LGI1_MOUSE
ID LGI1_MOUSE Reviewed; 557 AA.
AC Q9JIA1;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Leucine-rich glioma-inactivated protein 1;
DE Flags: Precursor;
GN Name=Lgi1;
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] (ISOFORM 1).
RX PubMed=10920229; DOI=10.1007/s0033500101280;
RA Somerville R.P.T., Chernova O., Liu S., Shoshan Y., Cowell J.K.;
RT "Identification of the promoter, genomic structure, and mouse ortholog of
RT LGI1.";
RL Mamm. Genome 11:622-627(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PROTEIN SEQUENCE OF 161-171 AND 442-450, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15857855; DOI=10.1093/hmg/ddi169;
RA Senechal K.R., Thaller C., Noebels J.L.;
RT "ADPEAF mutations reduce levels of secreted LGI1, a putative tumor
RT suppressor protein linked to epilepsy.";
RL Hum. Mol. Genet. 14:1613-1620(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16787412; DOI=10.1111/j.1471-4159.2006.03939.x;
RA Furlan S., Roncaroli F., Forner F., Vitiello L., Calabria E.,
RA Piquer-Sirerol S., Valle G., Perez-Tur J., Michelucci R., Nobile C.;
RT "The LGI1/epitempin gene encodes two protein isoforms differentially
RT expressed in human brain.";
RL J. Neurochem. 98:985-991(2006).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP INTERACTION WITH ADAM11; ADAM22 AND ADAM23.
RX PubMed=18974846; DOI=10.7150/ijbs.4.387;
RA Sagane K., Ishihama Y., Sugimoto H.;
RT "LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11.";
RL Int. J. Biol. Sci. 4:387-396(2008).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=19833108; DOI=10.1016/j.brainres.2009.10.013;
RA Herranz-Perez V., Olucha-Bordonau F.E., Morante-Redolat J.M., Perez-Tur J.;
RT "Regional distribution of the leucine-rich glioma inactivated (LGI) gene
RT family transcripts in the adult mouse brain.";
RL Brain Res. 1307:177-194(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Regulates voltage-gated potassium channels assembled from
CC KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by
CC precluding channel closure mediated by the KCNAB1 subunit. Ligand for
CC ADAM22 that positively regulates synaptic transmission mediated by
CC AMPA-type glutamate receptors. Plays a role in suppressing the
CC production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK
CC pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomer (By similarity). Interacts with KCNA1 within a
CC complex containing KCNA1, KCNA4 and KCNAB1 (By similarity). Part of a
CC complex containing ADAM22, DLG4/PSD95 and CACNG2 (stargazin) (By
CC similarity). Can bind to ADAM11 and ADAM23. {ECO:0000250,
CC ECO:0000269|PubMed:18974846}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15857855,
CC ECO:0000269|PubMed:16787412}. Synapse {ECO:0000250}. Note=Isoform 1 and
CC isoform 2 are detected in the cytosolic and microsomal fractions
CC respectively.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JIA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIA1-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Brain. Highly expressed in the dentate gyrus and
CC CA3 field of the hippocampus. {ECO:0000269|PubMed:16787412,
CC ECO:0000269|PubMed:19833108}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
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DR EMBL; AF246818; AAF87077.1; -; mRNA.
DR EMBL; AK045443; BAC32370.1; -; mRNA.
DR EMBL; BC066090; AAH66090.1; -; mRNA.
DR CCDS; CCDS29786.1; -. [Q9JIA1-1]
DR RefSeq; NP_064674.1; NM_020278.2. [Q9JIA1-1]
DR AlphaFoldDB; Q9JIA1; -.
DR SMR; Q9JIA1; -.
DR BioGRID; 208189; 7.
DR IntAct; Q9JIA1; 5.
DR MINT; Q9JIA1; -.
DR STRING; 10090.ENSMUSP00000084507; -.
DR GlyConnect; 2464; 5 N-Linked glycans (1 site).
DR GlyGen; Q9JIA1; 3 sites, 5 N-linked glycans (1 site).
DR iPTMnet; Q9JIA1; -.
