MPP3_RAT
ID MPP3_RAT Reviewed; 585 AA.
AC O88954; A6HJG0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=MAGUK p55 subfamily member 3 {ECO:0000250|UniProtKB:O88910};
DE AltName: Full=Discs large homolog 3;
DE AltName: Full=Protein MPP3 {ECO:0000250|UniProtKB:O88910};
GN Name=Mpp3 {ECO:0000312|RGD:620015};
GN Synonyms=Dlg3, Dusp3 {ECO:0000312|RGD:620015};
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] {ECO:0000305}
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAC78485.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-235.
RC TISSUE=Brain {ECO:0000312|EMBL:AAC78485.1};
RX PubMed=9753324; DOI=10.1016/s0092-8674(00)81736-5;
RA Butz S., Okamoto M., Suedhof T.C.;
RT "A tripartite protein complex with the potential to couple synaptic vesicle
RT exocytosis to cell adhesion in brain.";
RL Cell 94:773-782(1998).
RN [3] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP 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).
CC -!- SUBUNIT: May interact with HTR2A. Interacts (via PDZ domain) with CADM1
CC (via C-terminus). Interacts with HTR4 (By similarity).
CC {ECO:0000250|UniProtKB:O88910}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000255}.
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DR EMBL; CH473948; EDM06165.1; -; Genomic_DNA.
DR EMBL; AF087697; AAC78485.1; -; mRNA.
DR RefSeq; NP_446120.1; NM_053668.1.
DR RefSeq; XP_008766153.1; XM_008767931.1.
DR RefSeq; XP_008766154.1; XM_008767932.2.
DR AlphaFoldDB; O88954; -.
DR SMR; O88954; -.
DR BioGRID; 250305; 2.
DR STRING; 10116.ENSRNOP00000028264; -.
DR iPTMnet; O88954; -.
DR PhosphoSitePlus; O88954; -.
DR jPOST; O88954; -.
DR PaxDb; O88954; -.
DR PRIDE; O88954; -.
DR Ensembl; ENSRNOT00000028264; ENSRNOP00000028264; ENSRNOG00000033653.
DR GeneID; 114202; -.
DR KEGG; rno:114202; -.
DR UCSC; RGD:620015; rat.
DR CTD; 4356; -.
DR RGD; 620015; Mpp3.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000157190; -.
DR InParanoid; O88954; -.
DR OMA; EGYFKGH; -.
DR OrthoDB; 531106at2759; -.
DR PhylomeDB; O88954; -.
DR TreeFam; TF314263; -.
DR PRO; PR:O88954; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000033653; Expressed in cerebellum and 20 other tissues.
DR Genevisible; O88954; RN.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR CDD; cd12039; SH3_MPP3; 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; IPR035604; MPP3_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 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 Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..585
FT /note="MAGUK p55 subfamily member 3"
FT /id="PRO_0000365634"
FT DOMAIN 6..60
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 61..118
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 137..218
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 226..296
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 385..570
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 510..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 585 AA; 66589 MW; 6558942A9BC8BA20 CRC64;
MPVLSEDSGL HETLALLTSQ LRPDSNHREE MGFLRDVFSE KSLGYLMKIH EKLRYYERQS
PTPVLHSAMA LAEDVMEELQ AASVHSDERE LLQLLSTPHL RAVLMVHDTV AQKNFDPVLP
PLPDNIDEDF EEESVKIVRL VKNKEPLGAT IRRDEHSGAV VVARIMRGGA ADRSGLVHVG
DELREVNGIT VLHKRPDEIS QILAQSQGSI TLKIIPATQE EDRFKESKVF MRALFHYDPR
EDRAIPCQEA GLPFQQRQVL EVVSQDDPTW WQAKRVGDTN LRAGLIPSKQ FQERRLSYRR
TTGTIPSPQN LRKPLYDQPC DKETCDCDGY FKGHYVAGLR RSFRLGCRER LTGSQEVKVP
VGAESQVLLT YEEVARYQHQ PGERSRLVVL IGSLGAHLHE LKQRVVAEDP QHFGVAVPHT
TRPRKSHERE GVEYHFVSKQ AFEADIQHNK FLEHGEHKEN LYGTSLEAIQ TVMAKNKVCL
VDVEPEALRH LRTPEFKPYV IFVKPAIQEK RKTPPVSPDS EDPATPLDEQ QQEMAASAAF
IDQHYGHLID TVLVRQDLQS VCSQLRAVIE SLSKDTYWVP ISWVR
