NLGN3_HUMAN
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 03-AUG-2022, entry version 188.
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, AND VARIANT ASPGX1 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: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-
CC terminus) with DLG4/PSD-95 (via PDZ domain 3) (By similarity).
CC Homodimer, and heterodimer with NLGN1 and NLGN2 (By similarity).
CC {ECO:0000250}.
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 -!- DISEASE: Asperger syndrome, X-linked, 1 (ASPGX1) [MIM:300494]: A
CC syndrome with features similar to autism. Affected individuals exhibit
CC qualitative impairment in social interaction, as manifest by impairment
CC in the use of non-verbal behaviors such as eye-to-eye gaze, facial
CC expression, body postures, and gestures, failure to develop appropriate
CC peer relationships, and lack of social sharing or reciprocity. Patients
CC also exhibit restricted, repetitive and stereotyped patterns of
CC behavior, interests, and activities, including abnormal preoccupation
CC with certain activities and inflexible adherence to routines or
CC rituals. Asperger syndrome is primarily distinguished from autism by
CC the higher cognitive abilities and a more normal and timely development
CC of language and communicative phrases. {ECO:0000269|PubMed:12669065}.
CC Note=Disease susceptibility is associated with variants affecting the
CC 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};
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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 AlphaFoldDB; Q9NZ94; -.
DR BMRB; Q9NZ94; -.
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 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; Q9NZ94; -.
DR PeptideAtlas; Q9NZ94; -.
DR PRIDE; Q9NZ94; -.
DR ProteomicsDB; 12770; -.
DR ProteomicsDB; 83341; -. [Q9NZ94-1]
DR ProteomicsDB; 83342; -. [Q9NZ94-2]
DR ABCD; Q9NZ94; 1 sequenced antibody.
DR Antibodypedia; 561; 312 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 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 MIM; 300494; 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; MPVWFTS; -.
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; 13 hits in 699 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 tissues.
DR ExpressionAtlas; Q9NZ94; baseline and differential.
DR Genevisible; Q9NZ94; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0089717; C:spanning component of membrane; TAS:ARUK-UCL.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000460; Nlgn.
DR InterPro; IPR030024; NLGN3.
DR PANTHER; PTHR43903:SF4; PTHR43903:SF4; 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 Alternative splicing; Asperger syndrome; Autism; Autism spectrum disorder;
KW Cell adhesion; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW 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 and ASPGX1)"
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