MPDZ_RAT
ID MPDZ_RAT Reviewed; 2054 AA.
AC O55164;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Multiple PDZ domain protein;
DE AltName: Full=Multi-PDZ domain protein 1;
GN Name=Mpdz; Synonyms=Mupp1;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=9537516; DOI=10.1016/s0014-5793(98)00141-0;
RA Ullmer C., Schmuck K., Figge A., Luebbert H.;
RT "Cloning and characterization of MUPP1, a novel PDZ domain protein.";
RL FEBS Lett. 424:63-68(1998).
RN [2]
RP SUBCELLULAR LOCATION, AND DOMAINS.
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 [3]
RP FUNCTION, INTERACTION WITH HTR2C, TISSUE SPECIFICITY, DOMAIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11150294; DOI=10.1074/jbc.m008089200;
RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J.,
RA Luebbert H., Ullmer C.;
RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10
RT of the multi-PDZ domain protein MUPP1.";
RL J. Biol. Chem. 276:12974-12982(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CLDN5.
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 [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH DLG4; GRIN1; SYNGAP1; CAMK2A AND
RP CAMK2B, AND FUNCTION.
RX PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
RA Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
RT "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity
RT and NMDA receptor-dependent synaptic AMPA receptor potentiation.";
RL Neuron 43:563-574(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1808, 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).
RN [7]
RP STRUCTURE BY NMR OF 21-59, AND INTERACTION WITH PALS1.
RX PubMed=15863617; DOI=10.1073/pnas.0409346102;
RA Feng W., Long J.-F., Zhang M.;
RT "A unified assembly mode revealed by the structures of tetrameric L27
RT domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005).
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 (PubMed:15312654). Promotes clustering of HT2RC at the cell
CC surface (PubMed:11150294). {ECO:0000269|PubMed:11150294,
CC ECO:0000269|PubMed:15312654}.
CC -!- SUBUNIT: Interacts with F11R/JAM, CLDN1, NG2, CXADR, CRB1, MPP4 and
CC PALS1, HTR2A, HTR2B, PLEKHA1/TAPP1 and PLEKHA2/TAPP2. Interacts with
CC CXADR (By similarity). Interacts with HTR2C, CLDN5, DLG4, GRIN1,
CC SYNGAP1, CAMK2A and CAMK2B. Interacts with FAT4 (via cytoplasmic
CC domain) (By similarity). Interacts with DLL1 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q8VBX6,
CC ECO:0000269|PubMed:11000240, ECO:0000269|PubMed:11150294,
CC ECO:0000269|PubMed:12403818, ECO:0000269|PubMed:15312654,
CC ECO:0000269|PubMed:15863617}.
CC -!- INTERACTION:
CC O55164; P32745: SSTR3; Xeno; NbExp=2; IntAct=EBI-7401093, EBI-6266935;
CC -!- SUBCELLULAR LOCATION: Endomembrane system. Cell junction, tight
CC junction. Synapse. Apical cell membrane {ECO:0000269|PubMed:11150294}.
CC Postsynaptic density. Cell projection, dendrite. Synapse, synaptosome.
CC Note=Associated with membranes. Enriched at the tight junctions of
CC epithelial cells. Association to the tight junctions depends on CXADR.
CC In the retina, localizes to the sub-apical region adjacent to the
CC adherens junction complex at the outer limiting membrane (By
CC similarity). Colocalizes with HTR2C on the apical membrane of
CC epithelial choroid plexus cells (PubMed:11150294). Localized mainly in
CC the Schmidt-Lanterman incisures of myelinating Schwann cells. Highly
CC enriched in postsynaptic densities (PSD). Localized to punctae on
CC dendrites of hippocampal neurons and colocalizes with the synaptic
CC marker DLG4. {ECO:0000250, ECO:0000269|PubMed:11150294}.
CC -!- TISSUE SPECIFICITY: Abundant in all cerebral cortical layers,
CC especially the piriform cortex, the pyramidal cells of the CA1-CA3
CC subfields of the hippocampus, as well as the granular layer of the
CC dentate gyrus. Detected in the internal granular layer and the mitral
CC cell layer of the olfactory bulb; in the medial habenular nucleus; and
CC in amygdaloid, thalamic, hypothalamic, and pontine nuclei. In the
CC cerebellum, found at high levels in the granular layer. Detected in the
CC lateral ventricle. Expression overlaps with 5-HT2C receptor expression
CC in all regions of the brain including the choroid plexus, where 5-HT2C
CC receptors are highly enriched. {ECO:0000269|PubMed:11150294}.
