MPP4_MOUSE
ID MPP4_MOUSE Reviewed; 635 AA.
AC Q6P7F1; Q0VG45; Q8BTT3; Q8BXM5; Q920P7; Q920P8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=MAGUK p55 subfamily member 4;
DE AltName: Full=Discs large homolog 6;
DE Short=mDLG6;
GN Name=Mpp4; Synonyms=Dlg6;
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 [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=12127943; DOI=10.1006/cbir.2002.0922;
RA Inagaki H., Tanaka K., Takada M., Maeda S., Ichihara S., Saito T.;
RT "Spatial distribution of mDLG6 mRNA in embryonic and adult mouse brain.";
RL Cell Biol. Int. 26:635-640(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Eye;
RX PubMed=15914641; DOI=10.1167/iovs.04-1417;
RA Kantardzhieva A., Gosens I., Alexeeva S., Punte I.M., Versteeg I.,
RA Krieger E., Neefjes-Mol C.A., den Hollander A.I., Letteboer S.J.F.,
RA Klooster J., Cremers F.P.M., Roepman R., Wijnholds J.;
RT "MPP5 recruits MPP4 to the CRB1 complex in photoreceptors.";
RL Invest. Ophthalmol. Vis. Sci. 46:2192-2201(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Retina, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12384283; DOI=10.1016/s0378-1119(02)00872-7;
RA Conte I., Lestingi M., den Hollander A., Miano M.G., Alfano G., Circolo D.,
RA Pugliese M., Testa F., Simonelli F., Rinaldi E., Baiget M., Banfi S.,
RA Ciccodicola A.;
RT "Characterization of MPP4, a gene highly expressed in photoreceptor cells,
RT and mutation analysis in retinitis pigmentosa.";
RL Gene 297:33-38(2002).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP FUNCTION.
RX PubMed=12859944; DOI=10.1016/s0006-291x(03)01142-2;
RA Li M., Zhang S.S.-M., Barnstable C.J.;
RT "Developmental and tissue expression patterns of mouse Mpp4 gene.";
RL Biochem. Biophys. Res. Commun. 307:229-235(2003).
RN [7]
RP INTERACTION WITH MPDZ.
RX PubMed=15316081; DOI=10.1242/jcs.01301;
RA van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J.,
RA Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W., Rashbass P.,
RA Le Bivic A., Wijnholds J.;
RT "Crumbs homologue 1 is required for maintenance of photoreceptor cell
RT polarization and adhesion during light exposure.";
RL J. Cell Sci. 117:4169-4177(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15558731; DOI=10.1002/cne.20367;
RA Stoehr H., Molday L.L., Molday R.S., Weber B.H.F., Biedermann B.,
RA Reichenbach A., Kraemer F.;
RT "Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with
RT Veli3 at distinct intercellular junctions of the neurosensory retina.";
RL J. Comp. Neurol. 481:31-41(2005).
CC -!- FUNCTION: May play a role in retinal photoreceptors development.
CC {ECO:0000269|PubMed:12859944}.
CC -!- SUBUNIT: May interact with GRIA2 (By similarity). Interacts with MPDZ.
