NLGN2_MOUSE
ID NLGN2_MOUSE Reviewed; 836 AA.
AC Q69ZK9; Q5F288;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Neuroligin-2;
DE Flags: Precursor;
GN Name=Nlgn2; Synonyms=Kiaa1366;
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].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 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 [5]
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 [6]
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 [7]
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 [8]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19553444; DOI=10.1523/jneurosci.0534-09.2009;
RA Hoon M., Bauer G., Fritschy J.M., Moser T., Falkenburger B.H.,
RA Varoqueaux F.;
RT "Neuroligin 2 controls the maturation of GABAergic synapses and information
RT processing in the retina.";
RL J. Neurosci. 29:8039-8050(2009).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19889999; DOI=10.1523/jneurosci.2457-09.2009;
RA Gibson J.R., Huber K.M., Sudhof T.C.;
RT "Neuroligin-2 deletion selectively decreases inhibitory synaptic
RT transmission originating from fast-spiking but not from somatostatin-
RT positive interneurons.";
RL J. Neurosci. 29:13883-13897(2009).
RN [10]
RP INTERACTION WITH GPHN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19755106; DOI=10.1016/j.neuron.2009.08.023;
RA Poulopoulos A., Aramuni G., Meyer G., Soykan T., Hoon M., Papadopoulos T.,
RA Zhang M., Paarmann I., Fuchs C., Harvey K., Jedlicka P., Schwarzacher S.W.,
RA Betz H., Harvey R.J., Brose N., Zhang W., Varoqueaux F.;
RT "Neuroligin 2 drives postsynaptic assembly at perisomatic inhibitory
RT synapses through gephyrin and collybistin.";
RL Neuron 63:628-642(2009).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714 AND SER-719, AND
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 [13]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19859968; DOI=10.1002/jnr.22258;
RA Lui L., Levinson J.N., Noel G., Handrigan G.R., Richman J.M.,
RA El-Husseini A., Moukhles H.;
RT "Synaptic localization of neuroligin 2 in the rodent retina: comparative
RT study with the dystroglycan-containing complex.";
RL J. Neurosci. Res. 88:837-849(2010).
RN [14]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20530218; DOI=10.1093/cercor/bhq100;
RA Jedlicka P., Hoon M., Papadopoulos T., Vlachos A., Winkels R.,
RA Poulopoulos A., Betz H., Deller T., Brose N., Varoqueaux F.,
RA Schwarzacher S.W.;
RT "Increased dentate gyrus excitability in neuroligin-2-deficient mice in
RT vivo.";
RL Cereb. Cortex 21:357-367(2011).
RN [15]
RP INTERACTION WITH MDGA1.
RX PubMed=23358245; DOI=10.1083/jcb.201206028;
RA Pettem K.L., Yokomaku D., Takahashi H., Ge Y., Craig A.M.;
RT "Interaction between autism-linked MDGAs and neuroligins suppresses
RT inhibitory synapse development.";
RL J. Cell Biol. 200:321-336(2013).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH MAGI2 AND IGSF9B.
RX PubMed=23751499; DOI=10.1083/jcb.201209132;
RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J.,
RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S.,
RA Craig A.M., Kim E.;
RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to
RT promote inhibitory synapse development.";
RL J. Cell Biol. 201:929-944(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 42-612, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-98.
RX PubMed=18250328; DOI=10.1073/pnas.0711701105;
RA Koehnke J., Jin X., Budreck E.C., Posy S., Scheiffele P., Honig B.,
RA Shapiro L.;
RT "Crystal structure of the extracellular cholinesterase-like domain from
RT neuroligin-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1873-1878(2008).
RN [18]
RP INTERACTION WITH LHFPL4.
RX PubMed=28279354; DOI=10.1016/j.neuron.2017.02.023;
RA Yamasaki T., Hoyos-Ramirez E., Martenson J.S., Morimoto-Tomita M.,
RA Tomita S.;
RT "GARLH family proteins stabilize GABAA receptors at synapses.";
RL Neuron 93:1138-1152(2017).
RN [19]
RP INTERACTION WITH LHFPL4, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29742426; DOI=10.1016/j.celrep.2018.04.015;
RA Wu M., Tian H.L., Liu X., Lai J.H.C., Du S., Xia J.;
RT "Impairment of inhibitory synapse formation and motor behavior in mice
RT lacking the NL2 binding partner LHFPL4/GARLH4.";
RL Cell Rep. 23:1691-1705(2018).
CC -!- FUNCTION: Transmembrane scaffolding protein involved in cell-cell
CC interactions via its interactions with neurexin family members.
CC Mediates cell-cell interactions both in neurons and in other types of
CC cells, such as Langerhans beta cells. Mediates cell-cell interactions
CC between Langerhans beta cells and modulates insulin secretion (By
CC similarity). Plays a role in synapse function and synaptic signal
CC transmission, especially via gamma-aminobutyric acid receptors (GABA(A)
CC receptors). Functions by recruiting and clustering synaptic proteins.
