NLGN1_MOUSE
ID NLGN1_MOUSE Reviewed; 843 AA.
AC Q99K10;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Neuroligin-1;
DE Flags: Precursor;
GN Name=Nlgn1; Synonyms=Kiaa1070;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.
RX PubMed=10892652; DOI=10.1016/s0092-8674(00)80877-6;
RA Scheiffele P., Fan J., Choih J., Fetter R., Serafini T.;
RT "Neuroligin expressed in nonneuronal cells triggers presynaptic development
RT in contacting axons.";
RL Cell 101:657-669(2000).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11329178; DOI=10.1002/glia.1050;
RA Gilbert M., Smith J., Roskams A.J., Auld V.J.;
RT "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory
RT ensheathing glia, a growth-promoting class of macroglia.";
RL Glia 34:151-164(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15620359; DOI=10.1016/j.cell.2004.11.035;
RA Graf E.R., Zhang X., Jin S.X., Linhoff M.W., Craig A.M.;
RT "Neurexins induce differentiation of GABA and glutamate postsynaptic
RT specializations via neuroligins.";
RL Cell 119:1013-1026(2004).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16982420; DOI=10.1016/j.neuron.2006.09.003;
RA Varoqueaux F., Aramuni G., Rawson R.L., Mohrmann R., Missler M.,
RA Gottmann K., Zhang W., Sudhof T.C., Brose N.;
RT "Neuroligins determine synapse maturation and function.";
RL Neuron 51:741-754(2006).
RN [7]
RP INTERACTION WITH NLGN3.
RX PubMed=17897391; DOI=10.1111/j.1460-9568.2007.05842.x;
RA Budreck E.C., Scheiffele P.;
RT "Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic
RT synapses.";
RL Eur. J. Neurosci. 26:1738-1748(2007).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=18434543; DOI=10.1073/pnas.0801383105;
RA Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V.,
RA Sudhof T.C.;
RT "Unusually rapid evolution of neuroligin-4 in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=19926856; DOI=10.1073/pnas.0809510106;
RA Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B.,
RA Cera M.R., Mascia L., Bussolino F., Arese M.;
RT "The synaptic proteins neurexins and neuroligins are widely expressed in
RT the vascular system and contribute to its functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009).
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).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=20147539; DOI=10.1523/jneurosci.4517-09.2010;
RA Blundell J., Blaiss C.A., Etherton M.R., Espinosa F., Tabuchi K., Walz C.,
RA Bolliger M.F., Sudhof T.C., Powell C.M.;
RT "Neuroligin-1 deletion results in impaired spatial memory and increased
RT repetitive behavior.";
RL J. Neurosci. 30:2115-2129(2010).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=23716671; DOI=10.1073/pnas.1221381110;
RA El Helou J., Belanger-Nelson E., Freyburger M., Dorsaz S., Curie T.,
RA La Spada F., Gaudreault P.O., Beaumont E., Pouliot P., Lesage F.,
RA Frank M.G., Franken P., Mongrain V.;
RT "Neuroligin-1 links neuronal activity to sleep-wake regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9974-9979(2013).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF PRO-89; THR-90; LEU-289; GLY-317; ARG-736 AND
RP HIS-815.
RX PubMed=28841651; DOI=10.1371/journal.pgen.1006940;
RA Nakanishi M., Nomura J., Ji X., Tamada K., Arai T., Takahashi E., Bucan M.,
RA Takumi T.;
RT "Functional significance of rare neuroligin 1 variants found in autism.";
RL PLoS Genet. 13:e1006940-e1006940(2017).
RN [14]
RP ERRATUM OF PUBMED:28841651.
RX PubMed=28972980; DOI=10.1371/journal.pgen.1007035;
RA Nakanishi M., Nomura J., Ji X., Tamada K., Arai T., Takahashi E., Bucan M.,
RA Takumi T.;
RT "Correction: Functional significance of rare neuroligin 1 variants found in
RT autism.";
RL PLoS Genet. 13:e1007035-e1007035(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 39-635 IN COMPLEX WITH HUMAN
RP NRX1B, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-109 AND ASN-547.
