX WITH
RP   DROSOPHILA CRB, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-386.
RX   PubMed=25385611; DOI=10.1073/pnas.1416515111;
RA   Li Y., Wei Z., Yan Y., Wan Q., Du Q., Zhang M.;
RT   "Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem
RT   reveals a highly specific assembly mechanism for the apical Crumbs
RT   complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:17444-17449(2014).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) OF 251-335 IN COMPLEX WITH CRB1, AND
RP   MUTAGENESIS OF PHE-318.
RX   PubMed=25760605; DOI=10.1107/s139900471402776x;
RA   Ivanova M.E., Fletcher G.C., O'Reilly N., Purkiss A.G., Thompson B.J.,
RA   McDonald N.Q.;
RT   "Structures of the human Pals1 PDZ domain with and without ligand suggest
RT   gated access of Crb to the PDZ peptide-binding groove.";
RL   Acta Crystallogr. D 71:555-564(2015).
CC   -!- FUNCTION: Plays a role in tight junction biogenesis and in the
CC       establishment of cell polarity in epithelial cells (PubMed:16678097,
CC       PubMed:25385611). Also involved in adherens junction biogenesis by
CC       ensuring correct localization of the exocyst complex protein EXOC4/SEC8
CC       which allows trafficking of adherens junction structural component CDH1
CC       to the cell surface (By similarity). Plays a role through its
CC       interaction with CDH5 in vascular lumen formation and endothelial
CC       membrane polarity (PubMed:27466317). Required during embryonic and
CC       postnatal retinal development (By similarity). Required for the
CC       maintenance of cerebellar progenitor cells in an undifferentiated
CC       proliferative state, preventing premature differentiation, and is
CC       required for cerebellar histogenesis, fissure formation, cerebellar
CC       layer organization and cortical development (By similarity). Plays a
CC       role in neuronal progenitor cell survival, potentially via promotion of
CC       mTOR signaling (By similarity). Plays a role in the radial and
CC       longitudinal extension of the myelin sheath in Schwann cells (By
CC       similarity). May modulate SC6A1/GAT1-mediated GABA uptake by
CC       stabilizing the transporter (By similarity). Plays a role in the T-cell
CC       receptor-mediated activation of NF-kappa-B (PubMed:21479189). Required
CC       for localization of EZR to the apical membrane of parietal cells and
CC       may play a role in the dynamic remodeling of the apical cytoskeleton
CC       (By similarity). Required for the normal polarized localization of the
CC       vesicular marker STX4 (By similarity). Required for the correct
CC       trafficking of the myelin proteins PMP22 and MAG (By similarity).
CC       Involved in promoting phosphorylation and cytoplasmic retention of
CC       transcriptional coactivators YAP1 and WWTR1/TAZ which leads to
CC       suppression of TGFB1-dependent transcription of target genes such as
CC       CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity).
CC       {ECO:0000250|UniProtKB:B4F7E7, ECO:0000250|UniProtKB:Q9JLB2,
CC       ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:21479189,
CC       ECO:0000269|PubMed:25385611, ECO:0000269|PubMed:27466317}.
CC   -!- FUNCTION: (Microbial infection) Acts as an interaction partner for
CC       human coronaviruses SARS-CoV and, probably, SARS-CoV-2 envelope protein
CC       E which results in delayed formation of tight junctions and
CC       disregulation of cell polarity. {ECO:0000269|PubMed:20861307,
CC       ECO:0000303|PubMed:32891874}.
CC   -!- SUBUNIT: Heterodimer with MPP1 (PubMed:17584769). Forms a
CC       heterotrimeric complex composed of PALS1, LIN7B and PATJ; the N-
CC       terminal L27 domain of PALS1 interacts with the L27 domain of PATJ and
CC       the C-terminal L27 domain of PALS1 interacts with the L27 domain of
CC       LIN7B (PubMed:22337881). Component of a complex composed of PALS1, CRB1
CC       and MPP4 (PubMed:15914641). Component of a complex whose core is
CC       composed of ARHGAP17, AMOT, PALS1, PATJ and PARD3/PAR3
CC       (PubMed:16678097). Component of a complex composed of PALS1, CRB1 and
CC       EPB41L5 (PubMed:17920587). Within the complex, interacts (via HOOK
CC       domain) with EPB41L5 (via FERM domain), and interacts with CRB1 (via
CC       intracellular domain) (PubMed:17920587). Component of a complex
CC       composed of PALS1, MPP3 and CRB1; PALS1 acts as a bridging protein
CC       between MPP3 (via guanylate kinase-like domain) and CRB1
CC       (PubMed:16519681). Component of a complex composed of CRB3, PALS1 and
CC       PATJ (By similarity). Interacts (via PDZ domain) with PATJ (via N-
CC       terminus) (PubMed:12527193). Interacts with EZR (By similarity).