CC Forms a complex with CRB1 and PALS1. Interacts with FASLG (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12859944,
CC ECO:0000269|PubMed:15558731}. Note=Localized at photoreceptor synaptic
CC terminals in retina. Localized in rod and cone photoreceptors at the
CC plasma membrane and at membranes of intracellular vesicles around the
CC subapical region (SAR) and adherens junction, and in the outer
CC plexiform layer (OPL).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=mDLG6A;
CC IsoId=Q6P7F1-1; Sequence=Displayed;
CC Name=3; Synonyms=mDLG6B;
CC IsoId=Q6P7F1-3; Sequence=VSP_013995;
CC Name=4;
CC IsoId=Q6P7F1-4; Sequence=VSP_013994, VSP_013995, VSP_013996,
CC VSP_013997;
CC -!- TISSUE SPECIFICITY: Detected in the retina (at protein level). Highly
CC enriched in the retina where it is mainly expressed by rod
CC photoreceptors; detected in the inner segment of the photoreceptor
CC layer and in the outer nuclear layer. Also detected at much lower
CC levels in pineal gland, cerebellum, cortex, hippocampus, olfactory
CC bulb, heart, liver and spleen. Expressed in the CA1-CA3 regions of
CC pyramidal cell layers and in the granule cell layer of dentate gyrus in
CC the hippocampus. In the cerebellum, expressed in Purkinje cells and
CC throughout the granule cell layer. In the olfactory bulb, expressed in
CC mitral cells. {ECO:0000269|PubMed:12127943,
CC ECO:0000269|PubMed:12384283, ECO:0000269|PubMed:12859944,
CC ECO:0000269|PubMed:15558731}.
CC -!- DEVELOPMENTAL STAGE: Expressed postnatally in the retina. The
CC expression in the retina coincides with one of the photoreceptor
CC specific genes. Expressed in forebrain of 9.5 dpc embryos and in whole
CC brain of 11.5 dpc embryos. {ECO:0000269|PubMed:12127943,
CC ECO:0000269|PubMed:12384283, ECO:0000269|PubMed:12859944}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61694.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI16724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB69494.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB69495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC32031.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC40562.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC40562.1; Type=Miscellaneous discrepancy; Note=Frameshifts and sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB059357; BAB69494.1; ALT_INIT; mRNA.
DR EMBL; AB059358; BAB69495.1; ALT_INIT; mRNA.
DR EMBL; AJ748820; CAG38657.1; -; mRNA.
DR EMBL; AK044682; BAC32031.1; ALT_FRAME; mRNA.
DR EMBL; AK088771; BAC40562.1; ALT_SEQ; mRNA.
DR EMBL; BC061694; AAH61694.2; ALT_INIT; mRNA.
DR EMBL; BC116723; AAI16724.1; ALT_INIT; mRNA.
DR CCDS; CCDS48271.1; -. [Q6P7F1-1]
DR RefSeq; NP_001158154.1; NM_001164682.1.
DR RefSeq; NP_660125.2; NM_145143.3. [Q6P7F1-1]
DR AlphaFoldDB; Q6P7F1; -.
DR SMR; Q6P7F1; -.
DR BioGRID; 230597; 3.
DR CORUM; Q6P7F1; -.
DR STRING; 10090.ENSMUSP00000109914; -.
DR iPTMnet; Q6P7F1; -.
DR PhosphoSitePlus; Q6P7F1; -.
DR MaxQB; Q6P7F1; -.
DR PaxDb; Q6P7F1; -.
DR PRIDE; Q6P7F1; -.
DR ProteomicsDB; 295584; -. [Q6P7F1-1]
DR ProteomicsDB; 295585; -. [Q6P7F1-3]
DR ProteomicsDB; 295586; -. [Q6P7F1-4]
DR Antibodypedia; 34145; 57 antibodies from 14 providers.
DR DNASU; 227157; -.
DR Ensembl; ENSMUST00000078874; ENSMUSP00000077914; ENSMUSG00000079550. [Q6P7F1-1]
DR Ensembl; ENSMUST00000191200; ENSMUSP00000140957; ENSMUSG00000079550. [Q6P7F1-3]
DR GeneID; 227157; -.
DR KEGG; mmu:227157; -.
DR UCSC; uc007bdh.1; mouse. [Q6P7F1-3]
DR UCSC; uc007bdi.2; mouse. [Q6P7F1-1]
DR UCSC; uc007bdj.1; mouse. [Q6P7F1-4]
DR CTD; 58538; -.
DR MGI; MGI:2386681; Mpp4.
DR VEuPathDB; HostDB:ENSMUSG00000079550; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000156444; -.
