MAGI2_MOUSE
ID MAGI2_MOUSE Reviewed; 1275 AA.
AC Q9WVQ1; Q3UH81; Q6GT88; Q8BYT1; Q8CA85;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2;
DE AltName: Full=Activin receptor-interacting protein 1;
DE Short=Acvrip1;
DE AltName: Full=Atrophin-1-interacting protein 1;
DE Short=AIP-1;
DE AltName: Full=Membrane-associated guanylate kinase inverted 2;
DE Short=MAGI-2;
GN Name=Magi2; Synonyms=Acvrinp1, Aip1, Arip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP SMAD2; SMAD3 AND ACVR2A, AND IDENTIFICATION IN A COMPLEX WITH ACVR2A;
RP ACVR1B AND SMAD3.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10681527; DOI=10.1074/jbc.275.8.5485;
RA Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z.,
RA Nakamura T., Sugino H.;
RT "Identification and characterization of a PDZ protein that interacts with
RT activin types II receptors.";
RL J. Biol. Chem. 275:5485-5492(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 INTERACTION WITH DLL1.
RX PubMed=15509766; DOI=10.1242/dev.01417;
RA Wright G.J., Leslie J.D., Ariza-McNaughton L., Lewis J.;
RT "Delta proteins and MAGI proteins: an interaction of Notch ligands with
RT intracellular scaffolding molecules and its significance for zebrafish
RT development.";
RL Development 131:5659-5669(2004).
RN [5]
RP INTERACTION WITH HTR2A.
RX PubMed=14988405; DOI=10.1074/jbc.m312106200;
RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A.,
RA Bockaert J., Marin P.;
RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of
RT PDZ proteins.";
RL J. Biol. Chem. 279:20257-20266(2004).
RN [6]
RP INTERACTION WITH HTR4.
RX PubMed=15466885; DOI=10.1242/jcs.01379;
RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA Marin P., Dumuis A., Bockaert J.;
RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT receptor splice variant: roles in receptor targeting.";
RL J. Cell Sci. 117:5367-5379(2004).
RN [7]
RP INTERACTION WITH IGSF9.
RX PubMed=15340156; DOI=10.1073/pnas.0405371101;
RA Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.;
RT "The immunoglobulin family member dendrite arborization and synapse
RT maturation 1 (Dasm1) controls excitatory synapse maturation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361 AND TYR-826, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361 AND SER-1013, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH IGSF9B AND NLGN2.
RX PubMed=23751499; DOI=10.1083/jcb.201209132;
RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J.,
RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S.,
RA Craig A.M., Kim E.;
RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to
RT promote inhibitory synapse development.";
RL J. Cell Biol. 201:929-944(2013).
RN [11]
RP FUNCTION, INTERACTION WITH USH1G, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF SER-1152.
RX PubMed=24608321; DOI=10.1093/hmg/ddu104;
RA Bauss K., Knapp B., Jores P., Roepman R., Kremer H., Wijk E.V., Maerker T.,
RA Wolfrum U.;
RT "Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-
RT mediated endocytosis.";
RL Hum. Mol. Genet. 23:3923-3942(2014).
CC -!- FUNCTION: Seems to act as a scaffold molecule at synaptic junctions by
CC assembling neurotransmitter receptors and cell adhesion proteins (By
CC similarity). Plays a role in nerve growth factor (NGF)-induced
CC recruitment of RAPGEF2 to late endosomes and neurite outgrowth (By
CC similarity). May play a role in regulating activin-mediated signaling
CC in neuronal cells (PubMed:10681527). Enhances the ability of PTEN to
CC suppress AKT1 activation (By similarity). Plays a role in receptor-
CC mediated clathrin-dependent endocytosis which is required for
CC ciliogenesis (PubMed:24608321). {ECO:0000250|UniProtKB:O88382,
CC ECO:0000250|UniProtKB:Q86UL8, ECO:0000269|PubMed:10681527,
CC ECO:0000269|PubMed:24608321}.
CC -!- SUBUNIT: Interacts (via its WW domains) with DRPLA (By similarity).
