NLGN1_HUMAN
ID NLGN1_HUMAN Reviewed; 863 AA.
AC Q8N2Q7; D2X2H5; Q9UPT2;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Neuroligin-1;
DE Flags: Precursor;
GN Name=NLGN1; Synonyms=KIAA1070;
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 [MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Duodenum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 330-840 (ISOFORMS 1/2).
RC TISSUE=Embryo;
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 [6]
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 [7]
RP INTERACTION WITH GOPC.
RX PubMed=16882988; DOI=10.1110/ps.062087506;
RA Li X., Zhang J., Cao Z., Wu J., Shi Y.;
RT "Solution structure of GOPC PDZ domain and its interaction with the C-
RT terminal motif of neuroligin.";
RL Protein Sci. 15:2149-2158(2006).
RN [8]
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 [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS AUTS20 LEU-89;
RP ILE-90; PRO-309; GLU-337 AND TYR-835, VARIANT HIS-756, CHARACTERIZATION OF
RP VARIANTS AUTS20 LEU-89; ILE-90; PRO-309; GLU-337 AND TYR-835, AND
RP CHARACTERIZATION OF VARIANT HIS-756.
RX PubMed=28841651; DOI=10.1371/journal.pgen.1006940;
RA Nakanishi M., Nomura J., Ji X., Tamada K., Arai T., Takahashi E., Bucan M.,
RA Takumi T.;
RT "Functional significance of rare neuroligin 1 variants found in autism.";
RL PLoS Genet. 13:e1006940-e1006940(2017).
RN [11]
RP ERRATUM OF PUBMED:28841651.
RX PubMed=28972980; DOI=10.1371/journal.pgen.1007035;
RA Nakanishi M., Nomura J., Ji X., Tamada K., Arai T., Takahashi E., Bucan M.,
RA Takumi T.;
RT "Correction: Functional significance of rare neuroligin 1 variants found in
RT autism.";
RL PLoS Genet. 13:e1007035-e1007035(2017).
RN [12]
RP VARIANT 25-LEU--VAL-863 DEL.
RX PubMed=30460678; DOI=10.1111/cge.13466;
RA Tejada M.I., Elcoroaristizabal X., Ibarluzea N., Botella M.P.,
RA de la Hoz A.B., Ocio I.;
RT "A novel nonsense homozygous variant in the NLGN1 gene found in a pair of
RT monozygotic twin brothers with intellectual disability and autism.";
RL Clin. Genet. 95:339-340(2019).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions via
CC its interactions with neurexin family members. Plays a role in synapse
CC function and synaptic signal transmission, and probably mediates its
CC effects by recruiting and clustering other synaptic proteins. May
CC promote the initial formation of synapses, but is not essential for
CC this. In vitro, triggers the de novo formation of presynaptic
CC structures. May be involved in specification of excitatory synapses.
CC Required to maintain wakefulness quality and normal synchrony of
CC cerebral cortex activity during wakefulness and sleep (By similarity).
CC The protein is involved in nervous system development.
CC {ECO:0000250|UniProtKB:Q99K10, ECO:0000269|PubMed:28841651}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts with NLGN3.
CC Interacts with AIP1 and PDZRN3 (By similarity). Interacts (via its C-
CC terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with GOPC.
CC {ECO:0000250, ECO:0000269|PubMed:16882988, ECO:0000269|PubMed:9278515}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28841651};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q62765}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q62765}. Synaptic cleft
CC {ECO:0000250|UniProtKB:Q62765}. Synaptic cell membrane
CC {ECO:0000250|UniProtKB:Q62765}. Note=Enriched in synaptic plasma
CC membranes and clustered in synaptic clefts and postsynaptic densities.
CC Colocalized with DLG4/PSD-95 and GRIN1/NMDAR1.
CC {ECO:0000250|UniProtKB:Q62765}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N2Q7-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N2Q7-2; Sequence=VSP_060231;
CC -!- TISSUE SPECIFICITY: Expressed in the blood vessel walls (at protein
CC level). Highly expressed in brain through prenatal stages, and at lower
CC levels in pancreas islet beta cells. {ECO:0000269|PubMed:18755801,
CC ECO:0000269|PubMed:19926856, ECO:0000269|PubMed:28841651}.
CC -!- DISEASE: Autism 20 (AUTS20) [MIM:618830]: A complex multifactorial,
CC pervasive developmental disorder characterized by impairments in
CC reciprocal social interaction and communication, restricted and
CC stereotyped patterns of interests and activities, and the presence of
CC developmental abnormalities by 3 years of age. Most individuals with
CC autism also manifest moderate intellectual disability. The transmission
CC pattern of AUTS20 is consistent with autosomal dominant inheritance.
CC {ECO:0000269|PubMed:28841651}. 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=BAA83022.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GQ489206; ADB12633.1; -; mRNA.
DR EMBL; AB028993; BAA83022.2; ALT_INIT; mRNA.
DR EMBL; AC008082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032555; AAH32555.1; -; mRNA.
DR EMBL; AK074522; BAC11039.1; ALT_INIT; mRNA.
DR CCDS; CCDS3222.1; -. [Q8N2Q7-2]
DR RefSeq; NP_055747.1; NM_014932.3. [Q8N2Q7-2]
DR RefSeq; XP_005247291.1; XM_005247234.2.
