MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Neuroligin-3; AltName: Full=Gliotactin homolog; Flags: Precursor; |
 |
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| MyHits synonyms | NLGN3_HUMAN , Q9NZ94 , B2RBK1 , D2X2H6 , D3DVV0 , D3DVV1 , Q86V51 , Q8NCD0 , Q9NZ95 , Q9NZ96 , Q9NZ97 , Q9P248 , B3EE2FAB7E427C82 |
 Legends: 1, Phosphoserine. {ECO:0000250|UniProtKB:Q62889}; 2, Phosphotyrosine. {ECO:0000250|UniProtKB:Q8BYM5}; 3, N-linked (GlcNAc...) asparagine. {ECO:0000255}; 4, VARIANT S -> Y (in dbSNP:rs17854698). {ECO:0000269|PubMed:15489334}; 5, VARIANT R -> C (in AUTSX1 and ASPGX1). {ECO:0000269|PubMed:12669065}; 6, VARIANT L -> I (in dbSNP:rs17854697). {ECO:0000269|PubMed:15489334}; 7, VARIANT G -> W (in dbSNP:rs17857400). {ECO:0000269|PubMed:15489334}; 8, VARIANT G -> S (in dbSNP:rs17857401). {ECO:0000269|PubMed:15489334}; 9, CONFLICT L -> P (in Ref. 1; AAF71230). {ECO:0000305}; 10, CONFLICT F -> S (in Ref. 3; BAG37248). {ECO:0000305}; 11, SIGNAL {ECO:0000255}; 12, TRANSMEM Helical. {ECO:0000255}; 13, TOPO_DOM Cytoplasmic. {ECO:0000255}; 14, VAR_SEQ Missing (in isoform 3). {ECO:0000305}; 15, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:10767552, ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:20034102}; 16, ipat:CARBOXYLESTERASE_B_2 [T].
| |
ID NLGN3_HUMAN Reviewed; 848 AA.
AC Q9NZ94; B2RBK1; D2X2H6; D3DVV0; D3DVV1; Q86V51; Q8NCD0; Q9NZ95;
AC Q9NZ96; Q9NZ97; Q9P248;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 10-MAY-2017, entry version 152.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP TISSUE 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
RT evolution in zebrafish.";
RL Dev. Dyn. 239:688-702(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP TYR-92; 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
RT project: 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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
RT partners in the pancreatic beta-cells and the involvement of
RT neuroligin in insulin 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.,
RA Assenzio B., Cera M.R., Mascia L., Bussolino F., Arese M.;
RT "The synaptic proteins neurexins and neuroligins are widely expressed
RT in 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.,
RA Gillberg I.C., Soderstrom H., Giros B., Leboyer M., Gillberg C.,
RA Bourgeron T., Nyden A., Philippe A., Cohen D., Chabane N.,
RA Mouren-Simeoni M.C., Brice A., Sponheim E., Spurkland I.,
RA Skjeldal O.H., Coleman M., Pearl P.L., Cohen I.L., Tsiouris J.,
RA Zappella M., Menchetti G., Pompella A., Aschauer H., Van Maldergem L.;
RT "Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4
RT are associated with autism.";
RL Nat. Genet. 34:27-29(2003).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions
CC via its interactions with neurexin family members. Plays a role in
CC synapse function and synaptic signal transmission, and may mediate
CC its effects by clustering other synaptic proteins. May promote the
CC initial formation of synapses, but is not essential for this. May
CC also play a role in glia-glia or glia-neuron interactions in the
CC developing peripheral nervous system (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15620359}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its
CC C-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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC type I membrane protein {ECO:0000250}. Cell junction, synapse
CC {ECO:0000250}. Note=Detected at both glutamatergic and GABAergic
CC 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 Note=No experimental evidence available. Gene prediction based
CC on EST data.;
CC -!- TISSUE SPECIFICITY: Expressed in the blood vessel walls (at
CC protein level). Detected in throughout the brain and in spinal
CC cord. Detected in brain, and at lower levels in pancreas islet
CC beta cells. {ECO:0000269|PubMed:10767552,
CC ECO:0000269|PubMed:18755801, 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,
CC and the presence of developmental abnormalities by 3 years of age.
CC Most individuals with autism also manifest moderate mental
CC retardation. {ECO:0000269|PubMed:12669065}. Note=Disease
CC susceptibility is associated with variations affecting the gene
CC represented in this entry.
CC -!- DISEASE: Asperger syndrome, X-linked, 1 (ASPGX1) [MIM:300494]: A
CC syndrome with features similar to autism. Affected individuals
CC exhibit qualitative impairment in social interaction, as manifest
CC by impairment in the use of non-verbal behaviors such as eye-to-
CC eye gaze, facial expression, body postures, and gestures, failure
CC to develop appropriate peer relationships, and lack of social
CC sharing or reciprocity. Patients also exhibit restricted,
CC repetitive and stereotyped patterns of behavior, interests, and
CC activities, including abnormal preoccupation with certain
CC activities and inflexible adherence to routines or rituals.
CC Asperger syndrome is primarily distinguished from autism by the
CC higher cognitive abilities and a more normal and timely
CC development of language and communicative phrases.
CC {ECO:0000269|PubMed:12669065}. Note=Disease susceptibility is
CC associated with variations affecting the gene represented in this
CC 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 UniGene; Hs.438877; -.