CC       Interacts (via PDZ domain) with CRB1 (via C-terminal ERLI motif)
CC       (PubMed:25385611, PubMed:25760605). While the PDZ domain is sufficient
CC       for interaction with CRB1, the adjacent SH3 and guanylate kinase-like
CC       domains are likely to contribute to a high affinity interaction
CC       (PubMed:25385611). Interacts with WWTR1/TAZ (via WW domain)
CC       (PubMed:21145499). Interacts with MPP7 (PubMed:16678097,
CC       PubMed:17332497). Interacts (via PDZ domain) with CRB3 (via C-terminus)
CC       (By similarity). Interacts with LIN7C (By similarity). Interacts with
CC       MPDZ (By similarity). Interacts with PARD6B (By similarity). Interacts
CC       with SC6A1 (By similarity). Interacts with CDH5; the interaction
CC       promotes PALS1 localization to cell junctions and is required for CDH5-
CC       mediated vascular lumen formation and endothelial cell
CC       (PubMed:27466317). Interacts with NPHP1 (via coiled coil and SH3
CC       domains) (PubMed:19755384). Interacts with NPHP4 (PubMed:19755384).
CC       Interacts with CRB2 (By similarity). {ECO:0000250|UniProtKB:E2QY99,
CC       ECO:0000250|UniProtKB:Q9JLB2, ECO:0000269|PubMed:12527193,
CC       ECO:0000269|PubMed:15914641, ECO:0000269|PubMed:16519681,
CC       ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:17332497,
CC       ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:17920587,
CC       ECO:0000269|PubMed:19755384, ECO:0000269|PubMed:21145499,
CC       ECO:0000269|PubMed:22337881, ECO:0000269|PubMed:25385611,
CC       ECO:0000269|PubMed:25760605, ECO:0000269|PubMed:27466317}.
CC   -!- SUBUNIT: (Microbial infection) Interacts (via PDZ domain) with human
CC       coronaviruses SARS-CoV and, probably, SARS-CoV-2 envelope small
CC       membrane protein E (via C-terminus); this inhibits the interaction
CC       between PALS1 and CRB3. {ECO:0000269|PubMed:20861307,
CC       ECO:0000303|PubMed:32891874}.
CC   -!- INTERACTION:
CC       Q8N3R9; P54252: ATXN3; NbExp=3; IntAct=EBI-2513978, EBI-946046;
CC       Q8N3R9; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-2513978, EBI-11519926;
CC       Q8N3R9; P82279: CRB1; NbExp=5; IntAct=EBI-2513978, EBI-1048648;
CC       Q8N3R9; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-2513978, EBI-12000556;
CC       Q8N3R9; Q9HCM4: EPB41L5; NbExp=4; IntAct=EBI-2513978, EBI-1047162;
CC       Q8N3R9; P22607: FGFR3; NbExp=3; IntAct=EBI-2513978, EBI-348399;
CC       Q8N3R9; O95954: FTCD; NbExp=3; IntAct=EBI-2513978, EBI-10192648;
CC       Q8N3R9; P06396: GSN; NbExp=3; IntAct=EBI-2513978, EBI-351506;
CC       Q8N3R9; P42858: HTT; NbExp=3; IntAct=EBI-2513978, EBI-466029;
CC       Q8N3R9; O14910: LIN7A; NbExp=9; IntAct=EBI-2513978, EBI-2513988;
CC       Q8N3R9; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-2513978, EBI-821335;
CC       Q8N3R9; Q9NUP9: LIN7C; NbExp=4; IntAct=EBI-2513978, EBI-1171517;
CC       Q8N3R9; Q96JB8: MPP4; NbExp=5; IntAct=EBI-2513978, EBI-2483346;
CC       Q8N3R9; Q8N3R9: PALS1; NbExp=2; IntAct=EBI-2513978, EBI-2513978;
CC       Q8N3R9; Q8NI35: PATJ; NbExp=4; IntAct=EBI-2513978, EBI-724390;
CC       Q8N3R9; Q9NY99-2: SNTG2; NbExp=3; IntAct=EBI-2513978, EBI-18173613;
CC       Q8N3R9; A0A286YEY3: SRGAP2B; NbExp=3; IntAct=EBI-2513978, EBI-17766455;
CC       Q8N3R9; Q12933: TRAF2; NbExp=3; IntAct=EBI-2513978, EBI-355744;
CC       Q8N3R9; P02766: TTR; NbExp=3; IntAct=EBI-2513978, EBI-711909;
