MPP7_HUMAN
ID MPP7_HUMAN Reviewed; 576 AA.
AC Q5T2T1; B2RCC9; B4DWL9; B5MDZ3; D3DRW3; Q5T2T0; Q8IY28;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=MAGUK p55 subfamily member 7;
GN Name=MPP7;
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), AND VARIANT
RP ARG-322.
RC TISSUE=Hippocampus, and Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-322.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-322.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION.
RX PubMed=14719143;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human MPP7 gene and mouse Mpp7 gene
RT in silico.";
RL Int. J. Mol. Med. 13:333-338(2004).
RN [6]
RP INTERACTION WITH PATJ AND PALS1.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH DLG1; LIN7A; LIN7B AND LIN7C.
RX PubMed=17237226; DOI=10.1074/jbc.m610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7 and
RT DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=17616219; DOI=10.1021/pr070245b;
RA Ngai H.-H., Sit W.-H., Jiang P.-P., Thongboonkerd V., Wan J.-M.;
RT "Markedly increased urinary preprohaptoglobin and haptoglobin in passive
RT Heymann nephritis: a differential proteomics approach.";
RL J. Proteome Res. 6:3313-3320(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH DLG1 AND PALS1, AND MUTAGENESIS OF LEU-38 AND LEU-95.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, 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 [12]
RP SUBCELLULAR LOCATION, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=26481050; DOI=10.1016/j.devcel.2015.09.016;
RA Bailey M.J., Prehoda K.E.;
RT "Establishment of Par-Polarized Cortical Domains via Phosphoregulated
RT Membrane Motifs.";
RL Dev. Cell 35:199-210(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 7-120 IN COMPLEX WITH DLG1 AND
RP LIN7C, AND SUBUNIT.
RX PubMed=20702775; DOI=10.1096/fj.10-163857;
RA Yang X., Xie X., Chen L., Zhou H., Wang Z., Zhao W., Tian R., Zhang R.,
RA Tian C., Long J., Shen Y.;
RT "Structural basis for tandem L27 domain-mediated polymerization.";
RL FASEB J. 24:4806-4815(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 135-225.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the PDZ domain of mpp7.";
RL Submitted (AUG-2010) to the PDB data bank.
CC -!- FUNCTION: Acts as an important adapter that promotes epithelial cell
CC polarity and tight junction formation via its interaction with DLG1.
CC Involved in the assembly of protein complexes at sites of cell-cell
CC contact. {ECO:0000269|PubMed:17332497}.
CC -!- SUBUNIT: Heterodimer; able to heterodimerize via its C-terminal L27
CC domain with LIN7A, LIN7B and LIN7C. Forms a tripartite complex composed
CC of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with DLG1 via its N-
CC terminal L27 domain. Interacts with PALS1 and PATJ.
CC {ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:17237226,
CC ECO:0000269|PubMed:17332497, ECO:0000269|PubMed:20702775}.
CC -!- INTERACTION:
CC Q5T2T1; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-2514004, EBI-12000556;
CC Q5T2T1; O75506: HSBP1; NbExp=3; IntAct=EBI-2514004, EBI-748664;
CC Q5T2T1; O14910: LIN7A; NbExp=9; IntAct=EBI-2514004, EBI-2513988;
CC Q5T2T1; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-2514004, EBI-821335;
CC Q5T2T1; Q9NUP9: LIN7C; NbExp=4; IntAct=EBI-2514004, EBI-1171517;
CC Q5T2T1; Q5VVJ2: MYSM1; NbExp=3; IntAct=EBI-2514004, EBI-12262412;
CC Q5T2T1; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-2514004, EBI-12840050;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:17332497}. Lateral cell membrane; Peripheral
CC membrane protein {ECO:0000269|PubMed:17332497}. Cell junction, tight
CC junction {ECO:0000269|PubMed:17237226, ECO:0000269|PubMed:17332497}.