DR PhosphoSitePlus; Q9JIA1; -.
DR MaxQB; Q9JIA1; -.
DR PaxDb; Q9JIA1; -.
DR PeptideAtlas; Q9JIA1; -.
DR PRIDE; Q9JIA1; -.
DR ProteomicsDB; 286188; -. [Q9JIA1-1]
DR ABCD; Q9JIA1; 1 sequenced antibody.
DR Antibodypedia; 30497; 279 antibodies from 34 providers.
DR DNASU; 56839; -.
DR Ensembl; ENSMUST00000198518; ENSMUSP00000143128; ENSMUSG00000067242. [Q9JIA1-1]
DR GeneID; 56839; -.
DR KEGG; mmu:56839; -.
DR UCSC; uc008hji.1; mouse. [Q9JIA1-1]
DR CTD; 9211; -.
DR MGI; MGI:1861691; Lgi1.
DR VEuPathDB; HostDB:ENSMUSG00000067242; -.
DR eggNOG; ENOG502REXX; Eukaryota.
DR GeneTree; ENSGT00940000159793; -.
DR HOGENOM; CLU_2721524_0_0_1; -.
DR InParanoid; Q9JIA1; -.
DR OMA; FTVGSWQ; -.
DR OrthoDB; 365688at2759; -.
DR PhylomeDB; Q9JIA1; -.
DR TreeFam; TF333155; -.
DR Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR BioGRID-ORCS; 56839; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Lgi1; mouse.
DR PRO; PR:Q9JIA1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9JIA1; protein.
DR Bgee; ENSMUSG00000067242; Expressed in dentate gyrus of hippocampal formation and 126 other tissues.
DR ExpressionAtlas; Q9JIA1; baseline and differential.
DR Genevisible; Q9JIA1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR009039; EAR.
DR InterPro; IPR005492; EPTP.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF03736; EPTP; 7.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS50912; EAR; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Glycoprotein;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal; Synapse.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..557
FT /note="Leucine-rich glioma-inactivated protein 1"
FT /id="PRO_0000017706"
FT DOMAIN 35..72
FT /note="LRRNT"
FT REPEAT 92..113
FT /note="LRR 1"
FT REPEAT 116..137
FT /note="LRR 2"
FT REPEAT 140..161
FT /note="LRR 3"
FT DOMAIN 173..223
FT /note="LRRCT"
FT REPEAT 225..267
FT /note="EAR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 271..313
FT /note="EAR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 317..364
FT /note="EAR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 366..415
FT /note="EAR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 419..462
FT /note="EAR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 464..506
FT /note="EAR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 510..552
FT /note="EAR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 557 AA; 63644 MW; 2692D53F13DEC431 CRC64;
MESESSRRMG NACIPLKRIA YFLCLFSVVL LTEGKKPAKP KCPAVCTCSK DNALCENARS
IPRTVPPDVI SLSFVRSGFT EISEGSFLFT PSLQLLLFTS NSFDVISDDA FIGLPHLEYL
FIENNNIKSI SRHTFRGLKS LIHLSLANNN LQTLPKDIFK GLDSLTNVDL RGNAFNCDCK
LKWLVEWLGH TNATVEDIYC EGPPEYKKRK INSLSPKDFD CIITEFAKSQ DLPYQSLSID
TFSYLNDEYV VIAQPFTGKC IFLEWDHVEK TFRNYDNITG TSTVVCKPIV IDTQLYVIVA
QLFGGSHIYK RDGFANKFIK IQDIEVLKIR KPNDIETFKI EDNWYFVVAD SSKAGFTTIY
KWNGNGFYSH QSLHAWYRDT DVEYLEIARP PLALRTPHLI LSSSSQRPVI YQWSKATQLF
TNQTDIPNME DVYAVKHFSV KGDVYICLTR FIGDSKVMKW GGSSFQDIQR MPSRGSMVFQ
PLQINNYQYA ILGSDYSFTQ VYNWDAEKAK FVKFQELNVQ APRSFTHVSI NKRNFLFASS
FKGNTQIYKH VIVDLSA
