MPDZ_MOUSE
ID MPDZ_MOUSE Reviewed; 2055 AA.
AC Q8VBX6; B7ZNA1; O08783; Q6P7U4; Q80ZY8; Q8BKJ1; Q8C0H8; Q8VBV5; Q8VBY0;
AC Q9Z1K3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Multiple PDZ domain protein;
DE AltName: Full=Multi-PDZ domain protein 1;
GN Name=Mpdz; Synonyms=Mupp1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6 X CBA; TISSUE=Brain;
RX PubMed=10395806; DOI=10.1006/geno.1999.5853;
RA Simpson E.H., Suffolk R., Jackson I.J.;
RT "Identification, sequence, and mapping of mouse multiple PDZ domain protein
RT gene, Mpdz.";
RL Genomics 59:102-104(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-541; VAL-691;
RP ARG-801; ALA-859; ASN-880; SER-914; VAL-977; MET-1338; ASN-1433 AND
RP ASN-1767.
RC STRAIN=129/J, A/HeJ, AKR/J, BALB/cJ, C3H/J, C57BL/6J, C57BR/cdJ, C57L/J,
RC CBA/J, CE/J, DBA/2J, DBA1/J, PL/J, SJL/J, SWR/J, WSP1, WSP2, WSR1, and
RC WSR2; TISSUE=Brain;
RX PubMed=11978849; DOI=10.1523/jneurosci.22-09-03730.2002;
RA Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT "Congenic mapping of alcohol and pentobarbital withdrawal liability loci to
RT a <1 centimorgan interval of murine chromosome 4: identification of Mpdz as
RT a candidate gene.";
RL J. Neurosci. 22:3730-3738(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1532-2055 (ISOFORM 4).
RC TISSUE=Pancreas;
RX PubMed=9192623; DOI=10.1073/pnas.94.13.6670;
RA Lee S.S., Weiss R.S., Javier R.T.;
RT "Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of
RT the Drosophila discs large tumor suppressor protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-62 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Testis;
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 [7]
RP INTERACTION WITH KIT, AND TISSUE SPECIFICITY.
RX PubMed=11018522; DOI=10.1016/s0014-5793(00)02036-6;
RA Mancini A., Koch A., Stefan M., Niemann H., Tamura T.;
RT "The direct association of the multiple PDZ domain containing proteins
RT (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase
RT activity.";
RL FEBS Lett. 482:54-58(2000).
RN [8]
RP INTERACTION WITH NG2.
RX PubMed=10967549;
RX DOI=10.1002/1097-4644(20001101)79:2<213::aid-jcb50>3.0.co;2-g;
RA Barritt D.S., Pearn M.T., Zisch A.H., Lee S.S., Javier R.T., Pasquale E.B.,
RA Stallcup W.B.;
RT "The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the
RT membrane-spanning proteoglycan NG2.";
RL J. Cell. Biochem. 79:213-224(2000).
RN [9]
RP INTERACTION WITH ADENOVIRUS TYPE 9 E4-ORF1 PROTEIN.
RX PubMed=11000240; DOI=10.1128/jvi.74.20.9680-9693.2000;
RA Lee S.S., Glaunsinger B., Mantovani F., Banks L., Javier R.T.;
RT "Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus
RT E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins.";
RL J. Virol. 74:9680-9693(2000).
RN [10]
RP INTERACTION WITH CLDN1 AND F11R, DOMAINS, AND SUBCELLULAR LOCATION.
RX PubMed=11689568; DOI=10.1074/jbc.m109005200;
RA Hamazaki Y., Itoh M., Sasaki H., Furuse M., Tsukita S.;
RT "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions
RT through its possible interaction with claudin-1 and junctional adhesion
RT molecule.";
RL J. Biol. Chem. 277:455-461(2002).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12403818; DOI=10.1083/jcb.200207050;
RA Poliak S., Matlis S., Ullmer C., Scherer S.S., Peles E.;
RT "Distinct claudins and associated PDZ proteins form different autotypic
RT tight junctions in myelinating Schwann cells.";
RL J. Cell Biol. 159:361-372(2002).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=12706259; DOI=10.1016/s0006-8993(03)02338-2;
RA Sitek B., Poschmann G., Schmidtke K., Ullmer C., Maskri L., Andriske M.,
RA Stichel C.C., Zhu X.-R., Luebbert H.;
RT "Expression of MUPP1 protein in mouse brain.";
RL Brain Res. 970:178-187(2003).
