LGI1_PANTR
ID LGI1_PANTR Reviewed; 557 AA.
AC Q1EGL2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Leucine-rich glioma-inactivated protein 1;
DE Flags: Precursor;
GN Name=LGI1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gu W., Gilbert Y., Freudenberg J., Elischer A., Bloch W., Meyer A.,
RA Steinlein O., Begemann G.;
RT "The evolution of the LGI family.";
RL Submitted (MAY-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; AY615298; AAV49150.1; -; mRNA.
DR RefSeq; NP_001065246.1; NM_001071778.1.
DR AlphaFoldDB; Q1EGL2; -.
DR SMR; Q1EGL2; -.
DR STRING; 9598.ENSPTRP00000004835; -.
DR PaxDb; Q1EGL2; -.
DR PRIDE; Q1EGL2; -.
DR Ensembl; ENSPTRT00000086732; ENSPTRP00000083692; ENSPTRG00000002771.
DR GeneID; 450619; -.
DR KEGG; ptr:450619; -.
DR CTD; 9211; -.
DR eggNOG; ENOG502REXX; Eukaryota.
DR GeneTree; ENSGT00940000159793; -.
DR HOGENOM; CLU_036403_0_0_1; -.
DR InParanoid; Q1EGL2; -.
DR OMA; FTVGSWQ; -.
DR OrthoDB; 365688at2759; -.
DR TreeFam; TF333155; -.
DR Proteomes; UP000002277; Chromosome 10.
DR Bgee; ENSPTRG00000002771; Expressed in primary visual cortex and 15 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
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_0000251155"
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; 63792 MW; 9F62336F4536C854 CRC64;
MESERSKRMG NACIPLKRIA YFLCLLSALL LTEGKKPAKP KCPAVCTCTK DNALCENARS
IPRTVPPDVI SLSFVRSGFT EISEGSFLFT 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 YQWNKATQSF
TNQTDIPNME DVYAVKHFSV KGDVYICLTR FIGDSKVMKW GGSSFQDIQR MPSRGSMVFQ
PLQINNYQYA ILGSDYSFTQ VYNWDAEKAK FVKFQELNVQ APRSFTHVSI NKRNFLFASS
FKGNTQIYKH VIVDLSA