CC       Q8N3R9; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2513978, EBI-741480;
CC       Q8N3R9; O76024: WFS1; NbExp=3; IntAct=EBI-2513978, EBI-720609;
CC       Q8N3R9; P0DTC4: E; Xeno; NbExp=6; IntAct=EBI-2513978, EBI-25475850;
CC       Q8N3R9; P59637: E; Xeno; NbExp=4; IntAct=EBI-2513978, EBI-25487741;
CC       Q8N3R9-1; PRO_0000021005 [Q9BUF7]: CRB3; NbExp=3; IntAct=EBI-8231026, EBI-25611611;
CC       Q8N3R9-1; P59637: E; Xeno; NbExp=9; IntAct=EBI-8231026, EBI-25487741;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:21479189}.
CC       Cell membrane; Peripheral membrane protein. Endomembrane system;
CC       Peripheral membrane protein. Cell junction, tight junction
CC       {ECO:0000269|PubMed:20861307}. Cell junction, adherens junction
CC       {ECO:0000269|PubMed:16519681}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9JLB2}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q9JLB2}. Apical cell membrane
CC       {ECO:0000269|PubMed:15914641, ECO:0000269|PubMed:16519681,
CC       ECO:0000269|PubMed:25385611}. Note=Localized to the tight junctions of
CC       epithelial cells (By similarity). Localized to the Golgi apparatus in T
CC       lymphocytes (PubMed:21479189). Localized to a subset of intracellular
CC       vesicles (By similarity). Localized to the Purkinje cell body and axon
CC       (By similarity). Localized to intercellular junctions in vascular
CC       endothelial cells (PubMed:27466317). Localized to Schmidt-Lanterman
CC       incisures, the adaxonal domain, and the inner part of paranodal loops
CC       in myelinating Schwann cells of the sciatic nerve (By similarity).
CC       Localized to apical membrane domains of the outer limiting membrane
CC       (OLM) junctions in the retina (By similarity). Colocalizes with CRB1 at
CC       the OLM, apical to the adherens junction (PubMed:15914641). Colocalizes
CC       with MPP1 in the retina at the OLM (PubMed:17584769). Colocalizes with
CC       MPP3 to the subapical region of adherens junctions in the retina OLM
CC       (PubMed:16519681). {ECO:0000250|UniProtKB:Q9JLB2,
CC       ECO:0000269|PubMed:15914641, ECO:0000269|PubMed:16519681,
CC       ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:21479189,
CC       ECO:0000269|PubMed:27466317}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment {ECO:0000269|PubMed:20861307}. Golgi apparatus
CC       {ECO:0000269|PubMed:20861307}. Note=(Microbial infection) Following
CC       infection by human SARS coronavirus, partially localized at the site of
CC       viral replication; the endoplasmic reticulum-Golgi intermediate
CC       compartment, reducing its levels at cell-cell contacts which results in
CC       delayed formation of tight junctions and affects establishment of cell
CC       polarity. {ECO:0000269|PubMed:20861307}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N3R9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N3R9-2; Sequence=VSP_014002;
CC   -!- TISSUE SPECIFICITY: Expressed at the outer limiting membrane in the
CC       retina (at protein level) (PubMed:15914641, PubMed:15558731,
CC       PubMed:16519681, PubMed:17584769). Expressed in T lymphocytes (at
CC       protein level) (PubMed:21479189). Expressed in the kidney (at protein
CC       level) (PubMed:17584769). {ECO:0000269|PubMed:15558731,
CC       ECO:0000269|PubMed:15914641, ECO:0000269|PubMed:16519681,
CC       ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:21479189}.