RN [13]
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 [14]
RP INTERACTION WITH CXADR, AND DOMAIN.
RX PubMed=15364909; DOI=10.1074/jbc.m409061200;
RA Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.;
RT "The coxsackievirus and adenovirus receptor interacts with the multi-PDZ
RT domain protein-1 (MUPP-1) within the tight junction.";
RL J. Biol. Chem. 279:48079-48084(2004).
RN [15]
RP INTERACTION WITH CRB1; PALS1 AND MPP4, AND SUBCELLULAR LOCATION.
RX PubMed=15316081; DOI=10.1242/jcs.01301;
RA van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J.,
RA Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W., Rashbass P.,
RA Le Bivic A., Wijnholds J.;
RT "Crumbs homologue 1 is required for maintenance of photoreceptor cell
RT polarization and adhesion during light exposure.";
RL J. Cell Sci. 117:4169-4177(2004).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [17]
RP INTERACTION WITH FAT4.
RX PubMed=19506035; DOI=10.1083/jcb.200811030;
RA Ishiuchi T., Misaki K., Yonemura S., Takeichi M., Tanoue T.;
RT "Mammalian Fat and Dachsous cadherins regulate apical membrane organization
RT in the embryonic cerebral cortex.";
RL J. Cell Biol. 185:959-967(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, and Lung;
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 [19]
RP DEVELOPMENTAL STAGE.
RX PubMed=23001562; DOI=10.1093/hmg/dds398;
RA Alves C.H., Sanz A.S., Park B., Pellissier L.P., Tanimoto N., Beck S.C.,
RA Huber G., Murtaza M., Richard F., Sridevi Gurubaran I., Garcia Garrido M.,
RA Levelt C.N., Rashbass P., Le Bivic A., Seeliger M.W., Wijnholds J.;
RT "Loss of CRB2 in the mouse retina mimics human retinitis pigmentosa due to
RT mutations in the CRB1 gene.";
RL Hum. Mol. Genet. 22:35-50(2013).
RN [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Member of the NMDAR signaling complex that may play a role in
CC control of AMPAR potentiation and synaptic plasticity in excitatory
CC synapses (By similarity). Promotes clustering of HT2RC at the cell
CC surface (By similarity). {ECO:0000250|UniProtKB:O55164,
CC ECO:0000250|UniProtKB:O75970}.
CC -!- SUBUNIT: Interacts with CLDN5, DLG4, GRIN1, SYNGAP1, CAMK2A and CAMK2B,
CC HTR2A, HTR2B, HTR2C, PLEKHA1/TAPP1 and PLEKHA2/TAPP2 (By similarity).
CC Interacts with F11R/JAM, CLDN1, NG2, CXADR, CRB1, MPP4 and PALS1.
CC Interacts with FAT4 (via cytoplasmic domain). Interacts with DLL1
CC (PubMed:15509766). {ECO:0000250, ECO:0000269|PubMed:10967549,
CC ECO:0000269|PubMed:11000240, ECO:0000269|PubMed:11018522,
CC ECO:0000269|PubMed:11689568, ECO:0000269|PubMed:15316081,
CC ECO:0000269|PubMed:15364909, ECO:0000269|PubMed:15509766,
CC ECO:0000269|PubMed:19506035}.
CC -!- INTERACTION:
CC Q8VBX6; O88551: Cldn1; NbExp=2; IntAct=EBI-8026435, EBI-7158428;
CC Q8VBX6; P10721: KIT; Xeno; NbExp=4; IntAct=EBI-8026435, EBI-1379503;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Apical cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Postsynaptic density. Cell projection, dendrite. Cell
CC junction, tight junction {ECO:0000250}. Synapse. Synapse, synaptosome
CC {ECO:0000250}. Note=Colocalizes with HTR2C on the apical membrane of
CC epithelial choroid plexus cells. Highly enriched in postsynaptic
CC densities (PSD) (By similarity). Localized to punctae on dendrites of
CC hippocampal neurons and colocalizes with the synaptic marker DLG4.
