Full text data of MPP7
MPP7
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
MAGUK p55 subfamily member 7
MAGUK p55 subfamily member 7
UniProt
Q5T2T1
ID MPP7_HUMAN Reviewed; 576 AA.
AC Q5T2T1; B2RCC9; B5MDZ3; D3DRW3; Q5T2T0; Q8IY28;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=MAGUK p55 subfamily member 7;
GN Name=MPP7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-322.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-322.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-322.
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION.
RX PubMed=14719143;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human MPP7 gene and mouse Mpp7
RT gene in silico.";
RL Int. J. Mol. Med. 13:333-338(2004).
RN [6]
RP INTERACTION WITH INADL AND MPP5.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH DLG1; LIN7A; LIN7B AND LIN7C.
RX PubMed=17237226; DOI=10.1074/jbc.M610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7
RT and DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=17616219; DOI=10.1021/pr070245b;
RA Ngai H.-H., Sit W.-H., Jiang P.-P., Thongboonkerd V., Wan J.-M.;
RT "Markedly increased urinary preprohaptoglobin and haptoglobin in
RT passive Heymann nephritis: a differential proteomics approach.";
RL J. Proteome Res. 6:3313-3320(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH DLG1 AND MPP5, AND MUTAGENESIS OF LEU-38 AND LEU-95.
RX PubMed=17332497; DOI=10.1091/mbc.E06-11-0980;
RA Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.;
RT "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and
RT facilitates epithelial tight junction formation.";
RL Mol. Biol. Cell 18:1744-1755(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Acts as an important adapter that promotes epithelial
CC cell polarity and tight junction formation via its interaction
CC with DLG1. Involved in the assembly of protein complexes at sites
CC of cell-cell contact.
CC -!- SUBUNIT: Heterodimer; able to heterodimerize via its C-terminal
CC L27 domain with LIN7A, LIN7B and LIN7C. Forms a tripartite complex
CC composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with
CC DLG1 via its N-terminal L27 domain. Interacts with MPP5 and
CC INADL/PATJ.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cell
CC junction, tight junction. Cell junction, adherens junction.
CC -!- INDUCTION: Down-regulated in patients suffering of passive Heymann
CC nephritis (at protein level).
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC -!- SIMILARITY: Contains 2 L27 domains.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI12709.1; Type=Erroneous gene model prediction;
CC Sequence=CAI13640.1; Type=Erroneous gene model prediction;
CC Sequence=CAI17344.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK315046; BAG37526.1; -; mRNA.
DR EMBL; AL390866; CAI12708.1; -; Genomic_DNA.
DR EMBL; AL355501; CAI12708.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI12708.1; JOINED; Genomic_DNA.
DR EMBL; AL390866; CAI12709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL355501; CAI12709.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI12709.1; JOINED; Genomic_DNA.
DR EMBL; AL355501; CAI13640.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL390866; CAI13640.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI13640.1; JOINED; Genomic_DNA.
DR EMBL; AL355501; CAI13641.1; -; Genomic_DNA.
DR EMBL; AL390866; CAI13641.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI13641.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI17344.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL355501; CAI17344.1; JOINED; Genomic_DNA.
DR EMBL; AL390866; CAI17344.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI17345.1; -; Genomic_DNA.
DR EMBL; AL355501; CAI17345.1; JOINED; Genomic_DNA.
DR EMBL; AL390866; CAI17345.1; JOINED; Genomic_DNA.
DR EMBL; CH471072; EAW86045.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86047.1; -; Genomic_DNA.
DR EMBL; BC038105; AAH38105.1; -; mRNA.
DR RefSeq; NP_775767.2; NM_173496.3.
DR RefSeq; XP_005252424.1; XM_005252367.1.
DR UniGene; Hs.499159; -.
DR PDB; 3LRA; X-ray; 2.95 A; A=9-120.
DR PDB; 3O46; X-ray; 1.30 A; A=135-225.
DR PDBsum; 3LRA; -.
DR PDBsum; 3O46; -.
DR ProteinModelPortal; Q5T2T1; -.
DR SMR; Q5T2T1; 1-219, 232-570.
DR IntAct; Q5T2T1; 1.
DR STRING; 9606.ENSP00000337907; -.
DR PhosphoSite; Q5T2T1; -.
DR DMDM; 74762233; -.
DR PaxDb; Q5T2T1; -.