CC Interacts (via its second PDZ domain) with PTEN (via unphosphorylated
CC C-terminus); this interaction diminishes the degradation rate of PTEN
CC (By similarity). Interacts (via guanylate kinase domain) with DLGAP1
CC (By similarity). Interacts (via the PDZ domains) with GRIN2A, GRID2 and
CC NLGN1 (By similarity). Interacts with CTNND2, CTNNB1 and MAGUIN-1 (By
CC similarity). Interacts with ACVR2A, SMAD2 and SMAD3 (PubMed:10681527).
CC Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3
CC (PubMed:10681527). May interact with HTR2A (PubMed:14988405). Interacts
CC with RAPGEF2 (By similarity). Identified in a complex with ACTN4, CASK,
CC IQGAP1, NPHS1, SPTAN1 and SPTBN1 (By similarity). Interacts with DDN
CC (By similarity). Found in a complex, at least composed of KIDINS220,
CC MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late
CC endosomes in a NGF-dependent manner (By similarity). Interacts with
CC RAPGEF2; the interaction occurs before or after nerve growth factor
CC (NGF) stimulation (By similarity). Interacts (via PDZ domain) with
CC KIDINS220 (via C-terminal domain) (By similarity). Interacts with IGSF9
CC and HTR4 (PubMed:15466885, PubMed:15340156). Interacts with DLL1
CC (PubMed:15509766). Found in a complex with IGSF9B and NLGN2; the
CC interaction with IGSF9B is mediated via the PDZ 5 and PDZ 6 domains,
CC while the interaction with NLGN2 is mediated via the WW1, WW2 and PDZ2
CC domains (PubMed:23751499). Interacts (via PDZ 6 domain) with USH1G (via
CC SAM domain); the interaction is triggered by phosphorylation of USH1G
CC by CK2 and negatively regulates MAGI2-mediated endocytosis
CC (PubMed:24608321). {ECO:0000250|UniProtKB:O88382,
CC ECO:0000269|PubMed:10681527, ECO:0000269|PubMed:14988405,
CC ECO:0000269|PubMed:15340156, ECO:0000269|PubMed:15466885,
CC ECO:0000269|PubMed:15509766, ECO:0000269|PubMed:23751499,
CC ECO:0000269|PubMed:24608321}.
CC -!- INTERACTION:
CC Q9WVQ1; Q61483: Dll1; NbExp=3; IntAct=EBI-297151, EBI-297125;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Late endosome
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:24608321}. Cell projection, cilium
CC {ECO:0000269|PubMed:24608321}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:24608321}.
CC Photoreceptor inner segment {ECO:0000269|PubMed:24608321}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:24608321}. Note=Localized diffusely in the
CC cytoplasm before nerve growth factor (NGF) stimulation. Recruited to
CC late endosomes after NGF stimulation. Membrane-associated in
CC synaptosomes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=long;
CC IsoId=Q9WVQ1-1; Sequence=Displayed;
CC Name=2; Synonyms=short;
CC IsoId=Q9WVQ1-2; Sequence=VSP_008436;
CC Name=3;
CC IsoId=Q9WVQ1-3; Sequence=VSP_018580, VSP_008437;
CC Name=4;
CC IsoId=Q9WVQ1-4; Sequence=VSP_008436, VSP_018581;
CC -!- TISSUE SPECIFICITY: Expressed throughout the retina except in the
CC nuclear layers and the photoreceptor outer segments (at protein level)
CC (PubMed:24608321). Highest retinal expression is observed in the outer
CC plexiform layer, the outer limiting membrane and the inner segment of
CC photoreceptor cells (at protein level) (PubMed:24608321). Expressed in
CC brain. {ECO:0000269|PubMed:24608321}.
CC -!- MISCELLANEOUS: [Isoform 2]: Major. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AB029485; BAA82294.1; -; mRNA.
DR EMBL; AK039336; BAC30321.1; -; mRNA.
DR EMBL; AK147530; BAE27976.1; -; mRNA.
DR EMBL; BC059005; AAH59005.1; -; mRNA.
DR CCDS; CCDS39019.1; -. [Q9WVQ1-2]
DR CCDS; CCDS51424.1; -. [Q9WVQ1-1]
DR CCDS; CCDS51425.1; -. [Q9WVQ1-4]
DR RefSeq; NP_001164216.1; NM_001170745.1. [Q9WVQ1-4]
DR RefSeq; NP_001164217.1; NM_001170746.1. [Q9WVQ1-1]
DR RefSeq; NP_056638.1; NM_015823.3. [Q9WVQ1-2]
DR PDB; 6JJZ; X-ray; 1.65 A; A/B=295-390.