CC Enriched at the tight junctions of epithelial cells. Association to the
CC tight junctions depends on CXADR (By similarity). In the retina,
CC localizes to the sub-apical region adjacent to the adherens junction
CC complex at the outer limiting membrane. Localized mainly in the
CC Schmidt-Lanterman incisures of myelinating Schwann cells. {ECO:0000250,
CC ECO:0000250|UniProtKB:O55164}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8VBX6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VBX6-2; Sequence=VSP_014201;
CC Name=3;
CC IsoId=Q8VBX6-3; Sequence=VSP_058771;
CC Name=4;
CC IsoId=Q8VBX6-4; Sequence=VSP_014202;
CC -!- TISSUE SPECIFICITY: In the brain, it is strongly expressed in the
CC choroid plexus. Within the hippocampal formation, strongest expression
CC was seen in the soma of CA1-4 pyramidal cells. Expressed in most
CC neocortical regions with the strongest expression in piriform cortex
CC and amygdaloid nuclei but also detected in the subiculum and olfactory
CC bulb. In the cerebellum, the highest level of expression was found in
CC Purkinje cells. Moderately expressed in the granular layer and
CC molecular layer. Expressed in the pontine nuclei, parts of spinal
CC trigeminal nuclei, and the principal sensory trigeminal nuclei of the
CC metencephalon. Expressed in all thalamic and hypothalamic nuclei, and
CC the substantia nigra (at protein level). Ubiquitously expressed.
CC {ECO:0000269|PubMed:11018522, ECO:0000269|PubMed:12706259}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the outer limiting membrane of the
CC retina at 3 months of age. {ECO:0000269|PubMed:23001562}.
CC -!- DOMAIN: The PDZ domain 2 mainly binds CAMK2A and CAMK2B. The PDZ
CC domains 7 and 10 bind the Ad9 E4-ORF1 oncoprotein. The PDZ domain 10
CC binds the C-terminal PDZ-binding motif of HTR2C. The PDZ domains 10 and
CC 13 bind PLEKHA1 and PLEKHA2. The PDZ domain 13 binds SYNGAP1 (By
CC similarity). The PDZ domain 1 binds NG2. The PDZ domain 9 binds F11R.
CC The PDZ domain 10 binds the C-terminus of CLDN1 and KIT. The PDZ domain
CC 13 binds CXADR. {ECO:0000250, ECO:0000269|PubMed:11689568,
CC ECO:0000269|PubMed:15364909}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27346.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC34766.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AJ131869; CAA10523.1; -; mRNA.
DR EMBL; AF326526; AAL37372.1; -; mRNA.
DR EMBL; AF326527; AAL37373.1; -; mRNA.
DR EMBL; AF326528; AAL37374.1; -; mRNA.
DR EMBL; AF326529; AAL37375.1; -; mRNA.
DR EMBL; AF326530; AAL37376.1; -; mRNA.
DR EMBL; AF326531; AAL37377.2; -; mRNA.
DR EMBL; AF326532; AAL37378.1; -; mRNA.
DR EMBL; AF326533; AAL37379.1; -; mRNA.
DR EMBL; AF326534; AAL37380.1; -; mRNA.
DR EMBL; AF326535; AAL37381.1; -; mRNA.
DR EMBL; AF326536; AAL37382.1; -; mRNA.
DR EMBL; AF326537; AAL37383.1; -; mRNA.
DR EMBL; AF326538; AAL37384.1; -; mRNA.
DR EMBL; AF326539; AAL37385.1; -; mRNA.
DR EMBL; AF326540; AAL37386.1; -; mRNA.
DR EMBL; AF326541; AAL37387.1; -; mRNA.
DR EMBL; AF326542; AAL37388.1; -; mRNA.
DR EMBL; AF326543; AAL37389.1; -; mRNA.
DR EMBL; AF326544; AAL37390.1; -; mRNA.
DR EMBL; AL670939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR352325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061504; AAH61504.1; -; mRNA.
