ID NLGN3_HUMAN Reviewed; 848 AA. AC Q9NZ94; B2RBK1; D2X2H6; D3DVV0; D3DVV1; Q86V51; Q8NCD0; Q9NZ95; Q9NZ96; AC Q9NZ97; Q9P248; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-2003, sequence version 2. DT 27-MAR-2024, entry version 197. DE RecName: Full=Neuroligin-3; DE AltName: Full=Gliotactin homolog; DE Flags: Precursor; GN Name=NLGN3; Synonyms=KIAA1480, NL3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE RP SPECIFICITY. RX PubMed=10767552; DOI=10.1016/s0378-1119(00)00049-4; RA Philibert R.A., Winfield S.L., Sandhu H.K., Martin B.M., Ginns E.I.; RT "The structure and expression of the human neuroligin-3 gene."; RL Gene 246:303-310(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=20034102; DOI=10.1002/dvdy.22196; RA Rissone A., Sangiorgio L., Monopoli M., Beltrame M., Zucchi I., RA Bussolino F., Arese M., Cotelli F.; RT "Characterization of the neuroligin gene family expression and evolution in RT zebrafish."; RL Dev. Dyn. 239:688-702(2010). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 410-848 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS TYR-92; RP ILE-718; TRP-751 AND SER-778. RC TISSUE=Brain; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-848. RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [8] RP INTERACTION WITH DLG4. RX PubMed=9278515; DOI=10.1126/science.277.5331.1511; RA Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K., RA Takai Y., Rosahl T.W., Suedhof T.C.; RT "Binding of neuroligins to PSD-95."; RL Science 277:1511-1515(1997). RN [9] RP FUNCTION. 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 [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 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 VARIANT AUTSX1 CYS-451. RX PubMed=12669065; DOI=10.1038/ng1136; RA Jamain S., Quach H., Betancur C., Rastam M., Colineaux C., Gillberg I.C., RA Soderstrom H., Giros B., Leboyer M., Gillberg C., Bourgeron T., Nyden A., RA Philippe A., Cohen D., Chabane N., Mouren-Simeoni M.C., Brice A., RA Sponheim E., Spurkland I., Skjeldal O.H., Coleman M., Pearl P.L., RA Cohen I.L., Tsiouris J., Zappella M., Menchetti G., Pompella A., RA Aschauer H., Van Maldergem L.; RT "Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are RT associated with autism."; RL Nat. Genet. 34:27-29(2003). 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 may mediate its effects CC by clustering other synaptic proteins. May promote the initial CC formation of synapses, but is not essential for this. May also play a CC role in glia-glia or glia-neuron interactions in the developing CC peripheral nervous system (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:15620359}. CC -!- SUBUNIT: Homodimer, and heterodimer with NLGN1 and NLGN2 (By CC similarity). Interacts with neurexins NRXN1, NRXN2 and NRXN3 (By CC similarity). Interaction with neurexins is mediated by heparan sulfate CC glycan modification on neurexin (By similarity). Interacts (via its C- CC terminus) with DLG4/PSD-95 (via PDZ domain 3) (By similarity). CC {ECO:0000250|UniProtKB:Q62889, ECO:0000250|UniProtKB:Q8BYM5}. CC -!- INTERACTION: CC Q9NZ94-2; P49753: ACOT2; NbExp=2; IntAct=EBI-16423037, EBI-1052865; CC Q9NZ94-2; P05108: CYP11A1; NbExp=3; IntAct=EBI-16423037, EBI-7183136; CC Q9NZ94-2; P68104: EEF1A1; NbExp=4; IntAct=EBI-16423037, EBI-352162; CC Q9NZ94-2; Q8IWB1: ITPRIP; NbExp=5; IntAct=EBI-16423037, EBI-2556412; CC Q9NZ94-2; P00403: MT-CO2; NbExp=4; IntAct=EBI-16423037, EBI-2105756; CC Q9NZ94-2; Q15274: QPRT; NbExp=4; IntAct=EBI-16423037, EBI-739851; CC Q9NZ94-2; Q86W33: TPRA1; NbExp=3; IntAct=EBI-16423037, EBI-16424742; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Note=Detected at CC both glutamatergic and GABAergic synapses. