NLGN1_RAT
ID NLGN1_RAT Reviewed; 843 AA.
AC Q62765;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Neuroligin-1;
DE AltName: Full=Neuroligin I;
DE Flags: Precursor;
GN Name=Nlgn1;
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] (ISOFORMS 1; 2; 3 AND 4), PARTIAL PROTEIN
RP SEQUENCE, CHARACTERIZATION, AND INTERACTION WITH NEUREXIN 1-BETA.
RC TISSUE=Brain;
RX PubMed=7736595; DOI=10.1016/0092-8674(95)90396-8;
RA Ichtchenko K., Hata Y., Nguyen T., Ullrich B., Missler M., Moomaw C.,
RA Suedhof T.C.;
RT "Neuroligin 1: a splice site-specific ligand for beta-neurexins.";
RL Cell 81:435-443(1995).
RN [2]
RP INTERACTION WITH NEUREXIN 1-BETA, AND FUNCTION.
RX PubMed=9325340; DOI=10.1074/jbc.272.41.26032;
RA Nguyen T., Suedhof T.C.;
RT "Binding properties of neuroligin 1 and neurexin 1beta reveal function as
RT heterophilic cell adhesion molecules.";
RL J. Biol. Chem. 272:26032-26039(1997).
RN [3]
RP BLOCKAGE OF N-TERMINUS, AND INTERACTION WITH NEUREXIN 1-BETA; NEUREXIN
RP 2-BETA AND NEUREXIN 3-BETA.
RX PubMed=8576240; DOI=10.1074/jbc.271.5.2676;
RA Ichtchenko K., Nguyen T., Suedhof T.C.;
RT "Structures, alternative splicing, and neurexin binding of multiple
RT neuroligins.";
RL J. Biol. Chem. 271:2676-2682(1996).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9927700; DOI=10.1073/pnas.96.3.1100;
RA Song J.-Y., Ichtchenko K., Suedhof T.C., Brose N.;
RT "Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory
RT synapses.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1100-1105(1999).
RN [5]
RP INTERACTION WITH AIP1.
RX PubMed=9694864; DOI=10.1074/jbc.273.33.21105;
RA Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M.,
RA Toyoda A., Suedhof T.C., Takai Y.;
RT "A novel multiple PDZ domain-containing molecule interacting with N-methyl-
RT d-aspartate receptors and neuronal cell adhesion proteins.";
RL J. Biol. Chem. 273:21105-21110(1998).
RN [6]
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 [7]
RP DISULFIDE BONDS, AND GLYCOSYLATION.
RX PubMed=14769026; DOI=10.1021/bi035278t;
RA Hoffman R.C., Jennings L.L., Tsigelny I., Comoletti D., Flynn R.E.,
RA Suedhof T.C., Taylor P.;
RT "Structural characterization of recombinant soluble rat neuroligin 1:
RT mapping of secondary structure and glycosylation by mass spectrometry.";
RL Biochemistry 43:1496-1506(2004).
RN [8]
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 [9]
RP INTERACTION WITH PDZRN3.
RX PubMed=15458844; DOI=10.1016/j.neuropharm.2004.06.023;
RA Meyer G., Varoqueaux F., Neeb A., Oschlies M., Brose N.;
RT "The complexity of PDZ domain-mediated interactions at glutamatergic
RT synapses: a case study on neuroligin.";
RL Neuropharmacology 47:724-733(2004).
RN [10]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=18755801; DOI=10.1210/en.2008-0274;
RA Suckow A.T., Comoletti D., Waldrop M.A., Mosedale M., Egodage S.,
RA Taylor P., Chessler S.D.;
RT "Expression of neurexin, neuroligin, and their cytoplasmic binding partners
RT in the pancreatic beta-cells and the involvement of neuroligin in insulin
RT secretion.";
RL Endocrinology 149:6006-6017(2008).
RN [11]
RP SUBCELLULAR LOCATION.
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 [12]
RP INTERACTION WITH NRXN1.
RX PubMed=18334216; DOI=10.1016/j.str.2007.12.024;
RA Koehnke J., Jin X., Trbovic N., Katsamba P.S., Brasch J., Ahlsen G.,
RA Scheiffele P., Honig B., Palmer A.G. III, Shapiro L.;
RT "Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and
RT dynamics of splice insertion sequence 4.";
RL Structure 16:410-421(2008).
RN [13]
RP INTERACTION WITH NRXN1.
RX PubMed=20624592; DOI=10.1016/j.neuron.2010.06.001;
RA Koehnke J., Katsamba P.S., Ahlsen G., Bahna F., Vendome J., Honig B.,
RA Shapiro L., Jin X.;
RT "Splice form dependence of beta-neurexin/neuroligin binding interactions.";
RL Neuron 67:61-74(2010).
