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};
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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 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 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
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