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=HNL3s; CC IsoId=Q9NZ94-1; Sequence=Displayed; CC Name=2; Synonyms=HNL3; CC IsoId=Q9NZ94-2; Sequence=VSP_007534; CC Name=3; CC IsoId=Q9NZ94-3; Sequence=VSP_053827; CC -!- TISSUE SPECIFICITY: Expressed in the blood vessel walls (at protein CC level). Detected in throughout the brain and in spinal cord. Detected CC in brain, and at lower levels in pancreas islet beta cells. CC {ECO:0000269|PubMed:10767552, ECO:0000269|PubMed:18755801, CC ECO:0000269|PubMed:19926856}. CC -!- DISEASE: Autism, X-linked 1 (AUTSX1) [MIM:300425]: A complex CC multifactorial, pervasive developmental disorder characterized by CC impairments in reciprocal social interaction and communication, CC restricted and stereotyped patterns of interests and activities, and CC the presence of developmental abnormalities by 3 years of age. Most CC individuals with autism also manifest moderate intellectual disability. CC {ECO:0000269|PubMed:12669065}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF71231.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA96004.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC11226.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF217411; AAF71230.1; -; mRNA. DR EMBL; AF217412; AAF71231.1; ALT_SEQ; mRNA. DR EMBL; AF217413; AAF71232.1; -; Genomic_DNA. DR EMBL; AF217413; AAF71233.1; -; Genomic_DNA. DR EMBL; GQ489207; ADB12634.1; -; mRNA. DR EMBL; AK074814; BAC11226.1; ALT_INIT; mRNA. DR EMBL; AK314699; BAG37248.1; -; mRNA. DR EMBL; AL590764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471132; EAX05307.1; -; Genomic_DNA. DR EMBL; CH471132; EAX05308.1; -; Genomic_DNA. DR EMBL; CH471132; EAX05309.1; -; Genomic_DNA. DR EMBL; CH471132; EAX05310.1; -; Genomic_DNA. DR EMBL; CH471132; EAX05312.1; -; Genomic_DNA. DR EMBL; CH471132; EAX05313.1; -; Genomic_DNA. DR EMBL; BC051715; AAH51715.1; -; mRNA. DR EMBL; AB040913; BAA96004.1; ALT_INIT; mRNA. DR CCDS; CCDS14407.1; -. [Q9NZ94-2] DR CCDS; CCDS55441.1; -. [Q9NZ94-1] DR CCDS; CCDS55442.1; -. [Q9NZ94-3] DR RefSeq; NP_001160132.1; NM_001166660.1. [Q9NZ94-3] DR RefSeq; NP_001308205.1; NM_001321276.1. DR RefSeq; NP_061850.2; NM_018977.3. [Q9NZ94-2] DR RefSeq; NP_851820.1; NM_181303.1. [Q9NZ94-1] DR PDB; 8GS3; EM; 3.90 A; A/B=1-848. DR PDBsum; 8GS3; -. DR AlphaFoldDB; Q9NZ94; -. DR BMRB; Q9NZ94; -. DR EMDB; EMD-34219; -. DR SMR; Q9NZ94; -. DR BioGRID; 119944; 93. DR IntAct; Q9NZ94; 81. DR MINT; Q9NZ94; -. DR STRING; 9606.ENSP00000351591; -. DR ESTHER; human-NLGN3; Neuroligin. DR MEROPS; S09.987; -. DR TCDB; 8.A.117.1.6; the neuroligin (nlg) family. DR GlyCosmos; Q9NZ94; 2 sites, No reported glycans. DR GlyGen; Q9NZ94; 2 sites. DR iPTMnet; Q9NZ94; -. DR PhosphoSitePlus; Q9NZ94; -. DR BioMuta; NLGN3; -. DR DMDM; 31076855; -. DR EPD; Q9NZ94; -. DR jPOST; Q9NZ94; -. DR MassIVE; Q9NZ94; -. DR PaxDb; 9606-ENSP00000351591; -. DR PeptideAtlas; Q9NZ94; -. DR ProteomicsDB; 12770; -. DR ProteomicsDB; 83341; -. [Q9NZ94-1] DR ProteomicsDB; 83342; -. [Q9NZ94-2] DR ABCD; Q9NZ94; 1 sequenced antibody. DR Antibodypedia; 561; 345 antibodies from 37 providers. DR DNASU; 54413; -. DR Ensembl; ENST00000358741.4; ENSP00000351591.4; ENSG00000196338.15. [Q9NZ94-1] DR