CC   -!- DOMAIN: The L27 domain 1 functions in targeting to the tight junctions
CC       by binding to and stabilizing PATJ. {ECO:0000250|UniProtKB:Q9JLB2}.
CC   -!- DOMAIN: The PDZ domain binds to the C-terminus of SC6A1.
CC       {ECO:0000250|UniProtKB:Q9JLB2}.
CC   -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH53366.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAB14172.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL832326; CAD38620.1; -; mRNA.
DR   EMBL; AL832578; CAD89937.1; -; mRNA.
DR   EMBL; CH471061; EAW80930.1; -; Genomic_DNA.
DR   EMBL; BC053366; AAH53366.1; ALT_SEQ; mRNA.
DR   EMBL; BC129933; AAI29934.1; -; mRNA.
DR   EMBL; AK022677; BAB14172.1; ALT_INIT; mRNA.
DR   EMBL; AK098373; BAC05295.1; -; mRNA.
DR   CCDS; CCDS58325.1; -. [Q8N3R9-2]
DR   CCDS; CCDS9779.1; -. [Q8N3R9-1]
DR   RefSeq; NP_001243479.1; NM_001256550.1. [Q8N3R9-2]
DR   RefSeq; NP_071919.2; NM_022474.3. [Q8N3R9-1]
DR   RefSeq; XP_005268060.1; XM_005268003.1. [Q8N3R9-2]
DR   RefSeq; XP_011535388.1; XM_011537086.2. [Q8N3R9-1]
DR   RefSeq; XP_011535389.1; XM_011537087.2. [Q8N3R9-1]
DR   PDB; 1Y76; NMR; -; B/D=118-177.
DR   PDB; 3UIT; X-ray; 2.05 A; A/B/C/D=119-232.
DR   PDB; 4UU5; X-ray; 1.23 A; A=251-335.
DR   PDB; 4UU6; X-ray; 1.80 A; A=251-335.
DR   PDB; 4WSI; X-ray; 2.95 A; A/B=236-675.
DR   PDB; 7M4R; EM; 3.65 A; A/B=236-675.
DR   PDB; 7NTJ; X-ray; 1.74 A; A/B=255-336.
DR   PDB; 7NTK; X-ray; 1.90 A; A/B/D/F=255-336.
DR   PDB; 7QCS; X-ray; 2.80 A; A/B/E=238-336.
DR   PDBsum; 1Y76; -.
DR   PDBsum; 3UIT; -.
DR   PDBsum; 4UU5; -.
DR   PDBsum; 4UU6; -.
DR   PDBsum; 4WSI; -.
DR   PDBsum; 7M4R; -.
DR   PDBsum; 7NTJ; -.
DR   PDBsum; 7NTK; -.
DR   PDBsum; 7QCS; -.
DR   AlphaFoldDB; Q8N3R9; -.
DR   BMRB; Q8N3R9; -.
DR   SMR; Q8N3R9; -.
DR   BioGRID; 122155; 84.
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; Q8N3R9; -.
DR   IntAct; Q8N3R9; 74.
DR   MINT; Q8N3R9; -.
DR   STRING; 9606.ENSP00000261681; -.
DR   GlyGen; Q8N3R9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N3R9; -.
DR   PhosphoSitePlus; Q8N3R9; -.
DR   SwissPalm; Q8N3R9; -.
DR   BioMuta; MPP5; -.
DR   DMDM; 116242632; -.
DR   EPD; Q8N3R9; -.
DR   jPOST; Q8N3R9; -.
DR   MassIVE; Q8N3R9; -.
DR   MaxQB; Q8N3R9; -.
DR   PaxDb; Q8N3R9; -.
DR   PeptideAtlas; Q8N3R9; -.
DR   ProteomicsDB; 71827; -. [Q8N3R9-1]
DR   ProteomicsDB; 71828; -. [Q8N3R9-2]
DR   Antibodypedia; 20; 378 antibodies from 38 providers.
DR   DNASU; 64398; -.