RN [14]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19914352; DOI=10.1016/j.neuroscience.2009.11.016;
RA Levinson J.N., Li R., Kang R., Moukhles H., El-Husseini A., Bamji S.X.;
RT "Postsynaptic scaffolding molecules modulate the localization of
RT neuroligins.";
RL Neuroscience 165:782-793(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 46-638 IN COMPLEX WITH NRXN1,
RP GLYCOSYLATION AT ASN-109 AND ASN-343, AND DISULFIDE BONDS.
RX PubMed=18093522; DOI=10.1016/j.neuron.2007.12.002;
RA Arac D., Boucard A.A., Ozkan E., Strop P., Newell E., Sudhof T.C.,
RA Brunger A.T.;
RT "Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex
RT reveal specific protein-protein and protein-Ca2+ interactions.";
RL Neuron 56:992-1003(2007).
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 (By similarity).
CC The protein is involved in nervous system development.
CC {ECO:0000250|UniProtKB:Q99K10, ECO:0000269|PubMed:15620359,
CC ECO:0000269|PubMed:9325340}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts with NLGN3.
CC Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3).
CC Interacts with GOPC (By similarity). Interacts with AIP1 and PDZRN3.
CC {ECO:0000250, ECO:0000269|PubMed:15458844, ECO:0000269|PubMed:18093522,
CC ECO:0000269|PubMed:18334216, ECO:0000269|PubMed:20624592,
CC ECO:0000269|PubMed:7736595, ECO:0000269|PubMed:8576240,
CC ECO:0000269|PubMed:9325340, ECO:0000269|PubMed:9694864}.
CC -!- INTERACTION:
CC Q62765; P97924-5: Kalrn; NbExp=5; IntAct=EBI-7281118, EBI-26961214;
CC Q62765; F1M0Z1: Trio; NbExp=2; IntAct=EBI-7281118, EBI-26961238;
CC Q62765-2; Q63373-3: Nrxn1; NbExp=5; IntAct=EBI-20994039, EBI-20994045;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Postsynaptic density {ECO:0000269|PubMed:18434543,
CC ECO:0000269|PubMed:19914352, ECO:0000269|PubMed:9927700}. Synaptic
CC cleft {ECO:0000269|PubMed:9927700}. Synaptic cell membrane
CC {ECO:0000269|PubMed:9927700}. 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:0000269|PubMed:19914352, ECO:0000269|PubMed:9927700}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q62765-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62765-2; Sequence=VSP_007531, VSP_007532;
CC Name=3;
CC IsoId=Q62765-3; Sequence=VSP_007532;
CC Name=4;
CC IsoId=Q62765-4; Sequence=VSP_007531;
CC -!- TISSUE SPECIFICITY: Expressed in brain, almost exclusively in neurons,
CC and spinal chord. Detected in pancreas islet beta cells.
CC {ECO:0000269|PubMed:11329178, ECO:0000269|PubMed:18755801,
CC ECO:0000269|PubMed:19914352, ECO:0000269|PubMed:9927700}.
CC -!- DEVELOPMENTAL STAGE: Expression is low in embryonic brains (E12-E16)
CC but increases dramatically after birth (postnatal days P0-P3) and
CC reaches a plateau during the period when most synapses are formed (P5-
CC P8). {ECO:0000269|PubMed:9927700}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; U22952; AAA85720.1; -; mRNA.
DR RefSeq; NP_446320.1; NM_053868.2. [Q62765-1]
DR RefSeq; XP_017446072.1; XM_017590583.1. [Q62765-4]
DR RefSeq; XP_017446073.1; XM_017590584.1. [Q62765-4]
DR RefSeq; XP_017446074.1; XM_017590585.1. [Q62765-4]
DR RefSeq; XP_017446075.1; XM_017590586.1. [Q62765-4]
DR RefSeq; XP_017446076.1; XM_017590587.1. [Q62765-4]
DR RefSeq; XP_017446077.1; XM_017590588.1. [Q62765-4]
DR RefSeq; XP_017446078.1; XM_017590589.1. [Q62765-4]
DR RefSeq; XP_017446079.1; XM_017590590.1. [Q62765-2]
DR PDB; 3BIW; X-ray; 3.50 A; A/B/C/D=46-638.
DR PDB; 3BIX; X-ray; 1.80 A; A/B/C/D=46-638.
DR PDB; 3VKF; X-ray; 3.30 A; A/B=45-638.
DR PDBsum; 3BIW; -.
DR PDBsum; 3BIX; -.
DR PDBsum; 3VKF; -.
DR AlphaFoldDB; Q62765; -.
DR SMR; Q62765; -.
DR BioGRID; 250532; 12.
DR ComplexPortal; CPX-4061; NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex. [Q62765-2]
DR ComplexPortal; CPX-4123; NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex.
DR DIP; DIP-44832N; -.
DR IntAct; Q62765; 7.
DR MINT; Q62765; -.
DR STRING; 10116.ENSRNOP00000049486; -.