DR PDB; 6KKG; X-ray; 2.15 A; A/B=295-390.
DR PDB; 7D6F; X-ray; 2.70 A; A=914-1010.
DR PDBsum; 6JJZ; -.
DR PDBsum; 6KKG; -.
DR PDBsum; 7D6F; -.
DR AlphaFoldDB; Q9WVQ1; -.
DR SMR; Q9WVQ1; -.
DR BioGRID; 206123; 14.
DR CORUM; Q9WVQ1; -.
DR IntAct; Q9WVQ1; 3.
DR MINT; Q9WVQ1; -.
DR STRING; 10090.ENSMUSP00000085872; -.
DR iPTMnet; Q9WVQ1; -.
DR PhosphoSitePlus; Q9WVQ1; -.
DR MaxQB; Q9WVQ1; -.
DR PaxDb; Q9WVQ1; -.
DR PeptideAtlas; Q9WVQ1; -.
DR PRIDE; Q9WVQ1; -.
DR ProteomicsDB; 292077; -. [Q9WVQ1-1]
DR ProteomicsDB; 292078; -. [Q9WVQ1-2]
DR ProteomicsDB; 292079; -. [Q9WVQ1-3]
DR ProteomicsDB; 292080; -. [Q9WVQ1-4]
DR Antibodypedia; 2880; 247 antibodies from 33 providers.
DR Ensembl; ENSMUST00000088516; ENSMUSP00000085872; ENSMUSG00000040003. [Q9WVQ1-1]
DR Ensembl; ENSMUST00000101558; ENSMUSP00000099094; ENSMUSG00000040003. [Q9WVQ1-4]
DR Ensembl; ENSMUST00000115267; ENSMUSP00000110922; ENSMUSG00000040003. [Q9WVQ1-2]
DR Ensembl; ENSMUST00000197553; ENSMUSP00000146769; ENSMUSG00000040003. [Q9WVQ1-3]
DR GeneID; 50791; -.
DR KEGG; mmu:50791; -.
DR UCSC; uc008wnv.2; mouse. [Q9WVQ1-1]
DR UCSC; uc008wnw.2; mouse. [Q9WVQ1-4]
DR UCSC; uc008wnx.1; mouse. [Q9WVQ1-3]
DR CTD; 9863; -.
DR MGI; MGI:1354953; Magi2.
DR VEuPathDB; HostDB:ENSMUSG00000040003; -.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000155057; -.
DR HOGENOM; CLU_004562_1_0_1; -.
DR InParanoid; Q9WVQ1; -.
DR OMA; LPQNIPY; -.
DR PhylomeDB; Q9WVQ1; -.
DR TreeFam; TF316816; -.
DR BioGRID-ORCS; 50791; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Magi2; mouse.
DR PRO; PR:Q9WVQ1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WVQ1; protein.
DR Bgee; ENSMUSG00000040003; Expressed in rostral migratory stream and 201 other tissues.
DR ExpressionAtlas; Q9WVQ1; baseline and differential.
DR Genevisible; Q9WVQ1; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0070697; F:activin receptor binding; IPI:MGI.
DR GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:MGI.
DR GO; GO:0098879; F:structural constituent of postsynaptic specialization; ISO:MGI.
DR GO; GO:0070699; F:type II activin receptor binding; IPI:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IDA:BHF-UCL.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IPI:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR030036; MAGI2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316:SF27; PTHR10316:SF27; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 6.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 6.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF50156; SSF50156; 6.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Endocytosis; Endosome; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..1275
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 2"
FT /id="PRO_0000094587"
FT DOMAIN 17..101
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 109..283
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 301..334
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 347..380
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 425..509
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 604..682
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 777..859
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 919..1009
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1139..1221
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 203..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..380
FT /note="Interaction with DDN"
FT /evidence="ECO:0000250"
FT REGION 698..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 361
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88382"
FT MOD_RES 826
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88382"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88382"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..390
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018580"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10681527,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_008436"
FT VAR_SEQ 756..770
FT /note="QQVPPRTSFRMDSSG -> R (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018581"
FT VAR_SEQ 1229..1275
FT /note="MVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGVLPLPPPQACRK -> A
FT FHSFLHLCSAFSVF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008437"
FT MUTAGEN 1152
FT /note="S->A: Does not affect interaction with USH1G."