RX PubMed=18084303; DOI=10.1038/nsmb1350;
RA Chen X., Liu H., Shim A.H., Focia P.J., He X.;
RT "Structural basis for synaptic adhesion mediated by neuroligin-neurexin
RT interactions.";
RL Nat. Struct. Mol. Biol. 15:50-56(2008).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions via
CC its interactions with neurexin family members. Plays a role in synapse
CC function and synaptic signal transmission, and probably mediates its
CC effects by recruiting and clustering other synaptic proteins. May
CC promote the initial formation of synapses, but is not essential for
CC this. In vitro, triggers the de novo formation of presynaptic
CC structures. May be involved in specification of excitatory synapses.
CC Required to maintain wakefulness quality and normal synchrony of
CC cerebral cortex activity during wakefulness and sleep
CC (PubMed:23716671). The protein is involved in nervous system
CC development. {ECO:0000269|PubMed:10892652, ECO:0000269|PubMed:15620359,
CC ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:23716671,
CC ECO:0000269|PubMed:28841651}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-
CC terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with AIP1,
CC GOPC and PDZRN3 (By similarity). Interacts with NLGN3. {ECO:0000250,
CC ECO:0000269|PubMed:17897391, ECO:0000269|PubMed:18084303}.
CC -!- INTERACTION:
CC Q99K10; P97924-5: Kalrn; Xeno; NbExp=2; IntAct=EBI-775037, EBI-26961214;
CC Q99K10; O14522: PTPRT; Xeno; NbExp=2; IntAct=EBI-775037, EBI-728180;
CC Q99K10-1; P58400-1: NRXN1; Xeno; NbExp=3; IntAct=EBI-15675933, EBI-16513622;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62765};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62765}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q62765}. Synaptic cleft
CC {ECO:0000250|UniProtKB:Q62765}. Synaptic cell membrane
CC {ECO:0000250|UniProtKB:Q62765}. Note=Enriched in synaptic plasma
CC membranes and clustered in synaptic clefts and postsynaptic densities.
CC Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1.
CC {ECO:0000250|UniProtKB:Q62765}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99K10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99K10-2; Sequence=VSP_007528, VSP_007529, VSP_007530;
CC -!- TISSUE SPECIFICITY: Brain and arteries (at protein level). Expressed in
CC olfactory bulb. Detected in brain. {ECO:0000269|PubMed:11329178,
CC ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:18434543,
CC ECO:0000269|PubMed:19926856}.
CC -!- INDUCTION: Expressed in a circadian manner in the brain with highest
CC expression seen at Zeitgeber time (ZT) 6 hours.
CC {ECO:0000269|PubMed:23716671}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype, but mice present subtle
CC behavorial changes with some deficits in spatial learning and memory.
CC In addition, mice have reduced brain volume. Mice lacking both NLGN1
CC and NLGN2, or NLGN1 and NLGN3, are viable, but have impaired breathing,
CC drastically reduced reproduction rates and striking deficits in raising
CC their offspring. Mice lacking NLGN1, NLGN2 and NLGN3 are born at the
CC expected Mendelian rate, but die shortly after birth due to respiratory
CC failure. They do not show a significant change in the number of
CC synapses, but synapse function is strongly impaired. Mice exhibit
CC social novelty and fear-conditioning deficits and also show reduced
CC wakefulness duration and altered EEG during wakefulness and sleep.
CC {ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:20147539,
CC ECO:0000269|PubMed:23716671}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65715.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122433; BAC65715.1; ALT_INIT; mRNA.
DR EMBL; BC005523; AAH05523.1; -; mRNA.
DR CCDS; CCDS17268.1; -. [Q99K10-1]
DR RefSeq; NP_619607.2; NM_138666.3. [Q99K10-1]
DR PDB; 3B3Q; X-ray; 2.40 A; A/B=46-635.
