LRRC7_MOUSE
ID LRRC7_MOUSE Reviewed; 1490 AA.
AC Q80TE7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Leucine-rich repeat-containing protein 7;
DE AltName: Full=Densin-180;
DE Short=Densin;
DE AltName: Full=Protein LAP1;
GN Name=Lrrc7; Synonyms=Kiaa1365, Lap1;
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].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1392, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-443; THR-831;
RP SER-850; THR-865; SER-869; SER-947; SER-949; SER-1118; SER-1233 AND
RP SER-1392, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Pancreas;
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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22072671; DOI=10.1523/jneurosci.5877-10.2011;
RA Carlisle H.J., Luong T.N., Medina-Marino A., Schenker L., Khorosheva E.,
RA Indersmitten T., Gunapala K.M., Steele A.D., O'Dell T.J., Patterson P.H.,
RA Kennedy M.B.;
RT "Deletion of densin-180 results in abnormal behaviors associated with
RT mental illness and reduces mGluR5 and DISC1 in the postsynaptic density
RT fraction.";
RL J. Neurosci. 31:16194-16207(2011).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Required for normal synaptic spine architecture and function.
CC Necessary for DISC1 and GRM5 localization to postsynaptic density
CC complexes and for both N-methyl D-aspartate receptor-dependent and
CC metabotropic glutamate receptor-dependent long term depression.
CC {ECO:0000269|PubMed:22072671}.
CC -!- SUBUNIT: Interacts with CNKSR2 and DLG4 (By similarity). Interacts with
CC CTNND2/Catenin delta-2. Forms a complex with N-cadherin through CTNND2.
CC Interacts with CAMK2A (By similarity). {ECO:0000250|UniProtKB:P70587,
CC ECO:0000250|UniProtKB:Q96NW7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density
CC {ECO:0000269|PubMed:22072671}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:22072671}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable and were born at the
CC expected Mendelian ratio, but they have a mortality rate of about 20%.
CC They show early growth retardation. Mutant animals exhibit behavioral
CC abnormalities, including clasping when suspended by the tail, impaired
CC both hippocampus-dependent and hippocampus-independent short-term
CC memories and absence of acoustic prepulse inhibition. They also exhibit
CC significantly higher levels of anxiety. They become hyperactive in
CC response to stress or novelty, but are more sedentary than wild-type in
CC a familiar environment. Males have a profound deficit in nest-making
CC behavior and were aggressive when group-housed, even with littermates.
CC {ECO:0000269|PubMed:22072671}.
CC -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65780.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122498; BAC65780.1; ALT_INIT; mRNA.
DR RefSeq; NP_001278381.1; NM_001291452.1.
DR AlphaFoldDB; Q80TE7; -.
DR SMR; Q80TE7; -.
DR BioGRID; 232388; 17.
DR IntAct; Q80TE7; 8.
DR MINT; Q80TE7; -.
DR STRING; 10090.ENSMUSP00000101659; -.
DR iPTMnet; Q80TE7; -.
DR PhosphoSitePlus; Q80TE7; -.
DR SwissPalm; Q80TE7; -.
DR MaxQB; Q80TE7; -.
DR PaxDb; Q80TE7; -.
DR PRIDE; Q80TE7; -.
DR ProteomicsDB; 252526; -.
DR GeneID; 242274; -.
DR KEGG; mmu:242274; -.
DR UCSC; uc008rvx.2; mouse.
DR CTD; 57554; -.
DR MGI; MGI:2676665; Lrrc7.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q80TE7; -.
DR OrthoDB; 40683at2759; -.
DR PhylomeDB; Q80TE7; -.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 242274; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Lrrc7; mouse.
DR PRO; PR:Q80TE7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80TE7; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043194; C:axon initial segment; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51450; LRR; 15.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Leucine-rich repeat; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Synapse.
