MPP7_RAT
ID MPP7_RAT Reviewed; 576 AA.
AC Q5U2Y3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=MAGUK p55 subfamily member 7;
GN Name=Mpp7;
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 [LARGE SCALE MRNA] OF 1-550.
RC TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 459-576.
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH85813.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC085813; AAH85813.1; ALT_SEQ; mRNA.
DR EMBL; CB580893; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001094045.1; NM_001100575.1.
DR RefSeq; XP_017456053.1; XM_017600564.1.
DR AlphaFoldDB; Q5U2Y3; -.
DR SMR; Q5U2Y3; -.
DR STRING; 10116.ENSRNOP00000025458; -.
DR iPTMnet; Q5U2Y3; -.
DR PhosphoSitePlus; Q5U2Y3; -.
DR PaxDb; Q5U2Y3; -.
DR PRIDE; Q5U2Y3; -.
DR Ensembl; ENSRNOT00000025458; ENSRNOP00000025458; ENSRNOG00000018760.
DR GeneID; 307035; -.
DR KEGG; rno:307035; -.
DR UCSC; RGD:1305675; rat.
DR CTD; 143098; -.
DR RGD; 1305675; Mpp7.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000156232; -.
DR HOGENOM; CLU_001715_5_0_1; -.
DR InParanoid; Q5U2Y3; -.
DR OMA; CDMLAAV; -.
DR OrthoDB; 531106at2759; -.
DR PhylomeDB; Q5U2Y3; -.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q5U2Y3; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000018760; Expressed in esophagus and 18 other tissues.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
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; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0071896; P:protein localization to adherens junction; ISO:RGD.
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; PF00018; SH3_1; 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 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Tight junction.
FT CHAIN 1..576
FT /note="MAGUK p55 subfamily member 7"
FT /id="PRO_0000320029"
FT DOMAIN 10..65
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 67..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:0000250|UniProtKB:Q5T2T1"
SQ SEQUENCE 576 AA; 65623 MW; 9A8E1C8D519D5507 CRC64;
MPALATGSAC DTGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL VKIHEKLHYY
EKQSPVPILH GAAALADDLA DELQNKPPNS EIRELLKLLS KPNVKALLSV HDTVAQKSYD
PVLPPMPDDI DDEEDSVKII RLVKNREPLG ATIKKDEQTG AITVARIMRG GAADRSGLIH
VGDELREVNG IPVEDKRPEE IIQILSQSQG AITFKIIPST KEEIPSKEGK IFIKALFDYD
PKEDKAIPCK EAGLSFRKGD ILQIMSQDDA TWWQAKHEGD TNPRAGLIPS KHFQERRLAL
RRPEIVVQPL KLSNRKSSGF RRSFRLSRKD KKTNKSMYEC KKSEQYDTAD VPTYEEVTPY
RRQTHDKYRL VVLVGPVGVG LNELKRKLLM SDTQHYGVTV PHTTRARRSQ ESDGVEYIFI
SKHLFETDVQ NNKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK
PYVIFIKPPS IERLRETRKN AKIISSRDDQ GTAKPFTEED FQEMIKSAQI MESQYGHLFD
KIIINDDLTV AFNELKTTFD KLETDAHWVP VSWLHS