DR EMBL; BC145117; AAI45118.1; -; mRNA.
DR EMBL; AF000168; AAB57835.1; -; mRNA.
DR EMBL; AK031321; BAC27346.1; ALT_FRAME; mRNA.
DR EMBL; AK051782; BAC34766.1; ALT_SEQ; mRNA.
DR CCDS; CCDS18292.1; -. [Q8VBX6-1]
DR CCDS; CCDS89767.1; -. [Q8VBX6-2]
DR PIR; T30259; T30259.
DR RefSeq; NP_001292213.1; NM_001305284.1.
DR RefSeq; NP_001292215.1; NM_001305286.1. [Q8VBX6-2]
DR RefSeq; NP_034950.2; NM_010820.3. [Q8VBX6-1]
DR PDB; 4XH7; X-ray; 1.65 A; A=521-665.
DR PDBsum; 4XH7; -.
DR AlphaFoldDB; Q8VBX6; -.
DR SMR; Q8VBX6; -.
DR BioGRID; 201476; 15.
DR CORUM; Q8VBX6; -.
DR DIP; DIP-41165N; -.
DR IntAct; Q8VBX6; 11.
DR MINT; Q8VBX6; -.
DR STRING; 10090.ENSMUSP00000099894; -.
DR ChEMBL; CHEMBL2176783; -.
DR iPTMnet; Q8VBX6; -.
DR PhosphoSitePlus; Q8VBX6; -.
DR EPD; Q8VBX6; -.
DR jPOST; Q8VBX6; -.
DR MaxQB; Q8VBX6; -.
DR PaxDb; Q8VBX6; -.
DR PRIDE; Q8VBX6; -.
DR ProteomicsDB; 252603; -. [Q8VBX6-1]
DR ProteomicsDB; 252604; -. [Q8VBX6-2]
DR ProteomicsDB; 252605; -. [Q8VBX6-3]
DR ProteomicsDB; 252606; -. [Q8VBX6-4]
DR Antibodypedia; 4615; 89 antibodies from 19 providers.
DR DNASU; 17475; -.
DR Ensembl; ENSMUST00000102830; ENSMUSP00000099894; ENSMUSG00000028402. [Q8VBX6-1]
DR Ensembl; ENSMUST00000107258; ENSMUSP00000102879; ENSMUSG00000028402. [Q8VBX6-2]
DR GeneID; 17475; -.
DR KEGG; mmu:17475; -.
DR UCSC; uc008tjw.3; mouse. [Q8VBX6-2]
DR UCSC; uc008tjx.2; mouse. [Q8VBX6-1]
DR CTD; 8777; -.
DR MGI; MGI:1343489; Mpdz.
DR VEuPathDB; HostDB:ENSMUSG00000028402; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155586; -.
DR HOGENOM; CLU_002378_0_0_1; -.
DR InParanoid; Q8VBX6; -.
DR OrthoDB; 1419918at2759; -.
DR TreeFam; TF330709; -.
DR BioGRID-ORCS; 17475; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Mpdz; mouse.
DR PRO; PR:Q8VBX6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VBX6; protein.
DR Bgee; ENSMUSG00000028402; Expressed in ureter smooth muscle and 260 other tissues.
DR ExpressionAtlas; Q8VBX6; baseline and differential.
DR Genevisible; Q8VBX6; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
DR GO; GO:0035003; C:subapical complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:0042552; P:myelination; ISO:MGI.
DR Gene3D; 2.30.42.10; -; 13.
DR InterPro; IPR015132; L27_2.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR032078; MPDZ.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF09045; L27_2; 1.
DR Pfam; PF16667; MPDZ_u10; 1.
DR Pfam; PF00595; PDZ; 13.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 13.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50156; SSF50156; 13.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 13.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Membrane; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Synaptosome; Tight junction.