CC Promotes clustering of postsynaptic GABRG2 and GPHN. Promotes
CC clustering of postsynaptic LHFPL4 (PubMed:29742426). Modulates
CC signaling by inhibitory synapses, and thereby plays a role in
CC controlling the ratio of signaling by excitatory and inhibitory
CC synapses and information processing. Required for normal signal
CC amplitude from inhibitory synapses, but is not essential for normal
CC signal frequency. May promote the initial formation of synapses, but is
CC not essential for this. In vitro, triggers the de novo formation of
CC presynaptic structures. {ECO:0000250, ECO:0000269|PubMed:10892652,
CC ECO:0000269|PubMed:15620359, ECO:0000269|PubMed:16982420,
CC ECO:0000269|PubMed:19553444, ECO:0000269|PubMed:19889999,
CC ECO:0000269|PubMed:20530218, ECO:0000269|PubMed:29742426}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-
CC terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with PATJ (By
CC similarity). Interacts with MDGA2 (By similarity). Interacts with GPHN
CC (PubMed:19755106). Interacts with MDGA1 (PubMed:23358245). Found in a
CC complex with MAGI2 and IGSF9B, where it interacts with MAGI2 (via WW 1,
CC WW 2 and PDZ 2 domains) (PubMed:23751499). Identified in a complex of
CC 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3
CC (By similarity). Interacts with LHFPL4; leading to mutual regulation of
CC the protein level and synaptic clustering (PubMed:29742426,
CC PubMed:28279354). Interacts with GABRA1 (By similarity).
CC {ECO:0000250|UniProtKB:Q62888, ECO:0000250|UniProtKB:Q8NFZ4,
CC ECO:0000269|PubMed:17897391, ECO:0000269|PubMed:19755106,
CC ECO:0000269|PubMed:23358245, ECO:0000269|PubMed:28279354,
CC ECO:0000269|PubMed:29742426}.
CC -!- INTERACTION:
CC Q69ZK9; Q69ZK9: Nlgn2; NbExp=2; IntAct=EBI-775065, EBI-775065;
CC Q69ZK9; O14522: PTPRT; Xeno; NbExp=2; IntAct=EBI-775065, EBI-728180;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Postsynaptic cell membrane {ECO:0000269|PubMed:29742426}.
CC Presynaptic cell membrane. Note=Detected at postsynaptic membranes in
CC brain. Detected at dendritic spines in cultured neurons. Colocalizes
CC with GPHN and ARHGEF9 at neuronal cell membranes (By similarity).
CC Localized at presynaptic membranes in retina. Colocalizes with GABRG2
CC at inhibitory synapses in the retina. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain and arteries. Detected in the retina outer
CC plexiform layer (at protein level). Widely expressed. Detected in
CC heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.
CC {ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:18434543,
CC ECO:0000269|PubMed:19755106, ECO:0000269|PubMed:19859968,
CC ECO:0000269|PubMed:19926856}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype, but mice present subtle
CC behavorial changes. Signaling from inhibitory synapses is impaired. In
CC addition, mice have reduced brain volume. Mice lacking both NLGN1 and
CC NLGN2, or NLGN2 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.
CC {ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:19553444,
CC ECO:0000269|PubMed:19889999, ECO:0000269|PubMed:20530218}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32437.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173159; BAD32437.1; ALT_INIT; mRNA.
DR EMBL; AL603707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24914.1; -.
DR RefSeq; NP_942562.2; NM_198862.2.
DR RefSeq; XP_006532964.1; XM_006532901.2.
DR PDB; 3BL8; X-ray; 3.30 A; A/B/C/D=42-612.
DR PDBsum; 3BL8; -.
DR AlphaFoldDB; Q69ZK9; -.
DR SMR; Q69ZK9; -.
DR BioGRID; 229806; 6.
DR CORUM; Q69ZK9; -.
DR DIP; DIP-29702N; -.
DR IntAct; Q69ZK9; 4.
DR MINT; Q69ZK9; -.
DR STRING; 10090.ENSMUSP00000053097; -.
DR ESTHER; mouse-2neur; Neuroligin.
DR GlyGen; Q69ZK9; 3 sites.
DR iPTMnet; Q69ZK9; -.
DR PhosphoSitePlus; Q69ZK9; -.
DR SwissPalm; Q69ZK9; -.
DR EPD; Q69ZK9; -.
DR MaxQB; Q69ZK9; -.
DR PaxDb; Q69ZK9; -.
DR PeptideAtlas; Q69ZK9; -.
DR PRIDE; Q69ZK9; -.
DR ProteomicsDB; 293856; -.
DR ABCD; Q69ZK9; 1 sequenced antibody.
DR Antibodypedia; 24107; 116 antibodies from 32 providers.
DR DNASU; 216856; -.
DR Ensembl; ENSMUST00000056484; ENSMUSP00000053097; ENSMUSG00000051790.
DR Ensembl; ENSMUST00000108634; ENSMUSP00000104274; ENSMUSG00000051790.
DR GeneID; 216856; -.
DR KEGG; mmu:216856; -.
