LGI1_RAT
ID LGI1_RAT Reviewed; 557 AA.
AC Q8K4Y5; Q5FWS7;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Leucine-rich glioma-inactivated protein 1;
DE Flags: Precursor;
GN Name=Lgi1;
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 [MRNA].
RC STRAIN=Wistar;
RX PubMed=12217514; DOI=10.1016/s0968-0004(02)02163-1;
RA Staub E., Perez-Tur J., Siebert R., Nobile C., Moschonas N.K., Deloukas P.,
RA Hinzmann B.;
RT "The novel EPTP repeat defines a superfamily of proteins implicated in
RT epileptic disorders.";
RL Trends Biochem. Sci. 27:441-444(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP FUNCTION, INTERACTION WITH KCNA1; KCNA4 AND KCNAB1, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16504945; DOI=10.1016/j.neuron.2006.01.033;
RA Schulte U., Thumfart J.-O., Kloecker N., Sailer C.A., Bildl W.,
RA Biniossek M., Dehn D., Deller T., Eble S., Abbass K., Wangler T.,
RA Knaus H.-G., Fakler B.;
RT "The epilepsy-linked Lgi1 protein assembles into presynaptic Kv1 channels
RT and inhibits inactivation by Kvbeta1.";
RL Neuron 49:697-706(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH ADAM22;
RP DLG4/PSD95 AND CACNG2, AND MUTAGENESIS OF GLU-383.
RX PubMed=16990550; DOI=10.1126/science.1129947;
RA Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., Fukata M.;
RT "Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic
RT transmission.";
RL Science 313:1792-1795(2006).
CC -!- FUNCTION: Plays a role in suppressing the production of MMP1/3 through
CC the phosphatidylinositol 3-kinase/ERK pathway (By similarity).
CC Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4
CC and KCNAB1. It slows down channel inactivation by precluding channel
CC closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that
CC positively regulates synaptic transmission mediated by AMPA-type
CC glutamate receptors. {ECO:0000250, ECO:0000269|PubMed:16504945,
CC ECO:0000269|PubMed:16990550}.
CC -!- SUBUNIT: Oligomer. Interacts with KCNA1 within a complex containing
CC KCNA1, KCNA4 and KCNAB1. Can bind to ADAM11 and ADAM23 (By similarity).
CC Part of a complex containing ADAM22, DLG4/PSD95 and CACNG2 (stargazin).
CC {ECO:0000250, ECO:0000269|PubMed:16504945,
CC ECO:0000269|PubMed:16990550}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16990550}. Synapse
CC {ECO:0000269|PubMed:16504945}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. High levels found in
CC hippocampus, thalamic nuclei, neocortex, and molecular and granule cell
CC layers of the cerebellum. {ECO:0000269|PubMed:16504945}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ487517; CAD31785.1; -; mRNA.
DR EMBL; BC089222; AAH89222.1; -; mRNA.
DR RefSeq; NP_665712.1; NM_145769.3.
DR AlphaFoldDB; Q8K4Y5; -.
DR SMR; Q8K4Y5; -.
DR BioGRID; 251653; 1.
DR CORUM; Q8K4Y5; -.
DR STRING; 10116.ENSRNOP00000020411; -.
DR GlyGen; Q8K4Y5; 3 sites.
DR iPTMnet; Q8K4Y5; -.
DR PhosphoSitePlus; Q8K4Y5; -.
DR SwissPalm; Q8K4Y5; -.
DR PaxDb; Q8K4Y5; -.
DR PRIDE; Q8K4Y5; -.
DR ABCD; Q8K4Y5; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000113976; ENSRNOP00000078389; ENSRNOG00000014758.
DR GeneID; 252892; -.
DR KEGG; rno:252892; -.
DR UCSC; RGD:628742; rat.
DR CTD; 9211; -.
DR RGD; 628742; Lgi1.
DR eggNOG; ENOG502REXX; Eukaryota.
DR GeneTree; ENSGT00940000159793; -.
DR HOGENOM; CLU_036403_0_0_1; -.
DR InParanoid; Q8K4Y5; -.
DR OMA; FTVGSWQ; -.
DR OrthoDB; 365688at2759; -.
DR PhylomeDB; Q8K4Y5; -.
DR TreeFam; TF333155; -.
DR Reactome; R-RNO-5682910; LGI-ADAM interactions.
DR PRO; PR:Q8K4Y5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014758; Expressed in cerebellum and 11 other tissues.
DR Genevisible; Q8K4Y5; RN.
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; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0043083; C:synaptic cleft; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IDA: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 Glycoprotein; Leucine-rich repeat; Reference proteome; Repeat; Secreted;
KW 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_0000017707"
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"
FT MUTAGEN 383
FT /note="E->A: Fails to bind to ADAM22."
FT /evidence="ECO:0000269|PubMed:16990550"
SQ SEQUENCE 557 AA; 63728 MW; 2296F36B6C91C32B CRC64;
MESESIRRMG NACIPLKRIA YFLCLFSVVL LTEGKKPAKP KCPAVCTCSK DNALCENARS
IPRTVPPDVI SLSFVRSGFT EISEGSFLFT PSLQLLLFTS NSFDVISDDA FIGLPHLEYL
FIENNNIKSI SRHTFRGLKS LIHLSLANNN LQTLPKDIFK GLDSLTNVDL RGNSFNCDCK
LKWLVEWLGH TNATVEDIYC EGPPEYKKRK INSLSPKDFD CIITEFAKSQ DLPYQSLSID
TFSYLNDEYV VIAQPFTGKC IFLEWDHVEK TFRNYDNITG TSTVVCKPIV IDTQLYVIVA
QLFGGSHIYK RDGFANKFIK IQDIEVLKIR KPNDIETFKI EDNWYFVVAD SSKAGFTTIY
KWNGNGFYSH QSLHAWYRDT DVEYLEIARP PLTLRTPHLI LSSSSQRPVI YQWSKATQLF
INQTDIPNME DVYAVKHFSV KGDVYICLTR FIGDSKVMKW GGSSFQDIQR MPSRGSMVFQ
PLQINNYQYA ILGSDYSFTQ VYNWDAEKAK FVKFQELNVQ APRSFTHVSI NKRNFLFASS
FKGNTQIYKH VIVDLSA