DR PDBsum; 3B3Q; -.
DR AlphaFoldDB; Q99K10; -.
DR SMR; Q99K10; -.
DR BioGRID; 228657; 2.
DR ComplexPortal; CPX-4122; NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex.
DR DIP; DIP-32027N; -.
DR IntAct; Q99K10; 5.
DR MINT; Q99K10; -.
DR STRING; 10090.ENSMUSP00000074565; -.
DR ESTHER; mouse-1neur; Neuroligin.
DR MEROPS; S09.994; -.
DR GlyGen; Q99K10; 7 sites.
DR iPTMnet; Q99K10; -.
DR PhosphoSitePlus; Q99K10; -.
DR MaxQB; Q99K10; -.
DR PaxDb; Q99K10; -.
DR PeptideAtlas; Q99K10; -.
DR PRIDE; Q99K10; -.
DR ProteomicsDB; 293573; -. [Q99K10-1]
DR ProteomicsDB; 293574; -. [Q99K10-2]
DR ABCD; Q99K10; 1 sequenced antibody.
DR Antibodypedia; 1513; 297 antibodies from 35 providers.
DR DNASU; 192167; -.
DR Ensembl; ENSMUST00000075054; ENSMUSP00000074565; ENSMUSG00000063887. [Q99K10-1]
DR Ensembl; ENSMUST00000193603; ENSMUSP00000142200; ENSMUSG00000063887. [Q99K10-1]
DR GeneID; 192167; -.
DR KEGG; mmu:192167; -.
DR UCSC; uc008otc.1; mouse. [Q99K10-1]
DR UCSC; uc008otd.1; mouse. [Q99K10-2]
DR CTD; 22871; -.
DR MGI; MGI:2179435; Nlgn1.
DR VEuPathDB; HostDB:ENSMUSG00000063887; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000155789; -.
DR InParanoid; Q99K10; -.
DR OMA; HDMVLRT; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q99K10; -.
DR TreeFam; TF326187; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 192167; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Nlgn1; mouse.
DR EvolutionaryTrace; Q99K10; -.
DR PRO; PR:Q99K10; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99K10; protein.
DR Bgee; ENSMUSG00000063887; Expressed in olfactory tubercle and 119 other tissues.
DR ExpressionAtlas; Q99K10; baseline and differential.
DR Genevisible; Q99K10; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IC:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0032433; C:filopodium tip; ISS:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISS:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IC:ComplexPortal.
DR GO; GO:0098984; C:neuron to neuron synapse; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0042043; F:neurexin family protein binding; IMP:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IDA:BHF-UCL.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0090125; P:cell-cell adhesion involved in synapse maturation; IC:ComplexPortal.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0048789; P:cytoskeletal matrix organization at active zone; IMP:BHF-UCL.
DR GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
DR GO; GO:1904861; P:excitatory synapse assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0099558; P:maintenance of synapse structure; IC:ComplexPortal.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IGI:MGI.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IDA:UniProtKB.
DR GO; GO:0097115; P:neurexin clustering involved in presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0140058; P:neuron projection arborization; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IC:ComplexPortal.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; ISS:BHF-UCL.
DR GO; GO:0010841; P:positive regulation of circadian sleep/wake cycle, wakefulness; IMP:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:BHF-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:BHF-UCL.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:MGI.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IC:ComplexPortal.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IC:ComplexPortal.
DR GO; GO:1905520; P:positive regulation of presynaptic active zone assembly; ISO:MGI.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; ISO:MGI.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISS:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IDA:BHF-UCL.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:BHF-UCL.
DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IDA:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0098698; P:postsynaptic specialization assembly; IDA:SynGO.
DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0035418; P:protein localization to synapse; IDA:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; ISO:MGI.
DR GO; GO:0097120; P:receptor localization to synapse; IDA:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:0045664; P:regulation of neuron differentiation; IDA:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IDA:BHF-UCL.