DR HOGENOM; CLU_001715_5_0_1; -.
DR InParanoid; Q6P7F1; -.
DR OMA; EAQYWQF; -.
DR OrthoDB; 278124at2759; -.
DR PhylomeDB; Q6P7F1; -.
DR BioGRID-ORCS; 227157; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mpp4; mouse.
DR PRO; PR:Q6P7F1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6P7F1; protein.
DR Bgee; ENSMUSG00000079550; Expressed in retinal neural layer and 69 other tissues.
DR ExpressionAtlas; Q6P7F1; baseline and differential.
DR Genevisible; Q6P7F1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0044316; C:cone cell pedicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0044317; C:rod spherule; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0035418; P:protein localization to synapse; IMP:MGI.
DR CDD; cd12034; SH3_MPP4; 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; IPR035600; MPP4_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; 1.
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 Alternative splicing; Coiled coil; Cytoplasm; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..635
FT /note="MAGUK p55 subfamily member 4"
FT /id="PRO_0000094578"
FT DOMAIN 23..79
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 86..136
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 153..234
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 241..311
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 426..615
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 567..622
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..150
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013994"
FT VAR_SEQ 331..336
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12127943,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013995"
FT VAR_SEQ 350..354
FT /note="DEETF -> GNSSS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013996"
FT VAR_SEQ 355..635
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013997"
FT CONFLICT 2
FT /note="R -> I (in Ref. 1; BAB69494/BAB69495)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="Q -> K (in Ref. 1; BAB69494/BAB69495)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="H -> N (in Ref. 1; BAB69494/BAB69495)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="T -> M (in Ref. 3; BAC32031/BAC40562 and 4;
FT AAI16724)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="V -> G (in Ref. 1; BAB69494/BAB69495)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="P -> H (in Ref. 3; BAC32031)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="G -> A (in Ref. 3; BAC40562)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="F -> S (in Ref. 1; BAB69494/BAB69495, 3; BAC32031
FT and 4; AAI16724)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="S -> L (in Ref. 1; BAB69494/BAB69495, 3; BAC32031
FT and 4; AAI16724)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="Y -> C (in Ref. 1; BAB69494/BAB69495)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="K -> R (in Ref. 1; BAB69494/BAB69495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 72001 MW; C8E08DDD122670C4 CRC64;
MRQSDRGAEL TNEDRALPTP PDPENGLSGI LRLLLQELSL FYSRDVNGLC LLYDLLHSPW
LQALLKVYDC LQRFKEKKLV PDTTHAQILA CEVLELLPKA SGSPEIQELR QVLQAPHCKA
LLSAHDTVAQ KDFEPLLPPL PDNIPDSEEA MRIVCLVKNQ QPLGATIKRH EITGDILVAR
VIHGGLVERS GLLYAGDKLV EVNGVSVEGL DPEQVIHILA MSCGTIMFKV IPVSAPPVSS
QKMVYVRAMI DYWPQEDPDI PCMDAGLPFL KGDILQIVDQ NDALWWQARK ISDLTICAGL
IPSNHLLKRK QREFWWSQPY QPHTCLKSTR ALSMEEEDSM KIDEKCVEAD EETFESEELA
EAKDEFVGDG QKFFIAGFRR SMRLCRRKSH FSQLHASLCC SCSCYSAVGA PYEEVVRYQR
QPADKHRLIV LVGPSGVGVN ELRRQLIGCN PSCFQSAVPH TTRFPKSYEM DGREYHYVSR
ETFESLMYGH KMLEYGEYKG HLYGTSVNAV HAVLDEGKIC IMDLEPQDIQ SARTRDLKPY
VIFIKPPNTS SMRHSRKNAK ITTDYYVDMK FKDEDLQEME ELAQKMESQF GQFFDHVIVN
DNLQDACGQL LSAIQKAQEE LQWVPEAWVS PDTES
