ID MPP2_RAT Reviewed; 552 AA.
AC D3ZAA9; G3V8T8;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=MAGUK p55 subfamily member 2;
DE AltName: Full=Protein MPP2;
GN Name=Mpp2 {ECO:0000312|RGD:620014}; ORFNames=rCG_34691;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; THR-117 AND SER-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, SUBUNIT, INTERACTION WITH CACNG2; DLG4; DLGAP1 AND CADM1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27756895; DOI=10.1038/srep35283;
RA Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.;
RT "MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell
RT adhesion molecules to core components of the postsynaptic density.";
RL Sci. Rep. 6:35283-35283(2016).
CC -!- FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell
CC adhesion molecules to core components of the postsynaptic density
CC (PubMed:27756895). In CA1 pyramidal neurons, required for synaptic
CC KCNN2-containing channel function and long-term potentiation expression
CC (By similarity). Seems to negatively regulate SRC function in
CC epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q14168,
CC ECO:0000250|UniProtKB:Q9WV34, ECO:0000269|PubMed:27756895}.
CC -!- SUBUNIT: Can homomultimerise (PubMed:27756895). Interacts with CACNG2
CC (PubMed:27756895). Interacts (via the SH3-Guanylate kinase-like sub-
CC module) with DLG4/PSD95 and DLGAP1/GKAP (PubMed:27756895). Interacts
CC (via the PDZ domain) with CADM1 (via C-terminus) (PubMed:27756895).
CC Interacts with KCNN2/SK2 (via N-terminal domain) (By similarity).
CC Interacts with SRC (By similarity). {ECO:0000250|UniProtKB:Q14168,
CC ECO:0000250|UniProtKB:Q9WV34, ECO:0000269|PubMed:27756895}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9WV34}. Postsynaptic density
CC {ECO:0000269|PubMed:27756895}. 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:0000250|UniProtKB:Q9WV34}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal neurons.
CC {ECO:0000269|PubMed:27756895}.
CC -!- PTM: Phosphorylated by SRC. {ECO:0000250|UniProtKB:Q14168}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AC098160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473948; EDM06167.1; -; Genomic_DNA.
DR EMBL; CH473948; EDM06168.1; -; Genomic_DNA.
DR RefSeq; NP_445965.1; NM_053513.1.
DR RefSeq; XP_008766351.1; XM_008768129.2.
DR AlphaFoldDB; D3ZAA9; -.
DR SMR; D3ZAA9; -.
DR IntAct; D3ZAA9; 2.
DR STRING; 10116.ENSRNOP00000073193; -.
DR iPTMnet; D3ZAA9; -.
DR PhosphoSitePlus; D3ZAA9; -.
DR jPOST; D3ZAA9; -.
DR PaxDb; 10116-ENSRNOP00000052061; -.
DR PeptideAtlas; D3ZAA9; -.
DR Ensembl; ENSRNOT00000092150.2; ENSRNOP00000072422.1; ENSRNOG00000059683.2.
DR Ensembl; ENSRNOT00055057746; ENSRNOP00055047632; ENSRNOG00055033391.
DR Ensembl; ENSRNOT00060026017; ENSRNOP00060020827; ENSRNOG00060015166.
DR Ensembl; ENSRNOT00065046111; ENSRNOP00065037832; ENSRNOG00065026717.
DR GeneID; 85275; -.
DR KEGG; rno:85275; -.
DR AGR; RGD:620014; -.
DR CTD; 4355; -.
DR RGD; 620014; Mpp2.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000155348; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; D3ZAA9; -.
DR OrthoDB; 2873706at2759; -.
DR TreeFam; TF314263; -.
DR PRO; PR:D3ZAA9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000059683; Expressed in frontal cortex and 15 other cell types or tissues.
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; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0099562; P:maintenance of postsynaptic density structure; ISO:RGD.
DR GO; GO:0099173; P:postsynapse organization; ISO:RGD.
DR GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd12037; SH3_MPP2; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.287.650; L27 domain; 1.
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; 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 PANTHER; PTHR23122:SF35; MAGUK P55 SUBFAMILY MEMBER 2; 1.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
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; L27 domain; 1.
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 Cell projection; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..552
FT /note="MAGUK p55 subfamily member 2"
FT /id="PRO_0000439282"
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:0007744|PubMed:22673903"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 552 AA; 61565 MW; D893EB55D41ADB8B 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
DSLIPCKEAG LRFNAGDLLQ IVNQDDANWW QACHVEGGSA GLIPSQLLEE KRKAFVKRDL
ELTPTSGTLC GSLSGKKKKR MMYLTTKNAE FDRHELLIYE EVARMPPFRR KTLVLIGAQG
VGRRSLKNKL ILWDPDRYGT TVPYTSRRPK DSEREGQGYS FVSRGEMEAD IRAGRYLEHG
EYEGNLYGTR IDSIRGVVAS GKVCVLDVNP QAVKVLRTAE FVPYVVFIEA PDFETLRAMN
RAALESGVST KQLTEADLRR TVEESSRIQR GYGHYFDLSL VNSNLERTFR ELQTAMEKLR
TEPQWVPVSW VY
//