Ensembl; ENST00000374051.7; ENSP00000363163.3; ENSG00000196338.15. [Q9NZ94-2] DR Ensembl; ENST00000536169.6; ENSP00000445298.1; ENSG00000196338.15. [Q9NZ94-3] DR GeneID; 54413; -. DR KEGG; hsa:54413; -. DR MANE-Select; ENST00000358741.4; ENSP00000351591.4; NM_181303.2; NP_851820.1. DR AGR; HGNC:14289; -. DR CTD; 54413; -. DR DisGeNET; 54413; -. DR GeneCards; NLGN3; -. DR HGNC; HGNC:14289; NLGN3. DR HPA; ENSG00000196338; Tissue enhanced (brain, seminal vesicle). DR MalaCards; NLGN3; -. DR MIM; 300336; gene. DR MIM; 300425; phenotype. DR neXtProt; NX_Q9NZ94; -. DR OpenTargets; ENSG00000196338; -. DR Orphanet; 1162; NON RARE IN EUROPE: Asperger syndrome. DR Orphanet; 106; NON RARE IN EUROPE: Autism. DR PharmGKB; PA31649; -. DR VEuPathDB; HostDB:ENSG00000196338; -. DR eggNOG; KOG1516; Eukaryota. DR GeneTree; ENSGT00940000159580; -. DR HOGENOM; CLU_006586_5_1_1; -. DR InParanoid; Q9NZ94; -. DR OMA; QCGHEGA; -. DR OrthoDB; 4386at2759; -. DR PhylomeDB; Q9NZ94; -. DR TreeFam; TF326187; -. DR PathwayCommons; Q9NZ94; -. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR SignaLink; Q9NZ94; -. DR SIGNOR; Q9NZ94; -. DR BioGRID-ORCS; 54413; 14 hits in 773 CRISPR screens. DR ChiTaRS; NLGN3; human. DR GeneWiki; NLGN3; -. DR GenomeRNAi; 54413; -. DR Pharos; Q9NZ94; Tbio. DR PRO; PR:Q9NZ94; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9NZ94; Protein. DR Bgee; ENSG00000196338; Expressed in cortical plate and 138 other cell types or tissues. DR ExpressionAtlas; Q9NZ94; baseline and differential. DR GO; GO:0098985; C:asymmetric, glutamatergic, excitatory synapse; TAS:ARUK-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0030139; C:endocytic vesicle; ISS:BHF-UCL. DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; TAS:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0098983; C:symmetric, GABA-ergic, inhibitory synapse; TAS:ARUK-UCL. DR GO; GO:0045202; C:synapse; ISS:UniProtKB. DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL. DR GO; GO:0042043; F:neurexin family protein binding; ISS:BHF-UCL. DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL. DR GO; GO:0038023; F:signaling receptor activity; ISS:BHF-UCL. DR GO; GO:0030534; P:adult behavior; IMP:BHF-UCL. DR GO; GO:0048675; P:axon extension; ISS:BHF-UCL. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISS:BHF-UCL. DR GO; GO:0007612; P:learning; IMP:BHF-UCL. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:BHF-UCL. DR GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL. DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; ISS:BHF-UCL. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL. DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL. DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL. DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL. DR GO; GO:0099054; P:presynapse assembly; TAS:ARUK-UCL. DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL. DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:BHF-UCL. DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISS:BHF-UCL. DR GO; GO:0060024; P:rhythmic synaptic transmission; ISS:BHF-UCL. DR GO; GO:0035176; P:social behavior; IMP:UniProtKB. DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL. DR GO; GO:0050808; P:synapse organization; IMP:UniProtKB. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central. DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL. DR DisProt; DP00553; -. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR InterPro; IPR000460; Nlgn. DR PANTHER; PTHR43903; NEUROLIGIN; 1. DR PANTHER; PTHR43903:SF4; NEUROLIGIN-3; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR01090; NEUROLIGIN. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. DR Genevisible; Q9NZ94; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Asperger syndrome; Autism; KW Autism spectrum disorder; Cell adhesion; Cell membrane; Disease variant; KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; KW Signal; Synapse; Transmembrane; Transmembrane helix. FT SIGNAL 1..37 FT /evidence="ECO:0000255" FT CHAIN 38..848 FT /note="Neuroligin-3" FT /id="PRO_0000008645" FT TOPO_DOM 38..709 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 710..730 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 731..848 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 170..195 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 645..694 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 645..689 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 745 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62889" FT MOD_RES 792 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q8BYM5" FT CARBOHYD 98 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 545 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 106..141 FT /evidence="ECO:0000250" FT DISULFID 340..351 FT /evidence="ECO:0000250" FT DISULFID 510..544 FT /evidence="ECO:0000250" FT VAR_SEQ 153..192 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_053827" FT VAR_SEQ 153..172 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10767552, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:20034102" FT /id="VSP_007534" FT VARIANT 92 FT /note="S -> Y (in dbSNP:rs17854698)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_068887" FT VARIANT 451 FT /note="R -> C (in AUTSX1)" FT /evidence="ECO:0000269|PubMed:12669065" FT /id="VAR_015668" FT VARIANT 718 FT /note="L -> I (in dbSNP:rs17854697)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_068888" FT VARIANT 751 FT /note="G -> W (in dbSNP:rs17857400)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_068889" FT VARIANT 778 FT /note="G -> S (in dbSNP:rs17857401)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_068890" FT CONFLICT 224 FT /note="L -> P (in Ref. 1; AAF71230)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="F -> S (in Ref. 3; BAG37248)" FT /evidence="ECO:0000305" SQ SEQUENCE 848 AA; 93895 MW; B3EE2FAB7E427C82 CRC64; MWLRLGPPSL SLSPKPTVGR SLCLTLWFLS LALRASTQAP APTVNTHFGK LRGARVPLPS EILGPVDQYL GVPYAAPPIG EKRFLPPEPP PSWSGIRNAT HFPPVCPQNI HTAVPEVMLP VWFTANLDIV ATYIQEPNED CLYLNVYVPT EDVKRISKEC ARKPNKKICR KGGSGAKKQG EDLADNDGDE DEDIRDSGAK PVMVYIHGGS YMEGTGNMID GSILASYGNV IVITLNYRVG VLGFLSTGDQ AAKGNYGLLD QIQALRWVSE NIAFFGGDPR RITVFGSGIG ASCVSLLTLS HHSEGLFQRA IIQSGSALSS WAVNYQPVKY TSLLADKVGC NVLDTVDMVD CLRQKSAKEL VEQDIQPARY HVAFGPVIDG DVIPDDPEIL MEQGEFLNYD IMLGVNQGEG LKFVEGVVDP EDGVSGTDFD YSVSNFVDNL YGYPEGKDTL RETIKFMYTD WADRDNPETR RKTLVALFTD HQWVEPSVVT ADLHARYGSP TYFYAFYHHC QSLMKPAWSD AAHGDEVPYV FGVPMVGPTD LFPCNFSKND VMLSAVVMTY WTNFAKTGDP NKPVPQDTKF IHTKANRFEE VAWSKYNPRD QLYLHIGLKP RVRDHYRATK VAFWKHLVPH LYNLHDMFHY TSTTTKVPPP DTTHSSHITR RPNGKTWSTK RPAISPAYSN ENAQGSWNGD QDAGPLLVEN PRDYSTELSV TIAVGASLLF LNVLAFAALY YRKDKRRQEP LRQPSPQRGA GAPELGAAPE EELAALQLGP THHECEAGPP HDTLRLTALP DYTLTLRRSP DDIPLMTPNT ITMIPNSLVG LQTLHPYNTF AAGFNSTGLP HSHSTTRV //