MPP2_MOUSE
ID MPP2_MOUSE Reviewed; 552 AA.
AC Q9WV34; B1AQF8; Q3T9W1; Q3TT52; Q3URK8;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=MAGUK p55 subfamily member 2;
DE AltName: Full=Discs large homolog 2;
DE AltName: Full=Protein MPP2;
GN Name=Mpp2 {ECO:0000312|MGI:MGI:1858257}; Synonyms=Dlgh2;
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).
RA Lin L., Chishti A.H.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pituitary, Spinal cord, and Spleen;
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 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 1).
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 [5]
RP PROTEIN SEQUENCE OF 38-46 AND 378-387, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-117 AND SER-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP KCNN2.
RX PubMed=26880549; DOI=10.7554/elife.12637;
RA Kim G., Lujan R., Schwenk J., Kelley M.H., Aguado C., Watanabe M.,
RA Fakler B., Maylie J., Adelman J.P.;
RT "Membrane palmitoylated protein 2 is a synaptic scaffold protein required
RT for synaptic SK2-containing channel function.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell
CC adhesion molecules to core components of the postsynaptic density (By
CC similarity). In CA1 pyramidal neurons, required for synaptic KCNN2-
CC containing channel function and long-term potentiation expression
CC (PubMed:26880549). Seems to negatively regulate SRC function in
CC epithelial cells (By similarity). {ECO:0000250|UniProtKB:D3ZAA9,
CC ECO:0000250|UniProtKB:Q14168, ECO:0000269|PubMed:26880549}.
CC -!- SUBUNIT: Can homomultimerise. Interacts with CACNG2. Interacts (via the
CC SH3-Guanylate kinase-like sub-module) with DLG4/PSD95 and DLGAP1/GKAP.
CC Interacts (via the PDZ domain) with CADM1 (via C-terminus) (By
CC similarity). Interacts with KCNN2/SK2 (via N-terminal domain)
CC (PubMed:26880549). Interacts with SRC (By similarity).
CC {ECO:0000250|UniProtKB:D3ZAA9, ECO:0000250|UniProtKB:Q14168,
CC ECO:0000269|PubMed:26880549}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000269|PubMed:26880549}. Postsynaptic density
CC {ECO:0000269|PubMed:26880549}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q14168}. Membrane
CC {ECO:0000250|UniProtKB:Q14168}. Note=Prominently expressed in the
CC postsynaptic densities of dendritic spines, is also detected in
CC dendritic shafts. {ECO:0000269|PubMed:26880549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WV34-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WV34-2; Sequence=VSP_022952;
CC -!- TISSUE SPECIFICITY: Expressed in pyramidal neurons of CA1 region of the
CC hippocampus. {ECO:0000269|PubMed:26880549}.
CC -!- PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:Q14168}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AF162685; AAD44342.1; -; mRNA.
DR EMBL; AK141422; BAE24680.1; -; mRNA.
DR EMBL; AK161577; BAE36473.1; -; mRNA.
DR EMBL; AK172253; BAE42909.1; -; mRNA.
DR EMBL; AL591145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053026; AAH53026.1; -; mRNA.
DR CCDS; CCDS25485.1; -. [Q9WV34-1]
DR CCDS; CCDS88261.1; -. [Q9WV34-2]
DR RefSeq; NP_057904.1; NM_016695.3. [Q9WV34-1]
DR RefSeq; XP_006533746.1; XM_006533683.3.
DR RefSeq; XP_006533747.1; XM_006533684.3. [Q9WV34-1]
DR RefSeq; XP_006533748.1; XM_006533685.3. [Q9WV34-1]
DR AlphaFoldDB; Q9WV34; -.
DR BMRB; Q9WV34; -.
DR SMR; Q9WV34; -.
DR BioGRID; 206171; 5.
DR IntAct; Q9WV34; 5.
DR MINT; Q9WV34; -.
DR STRING; 10090.ENSMUSP00000017458; -.
DR iPTMnet; Q9WV34; -.
DR PhosphoSitePlus; Q9WV34; -.
DR SwissPalm; Q9WV34; -.
DR EPD; Q9WV34; -.
DR MaxQB; Q9WV34; -.
DR PaxDb; Q9WV34; -.
DR PeptideAtlas; Q9WV34; -.
DR PRIDE; Q9WV34; -.
DR ProteomicsDB; 290303; -. [Q9WV34-1]
DR ProteomicsDB; 290304; -. [Q9WV34-2]
DR Antibodypedia; 17305; 222 antibodies from 26 providers.
DR DNASU; 50997; -.
DR Ensembl; ENSMUST00000017458; ENSMUSP00000017458; ENSMUSG00000017314. [Q9WV34-1]
DR Ensembl; ENSMUST00000100398; ENSMUSP00000097967; ENSMUSG00000017314. [Q9WV34-2]
DR GeneID; 50997; -.
DR KEGG; mmu:50997; -.
DR UCSC; uc007lqk.2; mouse. [Q9WV34-2]
DR UCSC; uc007lql.2; mouse. [Q9WV34-1]
DR CTD; 4355; -.
DR MGI; MGI:1858257; Mpp2.
DR VEuPathDB; HostDB:ENSMUSG00000017314; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000155348; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; Q9WV34; -.
DR OMA; NDNMERT; -.
DR OrthoDB; 847888at2759; -.
DR PhylomeDB; Q9WV34; -.
DR TreeFam; TF314263; -.
DR BioGRID-ORCS; 50997; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mpp2; mouse.
DR PRO; PR:Q9WV34; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WV34; protein.
DR Bgee; ENSMUSG00000017314; Expressed in dentate gyrus of hippocampal formation granule cell and 123 other tissues.
DR Genevisible; Q9WV34; MM.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR CDD; cd12037; SH3_MPP2; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR035602; MPP2_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; 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; 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 Alternative splicing; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Synapse.
FT CHAIN 1..552
FT /note="MAGUK p55 subfamily member 2"
FT /id="PRO_0000094574"
FT DOMAIN 8..59
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 60..118
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 140..219
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 225..293
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 350..537
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZAA9"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..10
FT /note="MPVAATNSES -> MACSPGSEGSLEGISLGSSEEAELRRE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022952"
FT CONFLICT 215
FT /note="I -> T (in Ref. 2; BAE42909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 61555 MW; E932CD208309E0FA CRC64;
MPVAATNSES AMQQVLDNLG SLPNATGAAE LDLIFLRGIM ESPIVRSLAK AHERLEETKL
EAVRDNNLEL VQEILRDLAE LAEQSSTAAE LARILQEPHF QSLLETHDSV ASKTYETPPP
SPGLDPTFSN QPVPPDAVRM VGIRKTAGEH LGVTFRVEGG ELVIARILHG GMVAQQGLLH
VGDIIKEVNG QPVGSDPRAL QELLRSASGS VILKILPSYQ EPHLPRQVFV KCHFDYDPAR
DSLSPCKEAG LRFNAGDLLQ IVNQDDANWW QACHVEGGSA GLIPSQLLEE KRKAFVKRDL
ELTPTSGTLC GSLSGKKKKR MMYLTTKNAE FDRHELLIYE EVARMPPFRR KTLVLIGAQG
VGRRSLKNKL ILWDPDRYGT TVPYTSRRPK DSEREGQGYS FVSRGEMEAD IRAGRYLEHG
EYEGNLYGTR IDSIRGVVAS GKVCVLDVNP QAVKVLRTAE FVPYVVFIEA PDYETLRAMN
RAALESGVST KQLTEADLRR TVEESSRIQR GYGHYFDLSL VNSNLERTFR ELQTAMEKLR
TEPQWVPVSW VY