CC -!- DOMAIN: The PDZ domain 1 binds NG2. The PDZ domain 2 mainly binds
CC CAMK2A and CAMK2B. The PDZ domain 9 binds F11R. The PDZ domain 10 binds
CC the C-terminus of CLDN1 and KIT. The PDZ domains 10 and 13 bind PLEKHA1
CC and PLEKHA2. The PDZ domain 13 binds CXADR and SYNGAP1 (By similarity).
CC The PDZ domains 7 and 10 bind the Ad9 E4-ORF1 oncoprotein. The PDZ
CC domain 10 binds the C-terminal PDZ-binding motif of HTR2C.
CC {ECO:0000250, ECO:0000269|PubMed:11000240,
CC ECO:0000269|PubMed:11150294}.
CC -!- MISCELLANEOUS: Sequestered into cytoplasmic, detergent-resistant bodies
CC upon Ad9 E4-ORF1 oncoprotein expression. Targeted to degradation upon
CC HPV-18 E6 oncoprotein expression.
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DR EMBL; AJ001320; CAA04681.1; -; mRNA.
DR PIR; T46612; T46612.
DR RefSeq; NP_062069.1; NM_019196.1.
DR PDB; 1Y76; NMR; -; A/C=4-65.
DR PDB; 5DTH; X-ray; 1.95 A; A/B/C/D=1312-1422.
DR PDBsum; 1Y76; -.
DR PDBsum; 5DTH; -.
DR AlphaFoldDB; O55164; -.
DR SMR; O55164; -.
DR BioGRID; 248019; 6.
DR CORUM; O55164; -.
DR ELM; O55164; -.
DR IntAct; O55164; 1.
DR MINT; O55164; -.
DR STRING; 10116.ENSRNOP00000051321; -.
DR iPTMnet; O55164; -.
DR PhosphoSitePlus; O55164; -.
DR PaxDb; O55164; -.
DR PRIDE; O55164; -.
DR GeneID; 29365; -.
DR KEGG; rno:29365; -.
DR UCSC; RGD:3105; rat.
DR CTD; 8777; -.
DR RGD; 3105; Mpdz.
DR VEuPathDB; HostDB:ENSRNOG00000007894; -.
DR eggNOG; KOG3528; Eukaryota.
DR HOGENOM; CLU_002378_0_0_1; -.
DR InParanoid; O55164; -.
DR PhylomeDB; O55164; -.
DR EvolutionaryTrace; O55164; -.
DR PRO; PR:O55164; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007894; Expressed in quadriceps femoris and 19 other tissues.
DR ExpressionAtlas; O55164; baseline and differential.
DR Genevisible; O55164; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
DR GO; GO:0035003; C:subapical complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR GO; GO:0042552; P:myelination; IPI:RGD.
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; Cell junction; Cell membrane; Cell projection; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW Synaptosome; Tight junction.
FT CHAIN 1..2054
FT /note="Multiple PDZ domain protein"
FT /id="PRO_0000094596"
FT DOMAIN 3..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 377..463
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 545..626
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 692..778
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 995..1076
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1138..1230
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1337..1420
FT /note="PDZ 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1470..1551
FT /note="PDZ 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1613..1696
FT /note="PDZ 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1709..1791
FT /note="PDZ 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1846..1932
FT /note="PDZ 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1971..2054
FT /note="PDZ 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1110..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1594