DR PRIDE; Q5T2T1; -.
DR Ensembl; ENST00000337532; ENSP00000337907; ENSG00000150054.
DR Ensembl; ENST00000375719; ENSP00000364871; ENSG00000150054.
DR Ensembl; ENST00000375732; ENSP00000364884; ENSG00000150054.
DR Ensembl; ENST00000540098; ENSP00000438693; ENSG00000150054.
DR GeneID; 143098; -.
DR KEGG; hsa:143098; -.
DR UCSC; uc001iua.1; human.
DR CTD; 143098; -.
DR GeneCards; GC10M028382; -.
DR H-InvDB; HIX0008732; -.
DR HGNC; HGNC:26542; MPP7.
DR HPA; HPA037598; -.
DR MIM; 610973; gene.
DR neXtProt; NX_Q5T2T1; -.
DR PharmGKB; PA134985345; -.
DR eggNOG; COG0194; -.
DR HOGENOM; HOG000233034; -.
DR HOVERGEN; HBG001858; -.
DR InParanoid; Q5T2T1; -.
DR OMA; SRDDQGA; -.
DR OrthoDB; EOG79CXZ5; -.
DR PhylomeDB; Q5T2T1; -.
DR EvolutionaryTrace; Q5T2T1; -.
DR GenomeRNAi; 143098; -.
DR NextBio; 84649; -.
DR PRO; PR:Q5T2T1; -.
DR ArrayExpress; Q5T2T1; -.
DR Bgee; Q5T2T1; -.
DR CleanEx; HS_MPP7; -.
DR Genevestigator; Q5T2T1; -.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IDA:BHF-UCL.
DR GO; GO:0005923; C:tight junction; IDA:BHF-UCL.
DR GO; GO:0032947; F:protein complex scaffold; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:BHF-UCL.
DR GO; GO:0035591; F:signaling adaptor activity; NAS:BHF-UCL.
DR GO; GO:0030010; P:establishment of cell polarity; TAS:BHF-UCL.
DR GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:BHF-UCL.
DR GO; GO:0070830; P:tight junction assembly; IDA:BHF-UCL.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR004172; L27.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR011511; SH3_2.
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 PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 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 3D-structure; Cell junction; Complete proteome; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain;
KW Tight junction.
FT CHAIN 1 576 MAGUK p55 subfamily member 7.
FT /FTId=PRO_0000320027.
FT DOMAIN 10 65 L27 1.
FT DOMAIN 67 122 L27 2.
FT DOMAIN 139 220 PDZ.
FT DOMAIN 228 298 SH3.
FT DOMAIN 368 560 Guanylate kinase-like.
FT MOD_RES 409 409 Phosphoserine.
FT VARIANT 322 322 K -> R (in dbSNP:rs2997211).
FT /FTId=VAR_039110.
FT MUTAGEN 38 38 L->S: Abolishes interaction with DLG1.
FT MUTAGEN 95 95 L->S: Does not affect the interaction
FT with DLG1.
FT STRAND 10 13
FT HELIX 14 19
FT HELIX 21 25
FT TURN 26 28
FT HELIX 34 41
FT HELIX 47 61
FT HELIX 72 84
FT HELIX 90 98
FT HELIX 102 115
FT STRAND 138 147
FT STRAND 151 155
FT TURN 157 159
FT STRAND 162 167
FT HELIX 172 176
FT STRAND 184 188
FT STRAND 191 193
FT HELIX 198 207
FT STRAND 210 217
SQ SEQUENCE 576 AA; 65524 MW; 86366E460A08C6A7 CRC64;
MPALSTGSGS DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL VKIHEKLHYY
EKQSPVPILH GAAALADDLA EELQNKPLNS EIRELLKLLS KPNVKALLSV HDTVAQKNYD
PVLPPMPEDI DDEEDSVKII RLVKNREPLG ATIKKDEQTG AIIVARIMRG GAADRSGLIH
VGDELREVNG IPVEDKRPEE IIQILAQSQG AITFKIIPGS KEETPSKEGK MFIKALFDYN
PNEDKAIPCK EAGLSFKKGD ILQIMSQDDA TWWQAKHEAD ANPRAGLIPS KHFQERRLAL
RRPEILVQPL KVSNRKSSGF RKSFRLSRKD KKTNKSMYEC KKSDQYDTAD VPTYEEVTPY
RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV PHTTRARRSQ ESDGVEYIFI
SKHLFETDVQ NNKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK
PYVIFIKPPS IERLRETRKN AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MESQYGHLFD
KIIINDDLTV AFNELKTTFD KLETETHWVP VSWLHS
//
ID MPP7_HUMAN Reviewed; 576 AA.