DR   Ensembl; ENST00000261681.9; ENSP00000261681.4; ENSG00000072415.10. [Q8N3R9-1]
DR   Ensembl; ENST00000555925.5; ENSP00000451488.1; ENSG00000072415.10. [Q8N3R9-2]
DR   Ensembl; ENST00000676464.1; ENSP00000503713.1; ENSG00000072415.10. [Q8N3R9-1]
DR   Ensembl; ENST00000677382.1; ENSP00000503322.1; ENSG00000072415.10. [Q8N3R9-1]
DR   Ensembl; ENST00000677835.1; ENSP00000503517.1; ENSG00000072415.10. [Q8N3R9-1]
DR   Ensembl; ENST00000678380.1; ENSP00000503321.1; ENSG00000072415.10. [Q8N3R9-1]
DR   GeneID; 64398; -.
DR   KEGG; hsa:64398; -.
DR   MANE-Select; ENST00000261681.9; ENSP00000261681.4; NM_022474.4; NP_071919.2.
DR   UCSC; uc001xjc.5; human. [Q8N3R9-1]
DR   AGR; HGNC:18669; -.
DR   CTD; 64398; -.
DR   DisGeNET; 64398; -.
DR   GeneCards; PALS1; -.
DR   HGNC; HGNC:18669; PALS1.
DR   HPA; ENSG00000072415; Low tissue specificity.
DR   MalaCards; PALS1; -.
DR   MIM; 606958; gene.
DR   neXtProt; NX_Q8N3R9; -.
DR   OpenTargets; ENSG00000072415; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   VEuPathDB; HostDB:ENSG00000072415; -.
DR   eggNOG; KOG0609; Eukaryota.
DR   GeneTree; ENSGT00940000156087; -.
DR   HOGENOM; CLU_001715_5_4_1; -.
DR   InParanoid; Q8N3R9; -.
DR   OMA; NNEADRF; -.
DR   OrthoDB; 2873706at2759; -.
DR   PhylomeDB; Q8N3R9; -.
DR   TreeFam; TF314263; -.
DR   PathwayCommons; Q8N3R9; -.
DR   Reactome; R-HSA-420029; Tight junction interactions.
DR   Reactome; R-HSA-9692912; SARS-CoV-1 targets PDZ proteins in cell-cell junction.
DR   Reactome; R-HSA-9705677; SARS-CoV-2 targets PDZ proteins in cell-cell junction.
DR   SignaLink; Q8N3R9; -.
DR   SIGNOR; Q8N3R9; -.
DR   BioGRID-ORCS; 64398; 21 hits in 1160 CRISPR screens.
DR   ChiTaRS; MPP5; human.
DR   EvolutionaryTrace; Q8N3R9; -.
DR   GeneWiki; MPP5; -.
DR   GenomeRNAi; 64398; -.
DR   Pharos; Q8N3R9; Tbio.
DR   PRO; PR:Q8N3R9; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q8N3R9; protein.
DR   Bgee; ENSG00000072415; Expressed in jejunal mucosa and 187 other tissues.
DR   ExpressionAtlas; Q8N3R9; baseline and differential.
DR   Genevisible; Q8N3R9; HS.
DR   GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR   GO; GO:0043296; C:apical junction complex; NAS:ComplexPortal.
DR   GO; GO:0016324; C:apical plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR   GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR   GO; GO:0021954; P:central nervous system neuron development; ISS:UniProtKB.
DR   GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR   GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IBA:GO_Central.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0048699; P:generation of neurons; IBA:GO_Central.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:UniProtKB.
DR   GO; GO:0032288; P:myelin assembly; IEA:Ensembl.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR   GO; GO:0035750; P:protein localization to myelin sheath abaxonal region; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd12036; SH3_MPP5; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.287.650; L27 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR004172; L27_dom.
DR   InterPro; IPR036892; L27_dom_sf.
DR   InterPro; IPR015145; L27_N.
DR   InterPro; IPR035601; MPP5_SH3.
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   PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR   PANTHER; PTHR23122:SF14; PROTEIN PALS1; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF09060; L27_N; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF101288; L27 domain; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell junction;
KW   Cell membrane; Cell projection; Golgi apparatus; Host-virus interaction;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   SH3 domain; Tight junction.
FT   CHAIN           1..675
FT                   /note="Protein PALS1"
FT                   /id="PRO_0000094580"
FT   DOMAIN          120..177
FT                   /note="L27 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT   DOMAIN          179..235
FT                   /note="L27 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT   DOMAIN          256..336
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          345..417
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          479..660
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   REGION          1..345
FT                   /note="Required for the correct localization of PALS1 and
FT                   PATJ at cell-cell contacts and the normal formation of
FT                   tight junctions and adherens junctions"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          21..140
FT                   /note="Interaction with PARD6B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT   REGION          51..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..243
FT                   /note="Interaction with LIN7C"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT   COMPBIAS        10..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         486..493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..34
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_014002"
FT   MUTAGEN         318
FT                   /note="F->A,C: Increases interaction with CRB1."
