ID   LGI1_PONAB              Reviewed;         557 AA.
AC   Q5R945;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Leucine-rich glioma-inactivated protein 1;
DE   Flags: Precursor;
GN   Name=LGI1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Interacts with KCNA1 within a complex containing
CC       KCNA1, KCNA4 and KCNAB1. Part of a complex containing ADAM22,
CC       DLG4/PSD95 and CACNG2 (stargazin). Can bind to ADAM11 and ADAM23.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Synapse {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
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DR   EMBL; CR859550; CAH91715.1; -; mRNA.
DR   RefSeq; NP_001125996.1; NM_001132524.1.
DR   AlphaFoldDB; Q5R945; -.
DR   SMR; Q5R945; -.
DR   STRING; 9601.ENSPPYP00000002892; -.
DR   GeneID; 100172937; -.
DR   KEGG; pon:100172937; -.
DR   CTD; 9211; -.
DR   eggNOG; ENOG502REXX; Eukaryota.
DR   InParanoid; Q5R945; -.
DR   OrthoDB; 365688at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript 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_0000251156"
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;  63728 MW;  F259FE4BC674231B CRC64;
     MESERSKRMG NACIPLKRIA YFLCLLSALL LTEGKKPAKP KCPAVCTCTK DNALCENARS
     IPRTVPPDVI SLSFVRSGFT EISEGGFLFT PSLQLLLFTS NSFDVISDDA FIGLPHLEYL
     FIENNNIKSI SRHTFRGLKS LIHLSLANNN LQTLPKDIFK GLDSLTNVDL RGNSFNCDCK
     LKWLVEWLGH TNATVEDIYC EGPPEYKKRK INSLSSKDFD CIITEFAKSQ DLPYQSLSID
     TFSYLNDEYV VIAQPFTGKC IFLEWDHVEK TFRNYDNITG TSTVVCKPIV IETQLYVIVA
     QLFGGSHIYK RDSFANKFIK IQDIEILKIR KPNDIETFKI ENNWYFVVAD SSKAGFTTIY
     KWNGNGFYSH QSLHAWYRDT DVEYLEIVRT PQTLRTPHLI LSSSSQRPVI YQWNKATQLF
     TNQTDIPNME DVYAVKHFSV KGDVYICLTR FIGDSKVMKW GGSSFQDIQR MPSRGSMVFQ
     PLQINNYQYA ILGSDYSFTQ VYNWDAEKAK FVKFQELNVQ APRSFTHVSI NKRNFLFASS
     FKGNTQICKH VIVDLSA