AC Q5T2T1; B2RCC9; B5MDZ3; D3DRW3; Q5T2T0; Q8IY28;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=MAGUK p55 subfamily member 7;
GN Name=MPP7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-322.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-322.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-322.
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION.
RX PubMed=14719143;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human MPP7 gene and mouse Mpp7
RT gene in silico.";
RL Int. J. Mol. Med. 13:333-338(2004).
RN [6]
RP INTERACTION WITH INADL AND MPP5.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH DLG1; LIN7A; LIN7B AND LIN7C.
RX PubMed=17237226; DOI=10.1074/jbc.M610002200;
RA Bohl J., Brimer N., Lyons C., Vande Pol S.B.;
RT "The stardust family protein MPP7 forms a tripartite complex with LIN7
RT and DLG1 that regulates the stability and localization of DLG1 to cell
RT junctions.";
RL J. Biol. Chem. 282:9392-9400(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=17616219; DOI=10.1021/pr070245b;
RA Ngai H.-H., Sit W.-H., Jiang P.-P., Thongboonkerd V., Wan J.-M.;
RT "Markedly increased urinary preprohaptoglobin and haptoglobin in
RT passive Heymann nephritis: a differential proteomics approach.";
RL J. Proteome Res. 6:3313-3320(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH DLG1 AND MPP5, AND MUTAGENESIS OF LEU-38 AND LEU-95.
RX PubMed=17332497; DOI=10.1091/mbc.E06-11-0980;
RA Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A.;
RT "The MAGUK protein MPP7 binds to the polarity protein hDlg1 and
RT facilitates epithelial tight junction formation.";
RL Mol. Biol. Cell 18:1744-1755(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Acts as an important adapter that promotes epithelial
CC cell polarity and tight junction formation via its interaction
CC with DLG1. Involved in the assembly of protein complexes at sites
CC of cell-cell contact.
CC -!- SUBUNIT: Heterodimer; able to heterodimerize via its C-terminal
CC L27 domain with LIN7A, LIN7B and LIN7C. Forms a tripartite complex
CC composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with
CC DLG1 via its N-terminal L27 domain. Interacts with MPP5 and
CC INADL/PATJ.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cell
CC junction, tight junction. Cell junction, adherens junction.
CC -!- INDUCTION: Down-regulated in patients suffering of passive Heymann
CC nephritis (at protein level).
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC -!- SIMILARITY: Contains 2 L27 domains.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI12709.1; Type=Erroneous gene model prediction;
CC Sequence=CAI13640.1; Type=Erroneous gene model prediction;
CC Sequence=CAI17344.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK315046; BAG37526.1; -; mRNA.
DR EMBL; AL390866; CAI12708.1; -; Genomic_DNA.
DR EMBL; AL355501; CAI12708.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI12708.1; JOINED; Genomic_DNA.
DR EMBL; AL390866; CAI12709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL355501; CAI12709.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI12709.1; JOINED; Genomic_DNA.
DR EMBL; AL355501; CAI13640.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL390866; CAI13640.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI13640.1; JOINED; Genomic_DNA.
DR EMBL; AL355501; CAI13641.1; -; Genomic_DNA.
DR EMBL; AL390866; CAI13641.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI13641.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI17344.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL355501; CAI17344.1; JOINED; Genomic_DNA.
DR EMBL; AL390866; CAI17344.1; JOINED; Genomic_DNA.
DR EMBL; AL391423; CAI17345.1; -; Genomic_DNA.
DR EMBL; AL355501; CAI17345.1; JOINED; Genomic_DNA.
DR EMBL; AL390866; CAI17345.1; JOINED; Genomic_DNA.
DR EMBL; CH471072; EAW86045.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86047.1; -; Genomic_DNA.
DR EMBL; BC038105; AAH38105.1; -; mRNA.
DR RefSeq; NP_775767.2; NM_173496.3.
DR RefSeq; XP_005252424.1; XM_005252367.1.
DR UniGene; Hs.499159; -.