DR UCSC; uc007jrw.1; mouse.
DR CTD; 57555; -.
DR MGI; MGI:2681835; Nlgn2.
DR VEuPathDB; HostDB:ENSMUSG00000051790; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000160598; -.
DR HOGENOM; CLU_006586_5_1_1; -.
DR InParanoid; Q69ZK9; -.
DR OMA; APPGIMK; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q69ZK9; -.
DR TreeFam; TF326187; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 216856; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Nlgn2; mouse.
DR EvolutionaryTrace; Q69ZK9; -.
DR PRO; PR:Q69ZK9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q69ZK9; protein.
DR Bgee; ENSMUSG00000051790; Expressed in subiculum and 218 other tissues.
DR ExpressionAtlas; Q69ZK9; baseline and differential.
DR Genevisible; Q69ZK9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:MGI.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097470; C:ribbon synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042043; F:neurexin family protein binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; IDA:BHF-UCL.
DR GO; GO:1904862; P:inhibitory synapse assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:1901142; P:insulin metabolic process; ISO:MGI.
DR GO; GO:0007630; P:jump response; ISS:BHF-UCL.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IGI:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0072578; P:neurotransmitter-gated ion channel clustering; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IMP:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; ISO:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IMP:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IDA:BHF-UCL.
DR GO; GO:1904034; P:positive regulation of t-SNARE clustering; ISO:MGI.
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:0034394; P:protein localization to cell surface; IDA:MGI.
DR GO; GO:0035418; P:protein localization to synapse; IDA:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:BHF-UCL.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IGI:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:BHF-UCL.
DR GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0050808; P:synapse organization; ISS:BHF-UCL.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IDA:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0072553; P:terminal button organization; ISS:BHF-UCL.
DR GO; GO:0001966; P:thigmotaxis; ISS:BHF-UCL.
DR DisProt; DP02755; -.
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; IPR030023; NLGN2.
DR PANTHER; PTHR43903:SF3; PTHR43903:SF3; 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; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000250"
FT CHAIN 15..836
FT /note="Neuroligin-2"
FT /id="PRO_0000041879"
FT TOPO_DOM 15..678
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 623..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..699
FT /note="Required for interaction with LHFPL4"
FT /evidence="ECO:0000269|PubMed:28279354"
FT REGION 711..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18250328"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..141
FT /evidence="ECO:0000269|PubMed:18250328"
FT DISULFID 317..328
FT /evidence="ECO:0000269|PubMed:18250328"
FT DISULFID 487..521
FT /evidence="ECO:0000269|PubMed:18250328"
FT CONFLICT 210
FT /note="V -> A (in Ref. 1; BAD32437)"
FT /evidence="ECO:0000305"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3BL8"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3BL8"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3BL8"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 322..329
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 403..416
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 444..459
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 461..473
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:3BL8"
FT TURN 500..503
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 525..544
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:3BL8"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:3BL8"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:3BL8"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:3BL8"
SQ SEQUENCE 836 AA; 90989 MW; 4C03297F4F1A1F14 CRC64;
MWLLALCLVG LAGAQRGGGG PGGGAPGGPG LGLGSLGEER FPVVNTAYGR VRGVRRELNN
EILGPVVQFL GVPYATPPLG ARRFQPPEAP ASWPGVRNAT TLPPACPQNL HGALPAIMLP
VWFTDNLEAA ATYVQNQSED CLYLNLYVPT EDGPLTKKRD EATLNPPDTD IRDSGKKPVM
LFLHGGSYME GTGNMFDGSV LAAYGNVIVV TLNYRLGVLG FLSTGDQAAK GNYGLLDQIQ
ALRWLSENIA HFGGDPERIT IFGSGAGASC VNLLILSHHS EGLFQKAIAQ SGTAISSWSV
NYQPLKYTRL LAAKVGCDRE DSTEAVECLR RKSSRELVDQ DVQPARYHIA FGPVVDGDVV
PDDPEILMQQ GEFLNYDMLI GVNQGEGLKF VEDSAESEDG VSASAFDFTV SNFVDNLYGY
PEGKDVLRET IKFMYTDWAD RDNGEMRRKT LLALFTDHQW VAPAVATAKL HADYQSPVYF
YTFYHHCQAE GRPEWADAAH GDELPYVFGV PMVGATDLFP CNFSKNDVML SAVVMTYWTN
FAKTGDPNQP VPQDTKFIHT KPNRFEEVVW SKFNSKEKQY LHIGLKPRVR DNYRANKVAF
WLELVPHLHN LHTELFTTTT RLPPYATRWP PRTPGPGTSG TRRPPPPATL PPESDIDLGP
RAYDRFPGDS RDYSTELSVT VAVGASLLFL NILAFAALYY KRDRRQELRC RRLSPPGGSG
SGVPGGGPLL PTAGRELPPE EELVSLQLKR GGGVGADPAE ALRPACPPDY TLALRRAPDD
VPLLAPGALT LLPSGLGPPP PPPPPSLHPF GPFPPPPPTA TSHNNTLPHP HSTTRV