DR GO; GO:0099174; P:regulation of presynapse organization; ISO:MGI.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IGI:MGI.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; ISO:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007416; P:synapse assembly; IDA:UniProtKB.
DR GO; GO:0060074; P:synapse maturation; IC:ComplexPortal.
DR GO; GO:0050808; P:synapse organization; IGI:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:BHF-UCL.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0016080; P:synaptic vesicle targeting; IMP:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; ISO:MGI.
DR GO; GO:0072553; P:terminal button organization; IMP:BHF-UCL.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000460; Nlgn.
DR InterPro; IPR030022; NLGN1.
DR PANTHER; PTHR43903:SF2; PTHR43903:SF2; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR01090; NEUROLIGIN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Cell adhesion;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Secreted; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..843
FT /note="Neuroligin-1"
FT /id="PRO_0000008641"
FT TOPO_DOM 46..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 167..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:18084303"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18084303"
FT CARBOHYD 683
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 686
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 117..153
FT /evidence="ECO:0000269|PubMed:18084303"
FT DISULFID 342..353
FT /evidence="ECO:0000269|PubMed:18084303"
FT DISULFID 512..546
FT /evidence="ECO:0000269|PubMed:18084303"
FT VAR_SEQ 165..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007528"
FT VAR_SEQ 236..269
FT /note="GFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFG -> EKETIKETISVALQ
FT ALRTKGGGFIPKQATYKRCE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007529"
FT VAR_SEQ 270..843
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007530"
FT MUTAGEN 89
FT /note="P->L: Decreased protein abundance. Not delivered to
FT the plasma membrane. Heterozygotes mice with this mutation
FT display abnormal social behavior."
FT /evidence="ECO:0000269|PubMed:28841651"
FT MUTAGEN 90
FT /note="T->I: No effect on protein abundance. Not associated
FT with changes in subcellular location."
FT /evidence="ECO:0000269|PubMed:28841651"
FT MUTAGEN 289
FT /note="L->P: Decreased protein abundance. Not delivered to
FT the plasma membrane."
FT /evidence="ECO:0000269|PubMed:28841651"
FT MUTAGEN 317
FT /note="G->E: Decreased protein abundance. Not delivered to
FT the plasma membrane."
FT /evidence="ECO:0000269|PubMed:28841651"
FT MUTAGEN 736
FT /note="R->H: Not associated with changes in subcellular
FT location."
FT /evidence="ECO:0000269|PubMed:28841651"
FT MUTAGEN 815
FT /note="H->Y: Decreased protein abundance. Not associated
FT with changes in subcellular location."
FT /evidence="ECO:0000269|PubMed:28841651"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3B3Q"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 329..339
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3B3Q"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 428..443
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 469..484
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 486..498
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:3B3Q"
FT TURN 525..528
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:3B3Q"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 550..569
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 572..576
FT /evidence="ECO:0007829|PDB:3B3Q"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 620..627
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 630..633
FT /evidence="ECO:0007829|PDB:3B3Q"
SQ SEQUENCE 843 AA; 94149 MW; 69E50709CF7D2E1F CRC64;
MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD VDPLVTTNFG
KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP PSPWSDIRNA TQFAPVCPQN
IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDGPLTKK HTDDLGDNDG
AEDEDIRDSG GPKPVMVYIH GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST
GDQAAKGNYG LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR
WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL VECLQKKPYK
ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN YDIMLGVNQG EGLKFVENIV
DSDDGVSASD FDFAVSNFVD NLYGYPEGKD VLRETIKFMY TDWADRHNPE TRRKTLLALF
TDHQWVAPAV ATADLHSNFG SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP
TELFPCNFSK NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ
KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP STDITLRPTR
KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI AVGASLLFLN ILAFAALYYK
KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI MSLQMKHTDL DHECESIHPH EVVLRTACPP
DYTLAMRRSP DDIPLMTPNT ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST
TRV