FT CHAIN 1..2055
FT /note="Multiple PDZ domain protein"
FT /id="PRO_0000094595"
FT DOMAIN 1..63
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 138..225
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 258..338
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 378..464
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 546..627
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 693..779
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 996..1077
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1139..1231
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1338..1421
FT /note="PDZ 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1471..1552
FT /note="PDZ 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1614..1697
FT /note="PDZ 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1710..1792
FT /note="PDZ 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1847..1933
FT /note="PDZ 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1972..2055
FT /note="PDZ 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 348..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75970"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75970"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75970"
FT MOD_RES 1158
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1803
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75970"
FT MOD_RES 1809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55164"
FT VAR_SEQ 1..1908
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_058771"
FT VAR_SEQ 1236..1268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014201"
FT VAR_SEQ 1714
FT /note="Q -> QLQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9192623"
FT /id="VSP_014202"
FT VARIANT 541
FT /note="N -> S (in strain: DBA/2J and DBA1/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 691
FT /note="G -> V (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 801
FT /note="H -> R (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 859
FT /note="T -> A (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 880
FT /note="S -> N (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 914
FT /note="R -> S (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 977
FT /note="A -> V (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 1338
FT /note="V -> M (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 1433
FT /note="I -> N (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT VARIANT 1767
FT /note="H -> N (in strain: DBA/2J, DBA1/J, CE/J, A/HeJ,
FT BALB/cJ, C57Br/cdJ, C57L/J, WSP2 and 129/J)"
FT /evidence="ECO:0000269|PubMed:11978849"
FT CONFLICT 583
FT /note="S -> N (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="S -> N (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="P -> S (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 909..910
FT /note="PP -> SS (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 914..919
FT /note="RPAPTS -> KPTPTF (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="V -> G (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 937..938
FT /note="EC -> QW (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 952
FT /note="S -> N (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 956
FT /note="S -> F (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="P -> S (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="P -> A (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="Q -> P (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 974..975
FT /note="SS -> TF (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="N -> T (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="T -> P (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 1532