DR PDB; 3LRA; X-ray; 2.95 A; A=9-120.
DR PDB; 3O46; X-ray; 1.30 A; A=135-225.
DR PDBsum; 3LRA; -.
DR PDBsum; 3O46; -.
DR ProteinModelPortal; Q5T2T1; -.
DR SMR; Q5T2T1; 1-219, 232-570.
DR IntAct; Q5T2T1; 1.
DR STRING; 9606.ENSP00000337907; -.
DR PhosphoSite; Q5T2T1; -.
DR DMDM; 74762233; -.
DR PaxDb; Q5T2T1; -.
DR PRIDE; Q5T2T1; -.
DR Ensembl; ENST00000337532; ENSP00000337907; ENSG00000150054.
DR Ensembl; ENST00000375719; ENSP00000364871; ENSG00000150054.
DR Ensembl; ENST00000375732; ENSP00000364884; ENSG00000150054.
DR Ensembl; ENST00000540098; ENSP00000438693; ENSG00000150054.
DR GeneID; 143098; -.
DR KEGG; hsa:143098; -.
DR UCSC; uc001iua.1; human.
DR CTD; 143098; -.
DR GeneCards; GC10M028382; -.
DR H-InvDB; HIX0008732; -.
DR HGNC; HGNC:26542; MPP7.
DR HPA; HPA037598; -.
DR MIM; 610973; gene.
DR neXtProt; NX_Q5T2T1; -.
DR PharmGKB; PA134985345; -.
DR eggNOG; COG0194; -.
DR HOGENOM; HOG000233034; -.
DR HOVERGEN; HBG001858; -.
DR InParanoid; Q5T2T1; -.
DR OMA; SRDDQGA; -.
DR OrthoDB; EOG79CXZ5; -.
DR PhylomeDB; Q5T2T1; -.
DR EvolutionaryTrace; Q5T2T1; -.
DR GenomeRNAi; 143098; -.
DR NextBio; 84649; -.
DR PRO; PR:Q5T2T1; -.
DR ArrayExpress; Q5T2T1; -.
DR Bgee; Q5T2T1; -.
DR CleanEx; HS_MPP7; -.
DR Genevestigator; Q5T2T1; -.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; IDA:BHF-UCL.
DR GO; GO:0005923; C:tight junction; IDA:BHF-UCL.
DR GO; GO:0032947; F:protein complex scaffold; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:BHF-UCL.
DR GO; GO:0035591; F:signaling adaptor activity; NAS:BHF-UCL.
DR GO; GO:0030010; P:establishment of cell polarity; TAS:BHF-UCL.
DR GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:BHF-UCL.
DR GO; GO:0070830; P:tight junction assembly; IDA:BHF-UCL.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR004172; L27.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR011511; SH3_2.
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 PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 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 3D-structure; Cell junction; Complete proteome; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain;
KW Tight junction.
FT CHAIN 1 576 MAGUK p55 subfamily member 7.
FT /FTId=PRO_0000320027.
FT DOMAIN 10 65 L27 1.
FT DOMAIN 67 122 L27 2.
FT DOMAIN 139 220 PDZ.
FT DOMAIN 228 298 SH3.
FT DOMAIN 368 560 Guanylate kinase-like.
FT MOD_RES 409 409 Phosphoserine.
FT VARIANT 322 322 K -> R (in dbSNP:rs2997211).
FT /FTId=VAR_039110.
FT MUTAGEN 38 38 L->S: Abolishes interaction with DLG1.
FT MUTAGEN 95 95 L->S: Does not affect the interaction
FT with DLG1.