DR ESTHER; ratno-1neur; Neuroligin.
DR MEROPS; S09.994; -.
DR GlyConnect; 433; 28 N-Linked glycans, 3 O-Linked glycans.
DR GlyGen; Q62765; 7 sites, 54 N-linked glycans (1 site), 6 O-linked glycans (1 site).
DR iPTMnet; Q62765; -.
DR PhosphoSitePlus; Q62765; -.
DR PaxDb; Q62765; -.
DR PRIDE; Q62765; -.
DR ABCD; Q62765; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000041111; ENSRNOP00000040172; ENSRNOG00000032576. [Q62765-1]
DR Ensembl; ENSRNOT00000092660; ENSRNOP00000075793; ENSRNOG00000032576. [Q62765-4]
DR GeneID; 116647; -.
DR KEGG; rno:116647; -.
DR UCSC; RGD:621117; rat. [Q62765-1]
DR CTD; 22871; -.
DR RGD; 621117; Nlgn1.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000155789; -.
DR HOGENOM; CLU_006586_5_1_1; -.
DR InParanoid; Q62765; -.
DR OMA; HDMVLRT; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q62765; -.
DR TreeFam; TF326187; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR EvolutionaryTrace; Q62765; -.
DR PRO; PR:Q62765; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000032576; Expressed in frontal cortex and 7 other tissues.
DR ExpressionAtlas; Q62765; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IC:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0032433; C:filopodium tip; IDA:BHF-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IC:ComplexPortal.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0060077; C:inhibitory synapse; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA: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; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0098635; C:protein complex involved in cell-cell adhesion; IPI:ComplexPortal.
DR GO; GO:0043235; C:receptor complex; ISS:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0043083; C:synaptic cleft; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0042043; F:neurexin family protein binding; IPI:ARUK-UCL.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IMP:BHF-UCL.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR GO; GO:0090125; P:cell-cell adhesion involved in synapse maturation; IC:ComplexPortal.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:ARUK-UCL.
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; ISS:BHF-UCL.
DR GO; GO:1904861; P:excitatory synapse assembly; ISO:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:RGD.
DR GO; GO:0099558; P:maintenance of synapse structure; IC:ComplexPortal.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:ARUK-UCL.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0097115; P:neurexin clustering involved in presynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0140058; P:neuron projection arborization; IGI:ARUK-UCL.
DR GO; GO:0031175; P:neuron projection development; IGI:ARUK-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; IC:ComplexPortal.
DR GO; GO:0045161; P:neuronal ion channel clustering; TAS:UniProtKB.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; IDA:BHF-UCL.
DR GO; GO:0010841; P:positive regulation of circadian sleep/wake cycle, wakefulness; ISS:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IDA: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; IDA:BHF-UCL.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IMP:RGD.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IDA:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:BHF-UCL.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:BHF-UCL.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:RGD.
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; ISS:BHF-UCL.
DR GO; GO:0098698; P:postsynaptic specialization assembly; ISO:RGD.
DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; IDA:UniProtKB.
DR GO; GO:0097120; P:receptor localization to synapse; ISS:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:BHF-UCL.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IDA:BHF-UCL.
DR GO; GO:0099174; P:regulation of presynapse organization; IDA:SynGO.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISO:RGD.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IMP:SynGO.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007416; P:synapse assembly; IDA:BHF-UCL.
DR GO; GO:0060074; P:synapse maturation; IC:ComplexPortal.
DR GO; GO:0050808; P:synapse organization; IDA:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:CACAO.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Secreted; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..843
FT /note="Neuroligin-1"
FT /id="PRO_0000008642"
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 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:18093522"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14769026"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:18093522"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14769026"
FT CARBOHYD 683
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:14769026"
FT CARBOHYD 686
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:14769026"
FT DISULFID 117..153
FT DISULFID 172..181
FT DISULFID 342..353
FT DISULFID 512..546
FT VAR_SEQ 165..184
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:7736595"
FT /id="VSP_007531"
FT VAR_SEQ 298..306
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7736595"
FT /id="VSP_007532"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3BIX"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3VKF"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:3BIX"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:3BIX"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 428..443
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 452..459
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 469..484
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 486..498
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:3VKF"
FT TURN 525..528
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 550..569
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:3BIX"
FT TURN 589..592
FT /evidence="ECO:0007829|PDB:3BIX"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:3BIX"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 620..627
FT /evidence="ECO:0007829|PDB:3BIX"
FT HELIX 629..634
FT /evidence="ECO:0007829|PDB:3BIX"
SQ SEQUENCE 843 AA; 94294 MW; 90A18540245B789D CRC64;
MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD VDPLVTTNFG
KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP PSPWSDIRNA TQFAPVCPQN
IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDVKRISK ECARKPGKKI
CRKGDIRDSG 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 DDVPLMTPNT ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST
TRV