FT                   /evidence="ECO:0000269|PubMed:25760605"
FT   MUTAGEN         386
FT                   /note="D->K: Reduces binding to Drosophila crb and causes
FT                   incorrect PALS1 localization and cell polarity."
FT                   /evidence="ECO:0000269|PubMed:25385611"
FT   CONFLICT        100
FT                   /note="D -> G (in Ref. 1; CAD38620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="S -> Y (in Ref. 1; CAD89937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="N -> S (in Ref. 4; BAC05295)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="M -> L (in Ref. 4; BAC05295)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="Q -> H (in Ref. 1; CAD89937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="N -> H (in Ref. 1; CAD89937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        490
FT                   /note="C -> F (in Ref. 4; BAB14172)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        613
FT                   /note="G -> V (in Ref. 1; CAD38620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        634
FT                   /note="N -> S (in Ref. 1; CAD38620)"
FT                   /evidence="ECO:0000305"
FT   HELIX           124..137
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   HELIX           141..155
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   HELIX           157..173
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   HELIX           186..197
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   TURN            198..200
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   HELIX           203..213
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   HELIX           215..229
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:3UIT"
FT   STRAND          249..251
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          255..261
FT                   /evidence="ECO:0007829|PDB:4UU5"
FT   STRAND          268..274
FT                   /evidence="ECO:0007829|PDB:4UU5"
FT   STRAND          277..283
FT                   /evidence="ECO:0007829|PDB:4UU5"
FT   HELIX           288..292
FT                   /evidence="ECO:0007829|PDB:4UU5"
FT   STRAND          300..304
FT                   /evidence="ECO:0007829|PDB:4UU5"
FT   HELIX           314..322
FT                   /evidence="ECO:0007829|PDB:4UU5"
FT   STRAND          326..333
FT                   /evidence="ECO:0007829|PDB:4UU5"
FT   STRAND          348..352
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           367..369
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          378..383
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          389..394
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          405..408
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          464..472
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          482..486
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   TURN            488..491
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           492..502
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   TURN            503..506
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   TURN            524..527
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           533..541
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          545..551
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          554..559
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           560..567
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   TURN            568..570
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          571..576
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           579..581
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           582..586
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          593..598
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           602..608
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           621..631
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           634..636
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          639..644
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           648..660
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   TURN            661..664
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   STRAND          667..670
FT                   /evidence="ECO:0007829|PDB:4WSI"
FT   HELIX           671..673
FT                   /evidence="ECO:0007829|PDB:4WSI"
SQ   SEQUENCE   675 AA;  77294 MW;  A3B2CB594E0908CA CRC64;
     MTTSHMNGHV TEESDSEVKN VDLASPEEHQ KHREMAVDCP GDLGTRMMPI RRSAQLERIR
     QQQEDMRRRR EEEGKKQELD LNSSMRLKKL AQIPPKTGID NPMFDTEEGI VLESPHYAVK
     ILEIEDLFSS LKHIQHTLVD SQSQEDISLL LQLVQNKDFQ NAFKIHNAIT VHMNKASPPF
     PLISNAQDLA QEVQTVLKPV HHKEGQELTA LLNTPHIQAL LLAHDKVAEQ EMQLEPITDE
     RVYESIGQYG GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE
     VLEINGIEIR GKDVNEVFDL LSDMHGTLTF VLIPSQQIKP PPAKETVIHV KAHFDYDPSD
     DPYVPCRELG LSFQKGDILH VISQEDPNWW QAYREGDEDN QPLAGLVPGK SFQQQREAMK
     QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY NANKNDDYDN EEILTYEEMS LYHQPANRKR
     PIILIGPQNC GQNELRQRLM NKEKDRFASA VPHTTRSRRD QEVAGRDYHF VSRQAFEADI
     AAGKFIEHGE FEKNLYGTSI DSVRQVINSG KICLLSLRTQ SLKTLRNSDL KPYIIFIAPP
     SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK AYQELLRLIN
     KLDTEPQWVP STWLR
//