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Multiple PDZ domain protein (Multi-PDZ domain protein 1)

 MPDZ_RAT                Reviewed;        2054 AA.
O55164;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 131.
RecName: Full=Multiple PDZ domain protein;
AltName: Full=Multi-PDZ domain protein 1;
Name=Mpdz; Synonyms=Mupp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9537516; DOI=10.1016/S0014-5793(98)00141-0;
Ullmer C., Schmuck K., Figge A., Luebbert H.;
"Cloning and characterization of MUPP1, a novel PDZ domain protein.";
FEBS Lett. 424:63-68(1998).
[2]
INTERACTION WITH ADENOVIRUS TYPE 9 E4-ORF1 PROTEIN AND HPV18 E6
PROTEIN, SUBCELLULAR LOCATION, AND DOMAINS.
PubMed=11000240; DOI=10.1128/JVI.74.20.9680-9693.2000;
Lee S.S., Glaunsinger B., Mantovani F., Banks L., Javier R.T.;
"Multi-PDZ domain protein MUPP1 is a cellular target for both
adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6
oncoproteins.";
J. Virol. 74:9680-9693(2000).
[3]
INTERACTION WITH HTR2C, TISSUE SPECIFICITY, DOMAIN, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=11150294; DOI=10.1074/jbc.M008089200;
Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J.,
Luebbert H., Ullmer C.;
"Interaction of serotonin 5-hydroxytryptamine type 2C receptors with
PDZ10 of the multi-PDZ domain protein MUPP1.";
J. Biol. Chem. 276:12974-12982(2001).
[4]
SUBCELLULAR LOCATION, AND INTERACTION WITH CLDN5.
PubMed=12403818; DOI=10.1083/jcb.200207050;
Poliak S., Matlis S., Ullmer C., Scherer S.S., Peles E.;
"Distinct claudins and associated PDZ proteins form different
autotypic tight junctions in myelinating Schwann cells.";
J. Cell Biol. 159:361-372(2002).
[5]
SUBCELLULAR LOCATION, INTERACTION WITH DLG4; GRIN1; SYNGAP1; CAMK2A
AND CAMK2B, AND FUNCTION.
PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase
activity and NMDA receptor-dependent synaptic AMPA receptor
potentiation.";
Neuron 43:563-574(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1808, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7]
STRUCTURE BY NMR OF 21-59, AND INTERACTION WITH MPP5.
PubMed=15863617; DOI=10.1073/pnas.0409346102;
Feng W., Long J.-F., Zhang M.;
"A unified assembly mode revealed by the structures of tetrameric L27
domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005).
-!- FUNCTION: Interacts with HTR2C and provokes its clustering at the
cell surface. Member of the NMDAR signaling complex that may play
a role in control of AMPAR potentiation and synaptic plasticity in
excitatory synapses. {ECO:0000269|PubMed:11150294,
ECO:0000269|PubMed:15312654}.
-!- SUBUNIT: Interacts with F11R/JAM, CLDN1, NG2, CXADR, CRB1, MPP4
and MPP5, HTR2A, HTR2B, PLEKHA1/TAPP1 and PLEKHA2/TAPP2. Interacts
with CXADR (By similarity). Interacts with HTR2C, CLDN5, DLG4,
GRIN1, SYNGAP1, CAMK2A and CAMK2B. Interacts with FAT4 (via
cytoplasmic domain) (By similarity). Interacts with the adenovirus
type 9 E4-ORF1 protein and the HPV18 E6 protein. Interacts with
DLL1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8VBX6,
ECO:0000269|PubMed:11000240, ECO:0000269|PubMed:11150294,
ECO:0000269|PubMed:12403818, ECO:0000269|PubMed:15312654,
ECO:0000269|PubMed:15863617}.
-!- INTERACTION:
P32745:SSTR3 (xeno); NbExp=2; IntAct=EBI-7401093, EBI-6266935;
-!- SUBCELLULAR LOCATION: Endomembrane system. Cell junction, tight
junction. Cell junction, synapse. Apical cell membrane. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density. Cell projection, dendrite. Cell junction, synapse,
synaptosome. Note=Associated with membranes. Enriched at the tight
junctions of epithelial cells. Association to the tight junctions
depends on CXADR. In the retina, localizes to the sub-apical
region adjacent to the adherens junction complex at the outer
limiting membrane (By similarity). Colocalizes with HTR2C on the
apical membrane of epithelial choroid plexus cells. Localized
mainly in the Schmidt-Lanterman incisures of myelinating Schwann
cells. Highly enriched in postsynaptic densities (PSD). Localized
to punctae on dendrites of hippocampal neurons and colocalizes
with the synaptic marker DLG4. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Abundant in all cerebral cortical layers,
especially the piriform cortex, the pyramidal cells of the CA1-CA3
subfields of the hippocampus, as well as the granular layer of the
dentate gyrus. Detected in the internal granular layer and the
mitral cell layer of the olfactory bulb; in the medial habenular
nucleus; and in amygdaloid, thalamic, hypothalamic, and pontine
nuclei. In the cerebellum, found at high levels in the granular
layer. Detected in the lateral ventricle. Expression overlaps with
5-HT2C receptor expression in all regions of the brain including
the choroid plexus, where 5-HT2C receptors are highly enriched.