FT STRAND 10 13
FT HELIX 14 19
FT HELIX 21 25
FT TURN 26 28
FT HELIX 34 41
FT HELIX 47 61
FT HELIX 72 84
FT HELIX 90 98
FT HELIX 102 115
FT STRAND 138 147
FT STRAND 151 155
FT TURN 157 159
FT STRAND 162 167
FT HELIX 172 176
FT STRAND 184 188
FT STRAND 191 193
FT HELIX 198 207
FT STRAND 210 217
SQ SEQUENCE 576 AA; 65524 MW; 86366E460A08C6A7 CRC64;
MPALSTGSGS DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL VKIHEKLHYY
EKQSPVPILH GAAALADDLA EELQNKPLNS EIRELLKLLS KPNVKALLSV HDTVAQKNYD
PVLPPMPEDI DDEEDSVKII RLVKNREPLG ATIKKDEQTG AIIVARIMRG GAADRSGLIH
VGDELREVNG IPVEDKRPEE IIQILAQSQG AITFKIIPGS KEETPSKEGK MFIKALFDYN
PNEDKAIPCK EAGLSFKKGD ILQIMSQDDA TWWQAKHEAD ANPRAGLIPS KHFQERRLAL
RRPEILVQPL KVSNRKSSGF RKSFRLSRKD KKTNKSMYEC KKSDQYDTAD VPTYEEVTPY
RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV PHTTRARRSQ ESDGVEYIFI
SKHLFETDVQ NNKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK
PYVIFIKPPS IERLRETRKN AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MESQYGHLFD
KIIINDDLTV AFNELKTTFD KLETETHWVP VSWLHS
//
MIM
610973
*RECORD*
*FIELD* NO
610973
*FIELD* TI
*610973 MEMBRANE PROTEIN, PALMITOYLATED 7; MPP7
*FIELD* TX
DESCRIPTION
Membrane-associated guanylate kinases (MAGUKs) are important adaptor
read moreproteins involved in the assembly of protein complexes at sites of
cell-cell contact. They are found in synapses, adherens junctions, and
tight junctions. All MAGUKs contain at least 1 PDZ domain, an SH3
domain, and a GUK domain, and many contain 1 or 2 L27 domains, which are
involved in multimerization of MAGUKs. MPP7 belongs to the p55 stardust
subfamily of MAGUKs, which is named for a Drosophila gene required for
establishment of cell polarity in the developing fly embryo (Bohl et
al., 2007).
CLONING
By searching databases for homologs of MPP5 (606958), Katoh and Katoh
(2004) identified MPP7. The deduced 576-amino acid protein has 2 L27
domains (L27N and L27C) at its N terminus, followed by a PDZ domain, an
SH3 domain, and a C-terminal GUK domain. It shares 93% amino acid
identity with mouse Mpp7, 76% identity with the zebrafish humpback
protein, and 56% identity with human MPP3 (601114). In silico expression
analysis suggested that MPP7 is widely expressed.
GENE FUNCTION
Bohl et al. (2007) found that MPP7 formed a tripartite complex with DLG1
(601014) and LIN7A (603380) or LIN7C in vitro and in vivo. MPP7
dimerized with the LIN7 proteins through its L27C domain. The LIN7/MPP7
dimer then linked to DLG1 though the L27N domain of MPP7. This complex
localized to epithelial adherens junctions in transfected Madin-Darby
canine kidney cells. Expression of an MPP7 construct lacking either the
PDZ or SH3 domain redistributed MPP7, DLG1, and LIN7 into the soluble
cytoplasmic fraction.
Stucke et al. (2007) showed that the L27N domain of endogenous MPP7
bound DLG1 in human epithelial cells. The SH3-HOOK domain of MPP7
interacted with MPP5, and in turn MPP5 interacted with CRB3 (609737).
MPP7 and DLG1 colocalized at the lateral surface of epithelial cells,
and they overlapped with markers of adherens junctions and tight
junctions. Recruitment of MPP7 to the plasma membrane was dependent on
its L27N-mediated interaction with DLG1 and on CRB3-dependent
recruitment via the SH3-HOOK domain of MPP7. Loss of either DLG1 or MPP7
from epithelial cells resulted in a significant defect in assembly and
maintenance of functional tight junctions. Stucke et al. (2007)
concluded that formation of the DLG1-MPP7 complex promotes epithelial
cell polarity and tight junction formation.
GENE STRUCTURE
Katoh and Katoh (2004) determined that the MPP7 gene contains at least
19 exons.
MAPPING
By genomic sequence analysis, Katoh and Katoh (2004) mapped the MPP7
gene to chromosome 10p12.1.
*FIELD* RF
1. Bohl, J.; Brimer, N.; Lyons, C.; Vande Pol, S. B.: The Stardust
family protein MPP7 forms a tripartite complex with LIN7 and DLG1
that regulates the stability and localization of DLG1 to cell junctions. J.
Biol. Chem. 282: 9392-9400, 2007.
2. Katoh, M.; Katoh, M.: Identification and characterization of human
MPP7 gene and mouse Mpp7 gene in silico. Int. J. Molec. Med. 13:
333-338, 2004.