FT CHAIN 1..1490
FT /note="Leucine-rich repeat-containing protein 7"
FT /id="PRO_0000188299"
FT REPEAT 23..44
FT /note="LRR 1"
FT REPEAT 47..68
FT /note="LRR 2"
FT REPEAT 70..91
FT /note="LRR 3"
FT REPEAT 93..114
FT /note="LRR 4"
FT REPEAT 116..137
FT /note="LRR 5"
FT REPEAT 139..161
FT /note="LRR 6"
FT REPEAT 162..183
FT /note="LRR 7"
FT REPEAT 185..206
FT /note="LRR 8"
FT REPEAT 208..229
FT /note="LRR 9"
FT REPEAT 231..253
FT /note="LRR 10"
FT REPEAT 254..275
FT /note="LRR 11"
FT REPEAT 277..298
FT /note="LRR 12"
FT REPEAT 300..321
FT /note="LRR 13"
FT REPEAT 323..344
FT /note="LRR 14"
FT REPEAT 346..367
FT /note="LRR 15"
FT REPEAT 369..391
FT /note="LRR 16"
FT REPEAT 392..413
FT /note="LRR 17"
FT DOMAIN 1398..1488
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 663..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70587"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 865
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1149
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70587"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1490 AA; 166901 MW; A27F2892981A2982 CRC64;
MTTKRKLIGR LVPCRCFRGE EEIISVLDYS HCSLQQVPKE VFNFERTLEE LYLDANQIEE
LPKQLFNCQA LRKLSIPDND LSSLPTSIAS LVNLKELDIS KNGVQEFPEN IKCCKCLTII
EASVNPISKL PDGFTQLLNL TQLYLNDAFL EFLPANFGRL VKLRILELRE NHLKTLPKSM
HKLAQLERLD LGNNEFSELP EVLDQIQNLR ELWMDNNALQ VLPGSIGKLK MLVYLDMSKN
RIETVDMDIS GCEALEDLLL SSNMLQQLPD SIGLLKKLTT LKVDDNQLTM LPNTIGNLSL
LEEFDCSCNE LESLPPTIGY LHSLRTLAVD ENFLPELPRE IGSCKNVTVM SLRSNKLEFL
PEEIGQMQRL RVLNLSDNRL KNLPFSFTKL KELAALWLSD NQSKALIPLQ TEAHPETKQR
VLTNYMFPQQ PRGDEDFQSD SDSFNPTLWE EQRQQRMTVA FEFEDKKEDD ESAGKVKALS
CQAPWDRGQR GITLQPARLS GDCCTPWARC DQQIQDMPVP QSDPQLAWGC ISGLQQERSM
CAPLPVAAQS TTLPSLSGRQ VEINLKRYPT PYPEDLKNMV KSVQNLVGKP SHGVRVENSN
PTANTEQTVK EKFEHKWPVA PKEITVEDSF VHPANEMRIG ELHPSLAETP LYPPKLVLLG
KDKKESTDES EVDKTHCLNN SVSSGTYSDY SPSQASSASS NTRMKVGSLQ ATAKDAVHNS
LWGNRIAPPF PQPLDAKPLL SQREAVPPGN IPQRPDRLPM SDAFPDNWTD GSHYDNTGFV
SEEAAGENAN NNPLLSSKAR SVPAHGRRPL IRQERIVGVP LELEQSTHRH TPETEVPPSN
PWQNWTRTPS PFEDRTAFPS KLETTPTTSP LPERKDHMKE PTETPGPFSP GVPWEYHDPT
PNRSLGNVFS QIHCRPDSSK GVIAISKSTE RLSPLMKDIK SNKFKKSQSI DEIDVGTYKV
YNIPLENYAS GSDHLGSHER PDKFLGPEHG MSSMSRSQSV PMLDDEMLMY GSSKGPPQQK
ASMTKKVYQF DQSFNPQGAV EVKAEKRIPP PFAHNSEYVQ QPSKNIAKDL VSPRAYRGYP
PMEQMFSFSQ PSVNEDAMVN AQFASQGPRA GFLRRADSLA SSTEMAMFRR VSEPHELPPG
DRYGRATYRG GLEGQSSISM TDPQFLKRNG RYEDEHPSYQ EVKAQAGSFP AKNLTQRRPL
SARSYSTESY GASQTRPVSA RPTMAALLEK IPSDYNLGNY GDKTSDNSDI KTRPTPVKGE
ESCGKMPADW RQQLLRHIEA RRLDRTPSQQ SNILDNGQED VSPSGQWNPY PLGRRDVPPD
TITKKAGSHI QTLMGSQSLQ HRSREQQPYE GNINKVTIQQ FQSPLPIQIP SSQATRGPQP
GRCLIQTKGQ RSMDGYPEQF CVRIEKNPGL GFSISGGISG QGNPFKPSDK GIFVTRVQPD
GPASNLLQPG DKILQANGHS FVHMEHEKAV LLLKSFQNTV DLVIQRELTV