FT /evidence="ECO:0000269|PubMed:24608321"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6JJZ"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6JJZ"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:6JJZ"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:6JJZ"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:6JJZ"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6JJZ"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:6JJZ"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:6JJZ"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6JJZ"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:6JJZ"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:6JJZ"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:6JJZ"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:6JJZ"
FT STRAND 918..923
FT /evidence="ECO:0007829|PDB:7D6F"
FT STRAND 926..928
FT /evidence="ECO:0007829|PDB:7D6F"
FT STRAND 932..936
FT /evidence="ECO:0007829|PDB:7D6F"
FT STRAND 952..956
FT /evidence="ECO:0007829|PDB:7D6F"
FT HELIX 961..965
FT /evidence="ECO:0007829|PDB:7D6F"
FT STRAND 976..979
FT /evidence="ECO:0007829|PDB:7D6F"
FT HELIX 987..995
FT /evidence="ECO:0007829|PDB:7D6F"
FT STRAND 999..1005
FT /evidence="ECO:0007829|PDB:7D6F"
SQ SEQUENCE 1275 AA; 140919 MW; F17DC52517806354 CRC64;
MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL
VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS
VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EEFMELEKSG ALLESGTYED
NYYGTPKPPA EPAPLLNVTD QILPGATPSA EGKRKRNKSV TNMEKASIEP PEEEEEERPV
VNGNGVVITP ESSEHEDKSA GASGETPSQP YPAPVYSQPE ELKDQMDDTK PTKPEENEDS
DPLPDNWEMA YTEKGEVYFI DHNTKTTSWL DPRLAKKAKP PEECKENELP YGWEKIDDPI
YGTYYVDHIN RRTQFENPVL EAKRKLQQHN MPHTELGAKP LQAPGFREKP LFTRDASQLK
GTFLSTTLKK SNMGFGFTII GGDEPDEFLQ VKSVIPDGPA AQDGKMETGD VIVYINEVCV
LGHTHADVVK LFQSVPIGQS VNLVLCRGYP LPFDPEDPAN SMVPPLAIME RPPPVMVNGR
HNYETYLEYI SRTSQSVPDI TDRPPHSLHS MPADGQLDGT YPPPVHDDNV SMASSGATQA
ELMTLTIVKG AQGFGFTIAD SPTGQRVKQI LDIQGCPGLC EGDLIVEINQ QNVQNLSHTE
VVDILKDCPV GSETSLIIHR GGFFSPWKTP KPMMDRWENQ GSPQTSLSAP AVPQNLPFPP
ALHRSSFPDS TEAFDPRKPD PYELYEKSRA IYESRQQVPP RTSFRMDSSG PDYKELDVHL
RRMESGFGFR ILGGDEPGQP ILIGAVIAMG SADRDGRLHP GDELVYVDGI PVAGKTHRYV
IDLMHHAARN GQVNLTVRRK VLCGGEPCPE NGRSPGSVST HHSSPRSDYA TYSNSNHAAP
SSNASPPEGF ASHSLQTSDV VIHRKENEGF GFVIISSLNR PESGATITVP HKIGRIIDGS
PADRCAKLKV GDRILAVNGQ SIINMPHADI VKLIKDAGLS VTLRIIPQEE LNSPTSAPSS
EKQSPMAQQH SPLAQQSPLA QPSPATPNSP VAQPAPPQPL QLQGHENSYR SEVKARQDVK
PDIRQPPFTD YRQPPLDYRQ PPGGDYSQPP PLDYRQHSPD TRQYPLSDYR QPQDFDYFTV
DMEKGAKGFG FSIRGGREYK MDLYVLRLAE DGPAIRNGRM RVGDQIIEIN GESTRDMTHA
RAIELIKSGG RRVRLLLKRG TGQVPEYGMV PSSLSMCMKS DKHGSPYFYL LGHPKDTTNP
TPGVLPLPPP QACRK