3. Stucke, V. M.; Timmerman, E.; Vandekerckhove, J.; Gevaert, K.;
Hall, A.: The MAGUK protein MPP7 binds to the polarity protein hDlg1
and facilitates epithelial tight junction formation. Molec. Biol.
Cell 18: 1744-1755, 2007.
*FIELD* CD
Alan F. Scott: 4/24/2007
*FIELD* ED
mgross: 04/24/2007
*RECORD*
*FIELD* NO
610973
*FIELD* TI
*610973 MEMBRANE PROTEIN, PALMITOYLATED 7; MPP7
*FIELD* TX
DESCRIPTION
Membrane-associated guanylate kinases (MAGUKs) are important adaptor
read moreproteins involved in the assembly of protein complexes at sites of
cell-cell contact. They are found in synapses, adherens junctions, and
tight junctions. All MAGUKs contain at least 1 PDZ domain, an SH3
domain, and a GUK domain, and many contain 1 or 2 L27 domains, which are
involved in multimerization of MAGUKs. MPP7 belongs to the p55 stardust
subfamily of MAGUKs, which is named for a Drosophila gene required for
establishment of cell polarity in the developing fly embryo (Bohl et
al., 2007).
CLONING
By searching databases for homologs of MPP5 (606958), Katoh and Katoh
(2004) identified MPP7. The deduced 576-amino acid protein has 2 L27
domains (L27N and L27C) at its N terminus, followed by a PDZ domain, an
SH3 domain, and a C-terminal GUK domain. It shares 93% amino acid
identity with mouse Mpp7, 76% identity with the zebrafish humpback
protein, and 56% identity with human MPP3 (601114). In silico expression
analysis suggested that MPP7 is widely expressed.
GENE FUNCTION
Bohl et al. (2007) found that MPP7 formed a tripartite complex with DLG1
(601014) and LIN7A (603380) or LIN7C in vitro and in vivo. MPP7
dimerized with the LIN7 proteins through its L27C domain. The LIN7/MPP7
dimer then linked to DLG1 though the L27N domain of MPP7. This complex
localized to epithelial adherens junctions in transfected Madin-Darby
canine kidney cells. Expression of an MPP7 construct lacking either the
PDZ or SH3 domain redistributed MPP7, DLG1, and LIN7 into the soluble
cytoplasmic fraction.
Stucke et al. (2007) showed that the L27N domain of endogenous MPP7
bound DLG1 in human epithelial cells. The SH3-HOOK domain of MPP7
interacted with MPP5, and in turn MPP5 interacted with CRB3 (609737).
MPP7 and DLG1 colocalized at the lateral surface of epithelial cells,
and they overlapped with markers of adherens junctions and tight
junctions. Recruitment of MPP7 to the plasma membrane was dependent on
its L27N-mediated interaction with DLG1 and on CRB3-dependent
recruitment via the SH3-HOOK domain of MPP7. Loss of either DLG1 or MPP7
from epithelial cells resulted in a significant defect in assembly and
maintenance of functional tight junctions. Stucke et al. (2007)
concluded that formation of the DLG1-MPP7 complex promotes epithelial
cell polarity and tight junction formation.
GENE STRUCTURE
Katoh and Katoh (2004) determined that the MPP7 gene contains at least
19 exons.
MAPPING
By genomic sequence analysis, Katoh and Katoh (2004) mapped the MPP7
gene to chromosome 10p12.1.
*FIELD* RF
1. Bohl, J.; Brimer, N.; Lyons, C.; Vande Pol, S. B.: The Stardust
family protein MPP7 forms a tripartite complex with LIN7 and DLG1
that regulates the stability and localization of DLG1 to cell junctions. J.
Biol. Chem. 282: 9392-9400, 2007.
2. Katoh, M.; Katoh, M.: Identification and characterization of human
MPP7 gene and mouse Mpp7 gene in silico. Int. J. Molec. Med. 13:
333-338, 2004.
3. Stucke, V. M.; Timmerman, E.; Vandekerckhove, J.; Gevaert, K.;
Hall, A.: The MAGUK protein MPP7 binds to the polarity protein hDlg1
and facilitates epithelial tight junction formation. Molec. Biol.
Cell 18: 1744-1755, 2007.
*FIELD* CD
Alan F. Scott: 4/24/2007
*FIELD* ED
mgross: 04/24/2007