{ECO:0000269|PubMed:11150294}.
-!- DOMAIN: The PDZ domain 1 binds NG2. The PDZ domain 2 mainly binds
CAMK2A and CAMK2B. The PDZ domain 9 binds F11R. The PDZ domain 10
binds the C-terminus of CLDN1 and KIT. The PDZ domains 10 and 13
bind PLEKHA1 and PLEKHA2. The PDZ domain 13 binds CXADR and
SYNGAP1 (By similarity). The PDZ domains 7 and 10 bind the Ad9 E4-
ORF1 oncoprotein. The PDZ domain 10 binds the C-terminal PDZ-
binding motif of HTR2C. {ECO:0000250, ECO:0000269|PubMed:11000240,
ECO:0000269|PubMed:11150294}.
-!- MISCELLANEOUS: Sequestered into cytoplasmic, detergent-resistant
bodies upon Ad9 E4-ORF1 oncoprotein expression. Targeted to
degradation upon HPV-18 E6 oncoprotein expression.
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EMBL; AJ001320; CAA04681.1; -; mRNA.
PIR; T46612; T46612.
RefSeq; NP_062069.1; NM_019196.1.
UniGene; Rn.6684; -.
PDB; 1Y76; NMR; -; A/C=4-65.
PDB; 5DTH; X-ray; 1.95 A; A/B/C/D=1312-1422.
PDBsum; 1Y76; -.
PDBsum; 5DTH; -.
ProteinModelPortal; O55164; -.
SMR; O55164; -.
BioGrid; 248019; 4.
CORUM; O55164; -.
ELM; O55164; -.
IntAct; O55164; 1.
MINT; MINT-143896; -.
STRING; 10116.ENSRNOP00000051321; -.
iPTMnet; O55164; -.
PhosphoSitePlus; O55164; -.
PaxDb; O55164; -.
PRIDE; O55164; -.
Ensembl; ENSRNOT00000051028; ENSRNOP00000051321; ENSRNOG00000007894.
GeneID; 29365; -.
KEGG; rno:29365; -.
UCSC; RGD:3105; rat.
CTD; 8777; -.
RGD; 3105; Mpdz.
eggNOG; KOG3528; Eukaryota.
eggNOG; ENOG4110362; LUCA.
GeneTree; ENSGT00760000119017; -.
HOGENOM; HOG000231304; -.
HOVERGEN; HBG080134; -.
InParanoid; O55164; -.
KO; K06095; -.
PhylomeDB; O55164; -.
EvolutionaryTrace; O55164; -.
PRO; PR:O55164; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000007894; -.
ExpressionAtlas; O55164; baseline and differential.
Genevisible; O55164; RN.
GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
GO; GO:0007155; P:cell adhesion; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
GO; GO:0042552; P:myelination; IPI:RGD.
Gene3D; 1.10.287.650; -; 1.
InterPro; IPR015132; L27_2.
InterPro; IPR004172; L27_dom.
InterPro; IPR036892; L27_dom_sf.
InterPro; IPR032078; MPDZ.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
Pfam; PF09045; L27_2; 1.
Pfam; PF16667; MPDZ_u10; 1.
Pfam; PF00595; PDZ; 12.
SMART; SM00569; L27; 1.
SMART; SM00228; PDZ; 13.
SUPFAM; SSF101288; SSF101288; 1.
SUPFAM; SSF50156; SSF50156; 13.
PROSITE; PS51022; L27; 1.
PROSITE; PS50106; PDZ; 13.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Cell projection;
Complete proteome; Membrane; Methylation; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; Synapse;
Synaptosome; Tight junction.
CHAIN 1 2054 Multiple PDZ domain protein.
/FTId=PRO_0000094596.
DOMAIN 3 63 L27. {ECO:0000255|PROSITE-
ProRule:PRU00365}.
DOMAIN 138 225 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 258 338 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 377 463 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 545 626 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 692 778 PDZ 5. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 995 1076 PDZ 6. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1138 1230 PDZ 7. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1337 1420 PDZ 8. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1470 1551 PDZ 9. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1613 1696 PDZ 10. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1709 1791 PDZ 11. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1846 1932 PDZ 12. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1971 2054 PDZ 13. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
COMPBIAS 1802 1831 Ser-rich.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 782 782 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 1065 1065 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 1157 1157 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8VBX6}.
MOD_RES 1802 1802 Phosphoserine.
{ECO:0000250|UniProtKB:O75970}.
MOD_RES 1808 1808 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
HELIX 6 24 {ECO:0000244|PDB:1Y76}.
HELIX 30 41 {ECO:0000244|PDB:1Y76}.
HELIX 43 61 {ECO:0000244|PDB:1Y76}.
HELIX 1321 1328 {ECO:0000244|PDB:5DTH}.
STRAND 1331 1341 {ECO:0000244|PDB:5DTH}.
STRAND 1349 1353 {ECO:0000244|PDB:5DTH}.
STRAND 1358 1367 {ECO:0000244|PDB:5DTH}.
HELIX 1372 1376 {ECO:0000244|PDB:5DTH}.
STRAND 1384 1388 {ECO:0000244|PDB:5DTH}.
HELIX 1398 1407 {ECO:0000244|PDB:5DTH}.
STRAND 1410 1418 {ECO:0000244|PDB:5DTH}.
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


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