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 27-MAR-2024, entry version 207. 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; 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; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-2513978, EBI-11519926; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 EMDB; EMD-23665; -. DR SMR; Q8N3R9; -. DR BioGRID; 122155; 87. 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; 76. 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; 9606-ENSP00000261681; -. DR PeptideAtlas; Q8N3R9; -. DR ProteomicsDB; 71827; -. [Q8N3R9-1] DR ProteomicsDB; 71828; -. [Q8N3R9-2] DR Pumba; Q8N3R9; -. DR Antibodypedia; 20; 389 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 189 other cell types or tissues. DR ExpressionAtlas; Q8N3R9; baseline and differential. 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. DR Genevisible; Q8N3R9; HS. 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 //