DR DisProt; DP00553; -.
DR ProteinModelPortal; Q9NZ94; -.
DR SMR; Q9NZ94; -.
DR BioGrid; 119944; 76.
DR IntAct; Q9NZ94; 2.
DR MINT; MINT-199096; -.
DR STRING; 9606.ENSP00000351591; -.
DR ESTHER; human-NLGN3; Neuroligin.
DR MEROPS; S09.987; -.
DR iPTMnet; Q9NZ94; -.
DR PhosphoSitePlus; Q9NZ94; -.
DR BioMuta; NLGN3; -.
DR DMDM; 31076855; -.
DR PaxDb; Q9NZ94; -.
DR PeptideAtlas; Q9NZ94; -.
DR PRIDE; Q9NZ94; -.
DR DNASU; 54413; -.
DR Ensembl; ENST00000358741; ENSP00000351591; ENSG00000196338. [Q9NZ94-1]
DR Ensembl; ENST00000374051; ENSP00000363163; ENSG00000196338. [Q9NZ94-2]
DR Ensembl; ENST00000536169; ENSP00000445298; ENSG00000196338. [Q9NZ94-3]
DR GeneID; 54413; -.
DR KEGG; hsa:54413; -.
DR CTD; 54413; -.
DR DisGeNET; 54413; -.
DR GeneCards; NLGN3; -.
DR GeneReviews; NLGN3; -.
DR HGNC; HGNC:14289; NLGN3.
DR HPA; HPA003183; -.
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; Asperger syndrome.
DR Orphanet; 106; Autism.
DR PharmGKB; PA31649; -.
DR eggNOG; KOG1516; Eukaryota.
DR eggNOG; COG2272; LUCA.
DR GeneTree; ENSGT00760000118946; -.
DR HOVERGEN; HBG008839; -.
DR InParanoid; Q9NZ94; -.
DR KO; K07378; -.
DR OMA; KPNKKIC; -.
DR OrthoDB; EOG091G0CHW; -.
DR PhylomeDB; Q9NZ94; -.
DR TreeFam; TF326187; -.
DR Reactome; R-HSA-6794361; Interactions of neurexins and neuroligins at synapses.
DR ChiTaRS; NLGN3; human.
DR GeneWiki; NLGN3; -.
DR GenomeRNAi; 54413; -.
DR PRO; PR:Q9NZ94; -.
DR Proteomes; UP000005640; Chromosome X.
DR Bgee; ENSG00000196338; -.
DR CleanEx; HS_NLGN3; -.
DR ExpressionAtlas; Q9NZ94; baseline and differential.
DR Genevisible; Q9NZ94; HS.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
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:0004872; F:receptor activity; ISS:BHF-UCL.
DR GO; GO:0097110; F:scaffold protein binding; IPI: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:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
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:2000809; P:positive regulation of synaptic vesicle clustering; IEA:Ensembl.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-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:1900271; P:regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IEA:Ensembl.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; ISS:BHF-UCL.
DR GO; GO:2000331; P:regulation of terminal button organization; IEA:Ensembl.
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:0008542; P:visual learning; IEA:Ensembl.
DR GO; GO:0071625; P:vocalization behavior; 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; IPR030024; NLGN3.
DR PANTHER; PTHR11559:SF285; PTHR11559:SF285; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR01090; NEUROLIGIN.
DR SUPFAM; SSF53474; SSF53474; 2.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Asperger syndrome; Autism;
KW Autism spectrum disorder; Cell adhesion; Cell junction; Cell membrane;
KW Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 37 {ECO:0000255}.
FT CHAIN 38 848 Neuroligin-3.
FT /FTId=PRO_0000008645.
FT TOPO_DOM 38 709 Extracellular. {ECO:0000255}.
FT TRANSMEM 710 730 Helical. {ECO:0000255}.
FT TOPO_DOM 731 848 Cytoplasmic. {ECO:0000255}.
FT MOD_RES 745 745 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q62889}.
FT MOD_RES 792 792 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:Q8BYM5}.
FT CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT DISULFID 106 141 {ECO:0000250}.
FT DISULFID 340 351 {ECO:0000250}.
FT DISULFID 510 544 {ECO:0000250}.
FT VAR_SEQ 153 192 Missing (in isoform 3). {ECO:0000305}.
FT /FTId=VSP_053827.
FT VAR_SEQ 153 172 Missing (in isoform 2).
FT {ECO:0000303|PubMed:10767552,
FT ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:20034102}.
FT /FTId=VSP_007534.
FT VARIANT 92 92 S -> Y (in dbSNP:rs17854698).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_068887.
FT VARIANT 451 451 R -> C (in AUTSX1 and ASPGX1).
FT {ECO:0000269|PubMed:12669065}.
FT /FTId=VAR_015668.
FT VARIANT 718 718 L -> I (in dbSNP:rs17854697).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_068888.
FT VARIANT 751 751 G -> W (in dbSNP:rs17857400).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_068889.
FT VARIANT 778 778 G -> S (in dbSNP:rs17857401).
FT {ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_068890.
FT CONFLICT 224 224 L -> P (in Ref. 1; AAF71230).
FT {ECO:0000305}.
FT CONFLICT 274 274 F -> S (in Ref. 3; BAG37248).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 41 624 ipfam:COesterase [T]
FT MYHIT 139 149 ipat:CARBOXYLESTERASE_B_2 [T]
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
//
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