LGI1_BOVIN
ID LGI1_BOVIN Reviewed; 533 AA.
AC Q5E9T6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Leucine-rich glioma-inactivated protein 1;
DE Flags: Precursor;
GN Name=LGI1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; BT020834; AAX08851.1; -; mRNA.
DR RefSeq; NP_001040056.2; NM_001046591.2.
DR AlphaFoldDB; Q5E9T6; -.
DR SMR; Q5E9T6; -.
DR STRING; 9913.ENSBTAP00000006728; -.
DR PaxDb; Q5E9T6; -.
DR Ensembl; ENSBTAT00000006728; ENSBTAP00000006728; ENSBTAG00000005106.
DR GeneID; 617080; -.
DR KEGG; bta:617080; -.
DR CTD; 9211; -.
DR VEuPathDB; HostDB:ENSBTAG00000005106; -.
DR eggNOG; ENOG502REXX; Eukaryota.
DR GeneTree; ENSGT00940000159793; -.
DR InParanoid; Q5E9T6; -.
DR OMA; FTVGSWQ; -.
DR OrthoDB; 365688at2759; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000005106; Expressed in occipital lobe and 83 other tissues.
DR ExpressionAtlas; Q5E9T6; baseline.
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; 2.
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..533
FT /note="Leucine-rich glioma-inactivated protein 1"
FT /id="PRO_0000251154"
FT DOMAIN 35..72
FT /note="LRRNT"
FT REPEAT 92..113
FT /note="LRR 1"
FT REPEAT 116..137
FT /note="LRR 2"
FT DOMAIN 149..199
FT /note="LRRCT"
FT REPEAT 201..243
FT /note="EAR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 247..289
FT /note="EAR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 293..340
FT /note="EAR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 342..391
FT /note="EAR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 395..438
FT /note="EAR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 440..482
FT /note="EAR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT REPEAT 486..528
FT /note="EAR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00075"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 533 AA; 61161 MW; 2D812184A01514A4 CRC64;
MESERSQRMG NACIPLKRIA YCLCLLSALL LTEGKKPAKP KCPAVCTCTK DNALCENARS
IPRTVPPDVI SLLFTSNSFD VISDDAFIGL PHLEYLFIEN NNIKSISRHT FRGLKSLIHL
SLANNNLQTL PKDIFKGLDS LTNVDLRGNS FNCDCKLKWL VEWLSHTNAT VEDIYCEGPP
EYKKRKINSL SSKDFDCIIT EFAKSQDLPY QSLSIDTFSY MNDEYVVIAQ PFTGKCIFLE
WDHVEKTFRN YDNITGTSTV VCKPIVIETQ LYVIVAQLFG GSHIYKRDSF ANKFIKIQDI
EILKIRKPND IETFKIENNW YFVVADSSKA GFTTIYKWNG NGFYSHQSLH AWYRDTDVEY
LEIARTPQTL RTPHLILSSS SQRPVIYQWN KAIQLFTNQT DIPNMEDVYA VKHFSVKGDV
YICLTRFIGD SKVMKWGGSS FQDIQRMPSR GSMVFQPLQI NNYQYAILGS DYSFTQVYNW
DAEKAKFVKF QELNVQAPRS FTHVSINKRN FLFASSFKGN TQIYKHVIVD LSA