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 1261..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..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 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75970"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75970"
FT MOD_RES 1157
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBX6"
FT MOD_RES 1802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75970"
FT MOD_RES 1808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:1Y76"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:1Y76"
FT HELIX 43..61
FT /evidence="ECO:0007829|PDB:1Y76"
FT HELIX 1321..1328
FT /evidence="ECO:0007829|PDB:5DTH"
FT STRAND 1331..1341
FT /evidence="ECO:0007829|PDB:5DTH"
FT STRAND 1349..1353
FT /evidence="ECO:0007829|PDB:5DTH"
FT STRAND 1358..1367
FT /evidence="ECO:0007829|PDB:5DTH"
FT HELIX 1372..1376
FT /evidence="ECO:0007829|PDB:5DTH"
FT STRAND 1384..1388
FT /evidence="ECO:0007829|PDB:5DTH"
FT HELIX 1398..1407
FT /evidence="ECO:0007829|PDB:5DTH"
FT STRAND 1410..1418
FT /evidence="ECO:0007829|PDB:5DTH"
SQ SEQUENCE 2054 AA; 218592 MW; 44BD3F42B801F78F CRC64;
MLETIDKNRA LQAAERLQSK LKERGDVANE DKLSLLKSVL QSPLFSQILS LQTSLQQLKD
QVNVATLATA NADHAHTPQF SSAIISNLQS ESLLLSPSNG NLEAISGPGA PPAMDGKPAC
EELDQLIKSM AQGRHVEIFE LLKPPCGGLG FSVVGLRSEN RGELGIFVQE IQEGSVAHRD
GRLKETDQIL AINGQVLDQT ITHQQAISIL QKAKDTIQLV IARGSLPHIS SPRISRSPSA
ASTVSAHSNP THWQHVETIE LVNDGSGLGF GIIGGKATGV IVKTILPGGV ADQHGRLCSG
DHILKIGDTD LAGMSSEQVA QVLRQCGNRV KLMIARGAVE ETPAPSSLGI TLSSSTSTSE
MRVDASTQKN EESETFDVEL TKNVQGLGIT IAGYIGDKKL EPSGIFVKSI TKSSAVELDG
RIQIGDQIVA VDGTNLQGFT NQQAVEVLRH TGQTVRLTLM RKGASQEAEI TSREDTAKDV
DLPAENYEKD EESLSLKRST SILPIEEEGY PLLSTELEET EDVQQEAALL TKWQRIMGIN
YEIVVAHVSK FSENSGLGIS LEATVGHHFI RSVLPEGPVG HSGKLFSGDE LLEVNGINLL
GENHQDVVNI LKELPIDVTM VCCRRTVPPT ALSEVDSLDI HDLELTEKPH IDLGEFIGSS
ETEDPMLAMS DVDQNAEEIQ TPLAMWEAGI QAIELEKGSR GLGFSILDYQ DPIDPANTVI
VIRSLVPGGI AEKDGRLFPG DRLMFVNDIN LENSTLEEAV EALKGAPSGM VRIGVAKPLP
LSPEEGYVSA KEDTFLCSPH TCKEMGLSDK ALFRADLALI DTPDAESVAE SRFESQFSPD
NDSVYSTQAS VLSLHDGACS DGMNYGPSLP SSPPKDVTNS SDLVLGLHLS LEELYTQNLL
QRQHAGSPPT DMSPAATSGF TVSDYTPANA VEQKYECANT VAWTPSQLPS GLSTTELAPA
LPAVAPKYLT EQSSLVSDAE SVTLQSMSQE AFERTVTIAK GSSSLGMTVS ANKDGLGVIV
RSIIHGGAIS RDGRIAVGDC ILSINEESTI SLTNAQARAM LRRHSLIGPD IKITYVPAEH
LEEFRVSFGQ QAGGIMALDI FSSYTGRDIP ELPEREEGEG EESELQNAAY SSWSQPRRVE
LWREPSKSLG ISIVGGRGMG SRLSNGEVMR GIFIKHVLED SPAGKNGTLK PGDRIVEVDG
MDLRDASHEQ AVEAIRKAGS PVVFMVQSIV NRPRKSPLPS LPHSLYPKCS FSSTNPFAES
LQLTSDKAPS QSESESEKAT LCSVPSSSPS VFSEMSSDYA QPSATTVAED EDKEDEFGYS
WKNIQERYGT LTGQLHMIEL EKGHSGLGLS LAGNKDRTRM SVFIVGIDPT GAAGRDGRLQ
IADELLEING QILYGRSHQN ASSIIKCAPS KVKIIFIRNA DAVNQMAVCP GSAADPLPST
SESPQNKEVE PSITTSASAV DLSSLTNVYH LELPKDQGGL GIAICEEDTL NGVTIKSLTE
RGGAAKDGRL KPGDRILAVD DELVAGCPIE KFISLLKTAK TTVKLTVGAE NPGCQAVPSA
AVTASGERKD SSQTPAVPAP DLEPIPSTSR SSTPAIFASD PATCPIIPGC ETTIEISKGQ
TGLGLSIVGG SDTLLGAIII HEVYEEGAAC KDGRLWAGDQ ILEVNGIDLR KATHDEAINV
LRQTPQRVRL TLYRDEAPYK EEDVCDTFTV ELQKRPGKGL GLSIVGKRND TGVFVSDIVK
GGIADADGRL MQGDQILMVN GEDVRNATQE AVAALLKCSL GTVTLEVGRI KAAPFHSERR
PSQSSQVSES SLSSFSLPRS GIHTSESSES SAKKNALASE IQGLRTVEIK KGPADALGLS
IAGGVGSPLG DVPIFIAMMH PNGVAAQTQK LRVGDRIVTI CGTSTDGMTH TQAVNLMKNA
SGSIEVQVVA GGDVSVVTGH QQELANPCLA FTGLTSSTIF PDDLGPPQSK TITLDRGPDG
LGFSIVGGYG SPHGDLPIYV KTVFAKGAAA EDGRLKRGDQ IIAVNGQSLE GVTHEEAVAI
LKRTKGTVTL MVLS