FT /note="K -> N (in Ref. 5; AAB57835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1547
FT /note="T -> I (in Ref. 5; AAB57835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1589
FT /note="T -> P (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 1616..1617
FT /note="EI -> GV (in Ref. 5; AAB57835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1691
FT /note="L -> V (in Ref. 5; AAB57835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1844
FT /note="G -> R (in Ref. 5; AAB57835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1914
FT /note="A -> V (in Ref. 4; AAH61504)"
FT /evidence="ECO:0000305"
FT CONFLICT 1968
FT /note="P -> S (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT CONFLICT 1983..1985
FT /note="GFS -> SFN (in Ref. 1; CAA10523)"
FT /evidence="ECO:0000305"
FT HELIX 521..538
FT /evidence="ECO:0007829|PDB:4XH7"
FT STRAND 542..550
FT /evidence="ECO:0007829|PDB:4XH7"
FT STRAND 559..565
FT /evidence="ECO:0007829|PDB:4XH7"
FT STRAND 568..574
FT /evidence="ECO:0007829|PDB:4XH7"
FT HELIX 579..583
FT /evidence="ECO:0007829|PDB:4XH7"
FT STRAND 591..595
FT /evidence="ECO:0007829|PDB:4XH7"
FT HELIX 605..613
FT /evidence="ECO:0007829|PDB:4XH7"
FT STRAND 617..626
FT /evidence="ECO:0007829|PDB:4XH7"
SQ SEQUENCE 2055 AA; 218711 MW; 26EA94B814214B69 CRC64;
MLETIDKNRA LQAAERLQSK LKERGDVANE DKLSLLKSVL QSPLFSQILN LQTSLQQLKD
QVNIATLATA AADHAHTPQF SSAVISNLQS ESLLLSPNHG NLEALPGPGA PAVMDGKPTC
DELDQLIKNM AQGRHVEIFE LLKPPCGGLG FSVVGLRSEN RGELGIFVQE IQEGSVAHRD
GRLKETDQIL AINGQVLDQT ITHQQAISIL QKAKDTVQLV IARGSLPPVS SPRISRSPSA
ASTISAHSNP MHWQHVETIE LVNDGSGLGF GIIGGKATGV IVKTILPGGV ADQHGRLCSG
DHILKIGDTD LAGMSSEQVA QVLRQCGNRV KLMIARGAVE ETPASSSLGI TLSSSTSSTS
EMRVDASTQK NDESETFDVE LTKNVQGLGI TIAGYIGDKK LEPSGIFVKS ITKSSAVEHD
GRIQIGDQII AVDGTNLQGF TNQQAVEVLR HTGQTVRLTL MRKGASQEAE LTSRGDTAKD
VDLPAENCEK DEESLSLKRN TSILPIEEEG FPLLSAELEE AEDVQQEAAL LTKWQRIMGI
NYEIVVAHVS KFSENSGLGI SLEATVGHHF IRSVLPEGPV GHSGKLFSGD ELLEVNGINL
LGENHQDVVN ILKELPIDVT MVCCRRTVPP IALSEMDSLD INDLELTEKP HIDLGEFIGS
SETEDPMLAM SDVDQNAEEI QTPLAMWEAG GQSIELEKGS RGLGFSILDY QDPIDPANTV
IVIRSLVPGG IAEKDGRLFP GDRLMFVNDI NLENSTLEEA VEALKGAPSG MVRIGVAKPL
PLSPEEGYVS AKEDAFLCSP HACKESGLSD KALFRADLAL IDTPDAESIA ESRFESQFSP
DNDSVYSTQA SIFSLHDGTC SDGMNYGPSL PSSPPKDVTS SSEVVLGLHL SLEELYTQNL
LQRQHAGSPP TDMRPAPTSG FPISDYTTTN AVEQKYECAN PVAWPHSQLP SSLSTSELAP
ALPAVAQKYL TDQSSLASDA ESVNLQSMSQ EAFERTVTIA KGSSSLGMTV SANKDGLGVI
VRSIIHGGAI SRDGRIAVGD CILSINEEST ISLTNAQARA MLRRHSLIGP DIKITYVPAE
HLEEFRVSFG QQAGGIMALD IFSSYTGRDI PELPEREEGE GEESELQNAA YSSWSQPRRV
ELWREPSKSL GISIVGGRGM GSRLSNGEVM RGIFIKHVLE DSPAGKNGTL KPGDRIIEVD
GMDLRDASHE QAVEAIRKAG NPVVFMVQSI INRPRKSPLP SLPHSLYPKY SFSSTNPFAD
SLQLTTDQAP SQSESETEKP ALCNVPPSSP SVFSEMGSDC AQPSATAVSE DEDKEDEFGY
SWKNIQERYG SLTGQLHVIE LEKGQSGLGL SLAGNKDRTR MSVFIVGIDP TGAAGRDGRL
QIADELLEIN GQILYGRSHQ NASSIIKCAP SKVKIIFIRN ADAVNQMAVC PGIAADSPSS
TSDSPQNKEV EPCSTTSASA ADLSSLTDVY QLELPKDQGG LGIAICEEDT INGVMIESLT
EHGGAAKDGR LKPGDHILAV DDEVVAGCPV EKFISLLKTA KATVKLTVRA ENPACPAVPS
SAVTVSGERK DNSQTPAVPA PDLEPIPSTS RSSTPAVFAS DPATCPIIPG CETTIEISKG
QTGLGLSIVG GSDTLLGAII IHEVYEEGAA CKDGRLWAGD QILEVNGIDL RKATHDEAIN
VLRQTPQRVR LTLYRDEAPY KEEDVCDTFT IELQKRPGKG LGLSIVGKRN DTGVFVSDIV
KGGIADADGR LMQGDQILMV NGEDVRHATQ EAVAALLKCS LGAVTLEVGR VKAAPFHSER
RPSQSSQVSE SSLSSFTPPL SGINTSESLE SNSKKNALAS EIQGLRTVEI KKGPADSLGL
SIAGGVGSPL GDVPIFIAMM HPNGVAAQTQ KLRVGDRIVT ICGTSTDGMT HTQAVNLMKN
ASGSIEVQVV AGGDVSVVTG HQQELANPCL AFTGLTSSSI FPDDLGPPQS KTITLDRGPD
GLGFSIVGGY GSPHGDLPIY VKTVFAKGAA AEDGRLKRGD QIIAVNGQSL EGVTHEEAVA
ILKRTKGTVT LMVLS
