MPP7_MOUSE
ID MPP7_MOUSE Reviewed; 576 AA.
AC Q8BVD5; Q148N6; Q8BZZ8; Q9D3K2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=MAGUK p55 subfamily member 7;
GN Name=Mpp7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Colon, Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as an important adapter that promotes epithelial cell
CC polarity and tight junction formation via its interaction with DLG1.
CC Involved in the assembly of protein complexes at sites of cell-cell
CC contact (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; able to heterodimerize via its C-terminal L27
CC domain with LIN7A, LIN7B and LIN7C. Forms a tripartite complex composed
CC of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). Interacts with DLG1 via its N-
CC terminal L27 domain. Interacts with PALS1 and PATJ (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q5T2T1};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q5T2T1}. Lateral
CC cell membrane {ECO:0000250|UniProtKB:Q5T2T1}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q5T2T1}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q5T2T1}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q5T2T1}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q5T2T1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5T2T1}. Note=In epidermal cells, detected
CC primarily at the lateral cell membrane. {ECO:0000250|UniProtKB:Q5T2T1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8BVD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BVD5-2; Sequence=VSP_031579, VSP_031580;
CC Name=3;
CC IsoId=Q8BVD5-3; Sequence=VSP_031574, VSP_031579, VSP_031580;
CC Name=4;
CC IsoId=Q8BVD5-4; Sequence=VSP_031575, VSP_031578;
CC Name=5;
CC IsoId=Q8BVD5-5; Sequence=VSP_031576, VSP_031577;
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC sufficient and important for interaction with phospholipids permitting
CC cortical localization (By similarity). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (By similarity). {ECO:0000250|UniProtKB:Q5T2T1}.
CC -!- PTM: Phosphorylated by aPKC which promotes dissociation from the cell
CC cortex. {ECO:0000250|UniProtKB:Q5T2T1}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AK017344; BAB30699.1; -; mRNA.
DR EMBL; AK033081; BAC28146.1; -; mRNA.
DR EMBL; AK078849; BAC37419.1; -; mRNA.
DR EMBL; AC139324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117550; AAI17551.1; -; mRNA.
DR EMBL; BC118058; AAI18059.1; -; mRNA.
DR CCDS; CCDS50217.1; -. [Q8BVD5-1]
DR CCDS; CCDS89187.1; -. [Q8BVD5-2]
DR RefSeq; NP_001074756.2; NM_001081287.2.
DR RefSeq; NP_001155092.1; NM_001161620.1. [Q8BVD5-2]
DR AlphaFoldDB; Q8BVD5; -.
DR SMR; Q8BVD5; -.
DR BioGRID; 217704; 3.
DR STRING; 10090.ENSMUSP00000111535; -.
DR iPTMnet; Q8BVD5; -.
DR PhosphoSitePlus; Q8BVD5; -.
DR MaxQB; Q8BVD5; -.
DR PaxDb; Q8BVD5; -.
DR PeptideAtlas; Q8BVD5; -.
DR PRIDE; Q8BVD5; -.
DR ProteomicsDB; 291492; -. [Q8BVD5-1]
DR ProteomicsDB; 291493; -. [Q8BVD5-2]
DR ProteomicsDB; 291494; -. [Q8BVD5-3]
DR ProteomicsDB; 291495; -. [Q8BVD5-4]
DR ProteomicsDB; 291496; -. [Q8BVD5-5]
DR Antibodypedia; 26125; 107 antibodies from 24 providers.
DR DNASU; 75739; -.
DR Ensembl; ENSMUST00000234510; ENSMUSP00000157260; ENSMUSG00000057440. [Q8BVD5-5]
DR Ensembl; ENSMUST00000234571; ENSMUSP00000157306; ENSMUSG00000057440. [Q8BVD5-2]
DR GeneID; 75739; -.
DR KEGG; mmu:75739; -.
DR UCSC; uc008dzt.1; mouse. [Q8BVD5-2]
DR UCSC; uc008dzu.1; mouse. [Q8BVD5-1]
DR UCSC; uc008dzv.1; mouse. [Q8BVD5-5]
DR UCSC; uc008dzx.1; mouse. [Q8BVD5-4]
DR CTD; 143098; -.
DR MGI; MGI:1922989; Mpp7.
DR VEuPathDB; HostDB:ENSMUSG00000057440; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000156232; -.
DR InParanoid; Q8BVD5; -.
DR OrthoDB; 531106at2759; -.
DR PhylomeDB; Q8BVD5; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 75739; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Mpp7; mouse.
DR PRO; PR:Q8BVD5; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BVD5; protein.
DR Bgee; ENSMUSG00000057440; Expressed in seminal vesicle and 230 other tissues.
DR ExpressionAtlas; Q8BVD5; baseline and differential.
DR GO; GO:0005912; C:adherens junction; ISS:BHF-UCL.
DR GO; GO:0005923; C:bicellular tight junction; ISS:BHF-UCL.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; ISS:BHF-UCL.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:BHF-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:BHF-UCL.
DR GO; GO:0071896; P:protein localization to adherens junction; ISS:BHF-UCL.
DR CDD; cd12033; SH3_MPP7; 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; IPR035599; MPP7_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 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; 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 Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..576
FT /note="MAGUK p55 subfamily member 7"
FT /id="PRO_0000320028"
FT DOMAIN 10..64
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 65..122
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 139..220
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 228..298
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 368..560
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 289..383
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000250|UniProtKB:Q5T2T1"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 308
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031574"
FT VAR_SEQ 318..326
FT /note="SGFRRSFRL -> CKFVNKNTQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031575"
FT VAR_SEQ 318..321
FT /note="SGFR -> FPFT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031576"
FT VAR_SEQ 322..576
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031577"
FT VAR_SEQ 327..576
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031578"
FT VAR_SEQ 402..427
FT /note="HTTRARRSQESDGVEYIFISKHLFET -> REFSGPWWFSEDISKLSEQLKK
FT LTLC (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031579"
FT VAR_SEQ 428..576
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031580"
SQ SEQUENCE 576 AA; 65540 MW; 87E3A16D4EC4EFBB CRC64;
MPALATGSAC DMGLYELLAA LPAQLQPHVD SQEDLTFLWD VFGEKSLHSL VKIHEKLHCY
EKQNPLPILH GAAALADDLT EELQNKLPNS EIRELLKLLS KPNVKALLSV HDTVAQKSYD
PVLPPVPDDI DDEEDSVKII RLVKNSEPLG ATIKKDEQTG AITVARIMRG GAADRSGLIH
VGDELREVNG IPVEDKRPEE IIKILSQSKG AITFKIIPST KEETPSKEGK IFIKALFDYD
PKEDKAIPCK EAGLSFRKGD ILQIMSQDDV TWWQAKHEGD ANPRAGLIPS KHFQERRLAL
RRPEIVVQPL KLSNTKSSGF RRSFRLSRKN KKINKSMYEC KKSEQYDTAD VPTYEEVTPY
RRQIHDKYRL IVLVGPVGVG LNELKRKLLM SDAQHYGVIV PHTTRARRSQ ESDGVEYIFI
SKHLFETDVQ INKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK
PYVIFIKPPS IERLRETRKN AKIISSRDDQ GTAKPFTEED FQEMIKSAQI MESQYGHLFD
KIIINDDLTV AFNELKTTFD KLETDTHWVP VSWLHS