CC Cell junction, adherens junction {ECO:0000269|PubMed:17237226,
CC ECO:0000269|PubMed:17332497}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:26481050}. Cytoplasm {ECO:0000269|PubMed:26481050}.
CC Note=In epidermal cells, detected primarily at the lateral cell
CC membrane. {ECO:0000269|PubMed:17332497}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T2T1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T2T1-2; Sequence=VSP_056065, VSP_056066, VSP_056067;
CC -!- INDUCTION: Down-regulated in patients suffering of passive Heymann
CC nephritis (at protein level). {ECO:0000269|PubMed:17616219}.
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC sufficient and important for interaction with phospholipids permitting
CC cortical localization (PubMed:26481050). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (PubMed:26481050). {ECO:0000269|PubMed:26481050}.
CC -!- PTM: Phosphorylated by aPKC which promotes dissociation from the cell
CC cortex. {ECO:0000269|PubMed:26481050}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AK301592; BAG63081.1; -; mRNA.
DR EMBL; AK315046; BAG37526.1; -; mRNA.
DR EMBL; AL355501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86045.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86047.1; -; Genomic_DNA.
DR EMBL; BC038105; AAH38105.1; -; mRNA.
DR CCDS; CCDS7158.1; -. [Q5T2T1-1]
DR RefSeq; NP_001305099.1; NM_001318170.1. [Q5T2T1-1]
DR RefSeq; NP_775767.2; NM_173496.4. [Q5T2T1-1]
DR RefSeq; XP_011517639.1; XM_011519337.2. [Q5T2T1-1]
DR PDB; 3LRA; X-ray; 2.95 A; A=9-120.
DR PDB; 3O46; X-ray; 1.30 A; A=135-225.
DR PDBsum; 3LRA; -.
DR PDBsum; 3O46; -.
DR AlphaFoldDB; Q5T2T1; -.
DR SMR; Q5T2T1; -.
DR BioGRID; 126785; 123.
DR CORUM; Q5T2T1; -.
DR IntAct; Q5T2T1; 29.
DR MINT; Q5T2T1; -.
DR STRING; 9606.ENSP00000337907; -.
DR GlyGen; Q5T2T1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T2T1; -.
DR PhosphoSitePlus; Q5T2T1; -.
DR BioMuta; MPP7; -.
DR DMDM; 74762233; -.
DR EPD; Q5T2T1; -.
DR jPOST; Q5T2T1; -.
DR MassIVE; Q5T2T1; -.
DR MaxQB; Q5T2T1; -.
DR PaxDb; Q5T2T1; -.
DR PeptideAtlas; Q5T2T1; -.
DR PRIDE; Q5T2T1; -.
DR ProteomicsDB; 5357; -.
DR ProteomicsDB; 64359; -. [Q5T2T1-1]
DR Antibodypedia; 26125; 107 antibodies from 24 providers.
DR DNASU; 143098; -.
DR Ensembl; ENST00000337532.9; ENSP00000337907.5; ENSG00000150054.19. [Q5T2T1-1]
DR Ensembl; ENST00000375719.7; ENSP00000364871.3; ENSG00000150054.19. [Q5T2T1-1]
DR Ensembl; ENST00000375732.5; ENSP00000364884.1; ENSG00000150054.19. [Q5T2T1-1]
DR Ensembl; ENST00000683449.1; ENSP00000507917.1; ENSG00000150054.19. [Q5T2T1-1]
DR GeneID; 143098; -.
DR KEGG; hsa:143098; -.
DR MANE-Select; ENST00000683449.1; ENSP00000507917.1; NM_001318170.2; NP_001305099.1.
DR UCSC; uc001iua.2; human. [Q5T2T1-1]
DR CTD; 143098; -.
DR DisGeNET; 143098; -.
DR GeneCards; MPP7; -.
DR HGNC; HGNC:26542; MPP7.
DR HPA; ENSG00000150054; Tissue enhanced (esophagus).
DR MIM; 610973; gene.
DR neXtProt; NX_Q5T2T1; -.
DR OpenTargets; ENSG00000150054; -.
DR PharmGKB; PA134985345; -.
DR VEuPathDB; HostDB:ENSG00000150054; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000156232; -.
DR HOGENOM; CLU_001715_5_0_1; -.
DR InParanoid; Q5T2T1; -.
DR OMA; CDMLAAV; -.
DR OrthoDB; 531106at2759; -.
DR PhylomeDB; Q5T2T1; -.
DR TreeFam; TF314263; -.
DR PathwayCommons; Q5T2T1; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q5T2T1; -.
DR BioGRID-ORCS; 143098; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; MPP7; human.
DR EvolutionaryTrace; Q5T2T1; -.
DR GenomeRNAi; 143098; -.
DR Pharos; Q5T2T1; Tbio.
DR PRO; PR:Q5T2T1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5T2T1; protein.
DR Bgee; ENSG00000150054; Expressed in palpebral conjunctiva and 173 other tissues.
DR ExpressionAtlas; Q5T2T1; baseline and differential.
DR Genevisible; Q5T2T1; HS.
DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL.
DR GO; GO:0005923; C:bicellular tight junction; IDA:BHF-UCL.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
DR GO; GO:0035591; F:signaling adaptor activity; TAS:BHF-UCL.
DR GO; GO:0070830; P:bicellular tight junction assembly; IDA:BHF-UCL.
DR GO; GO:0030010; P:establishment of cell polarity; TAS:BHF-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:BHF-UCL.
DR CDD; cd12033; SH3_MPP7; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00515; -.
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; IPR035599; MPP7_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 Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Cell junction; Cell membrane;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain; Tight junction.
FT CHAIN 1..576
FT /note="MAGUK p55 subfamily member 7"
FT /id="PRO_0000320027"
FT DOMAIN 10..65
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 67..122
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 139..220
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 228..298
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 368..560
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 289..383
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000269|PubMed:26481050"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056065"
FT VAR_SEQ 470..499
FT /note="TVKHLRTLEFKPYVIFIKPPSIERLRETRK -> GPWFLLPLMAVPWGAKPP
FT NARMTCGSPLDL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056066"
FT VAR_SEQ 500..576
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056067"
FT VARIANT 322
FT /note="K -> R (in dbSNP:rs2997211)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_039110"
FT MUTAGEN 38
FT /note="L->S: Abolishes interaction with DLG1."
FT /evidence="ECO:0000269|PubMed:17332497"
FT MUTAGEN 95
FT /note="L->S: Does not affect the interaction with DLG1."
FT /evidence="ECO:0000269|PubMed:17332497"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:3LRA"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:3LRA"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3LRA"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:3O46"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3O46"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3O46"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:3O46"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:3O46"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3O46"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3O46"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:3O46"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:3O46"
SQ SEQUENCE 576 AA; 65524 MW; 86366E460A08C6A7 CRC64;
MPALSTGSGS DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL VKIHEKLHYY
EKQSPVPILH GAAALADDLA EELQNKPLNS EIRELLKLLS KPNVKALLSV HDTVAQKNYD
PVLPPMPEDI DDEEDSVKII RLVKNREPLG ATIKKDEQTG AIIVARIMRG GAADRSGLIH
VGDELREVNG IPVEDKRPEE IIQILAQSQG AITFKIIPGS KEETPSKEGK MFIKALFDYN
PNEDKAIPCK EAGLSFKKGD ILQIMSQDDA TWWQAKHEAD ANPRAGLIPS KHFQERRLAL
RRPEILVQPL KVSNRKSSGF RKSFRLSRKD KKTNKSMYEC KKSDQYDTAD VPTYEEVTPY
RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV PHTTRARRSQ ESDGVEYIFI
SKHLFETDVQ NNKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK
PYVIFIKPPS IERLRETRKN AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MESQYGHLFD
KIIINDDLTV AFNELKTTFD KLETETHWVP VSWLHS