DR RefSeq; XP_005247292.1; XM_005247235.3.
DR RefSeq; XP_016861387.1; XM_017005898.1.
DR RefSeq; XP_016861388.1; XM_017005899.1.
DR RefSeq; XP_016861389.1; XM_017005900.1. [Q8N2Q7-2]
DR RefSeq; XP_016861390.1; XM_017005901.1.
DR PDB; 5OJ6; X-ray; 3.30 A; A=51-656.
DR PDB; 5OJK; X-ray; 2.55 A; A/B=51-654.
DR PDBsum; 5OJ6; -.
DR PDBsum; 5OJK; -.
DR AlphaFoldDB; Q8N2Q7; -.
DR SMR; Q8N2Q7; -.
DR BioGRID; 116538; 19.
DR ComplexPortal; CPX-4101; NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex.
DR ComplexPortal; CPX-909; NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex.
DR CORUM; Q8N2Q7; -.
DR IntAct; Q8N2Q7; 9.
DR MINT; Q8N2Q7; -.
DR STRING; 9606.ENSP00000392500; -.
DR ESTHER; human-NLGN1; Neuroligin.
DR MEROPS; S09.994; -.
DR TCDB; 8.A.117.1.2; the neuroligin (nlg) family.
DR GlyGen; Q8N2Q7; 6 sites.
DR iPTMnet; Q8N2Q7; -.
DR PhosphoSitePlus; Q8N2Q7; -.
DR BioMuta; NLGN1; -.
DR DMDM; 31076822; -.
DR EPD; Q8N2Q7; -.
DR jPOST; Q8N2Q7; -.
DR MassIVE; Q8N2Q7; -.
DR PaxDb; Q8N2Q7; -.
DR PeptideAtlas; Q8N2Q7; -.
DR PRIDE; Q8N2Q7; -.
DR ProteomicsDB; 71726; -. [Q8N2Q7-2]
DR Antibodypedia; 1513; 297 antibodies from 35 providers.
DR DNASU; 22871; -.
DR Ensembl; ENST00000361589.8; ENSP00000354541.4; ENSG00000169760.17. [Q8N2Q7-2]
DR Ensembl; ENST00000457714.5; ENSP00000392500.1; ENSG00000169760.17. [Q8N2Q7-2]
DR GeneID; 22871; -.
DR KEGG; hsa:22871; -.
DR UCSC; uc003fio.3; human. [Q8N2Q7-3]
DR CTD; 22871; -.
DR DisGeNET; 22871; -.
DR GeneCards; NLGN1; -.
DR HGNC; HGNC:14291; NLGN1.
DR HPA; ENSG00000169760; Tissue enhanced (brain, retina).
DR MalaCards; NLGN1; -.
DR MIM; 600568; gene.
DR MIM; 618830; phenotype.
DR neXtProt; NX_Q8N2Q7; -.
DR OpenTargets; ENSG00000169760; -.
DR PharmGKB; PA31647; -.
DR VEuPathDB; HostDB:ENSG00000169760; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000155789; -.
DR InParanoid; Q8N2Q7; -.
DR OMA; HDMVLRT; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q8N2Q7; -.
DR TreeFam; TF326187; -.
DR PathwayCommons; Q8N2Q7; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q8N2Q7; -.
DR SIGNOR; Q8N2Q7; -.
DR BioGRID-ORCS; 22871; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; NLGN1; human.
DR GeneWiki; NLGN1; -.
DR GenomeRNAi; 22871; -.
DR Pharos; Q8N2Q7; Tbio.
DR PRO; PR:Q8N2Q7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8N2Q7; protein.
DR Bgee; ENSG00000169760; Expressed in cortical plate and 148 other tissues.
DR ExpressionAtlas; Q8N2Q7; baseline and differential.
DR Genevisible; Q8N2Q7; 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; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; NAS:ARUK-UCL.
DR GO; GO:0032433; C:filopodium tip; ISS:BHF-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IC:ComplexPortal.
DR GO; GO:0098978; C:glutamatergic synapse; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
DR GO; GO:0060077; C:inhibitory synapse; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; TAS:BHF-UCL.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISS:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IC:ComplexPortal.
DR GO; GO:0098984; C:neuron to neuron synapse; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0098794; C:postsynapse; NAS:ARUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; TAS:BHF-UCL.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0098635; C:protein complex involved in cell-cell adhesion; IC:ComplexPortal.
DR GO; GO:0043235; C:receptor complex; ISS:BHF-UCL.
DR GO; GO:0089717; C:spanning component of membrane; TAS:ARUK-UCL.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0043083; C:synaptic cleft; IEA:UniProtKB-SubCell.
DR GO; GO:0001540; F:amyloid-beta binding; NAS:ARUK-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0042043; F:neurexin family protein binding; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IDA:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; ISS:BHF-UCL.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; ISS:BHF-UCL.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0090125; P:cell-cell adhesion involved in synapse maturation; IC:ComplexPortal.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:ARUK-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0048789; P:cytoskeletal matrix organization at active zone; ISS:BHF-UCL.
DR GO; GO:0045184; P:establishment of protein localization; ISS:BHF-UCL.
DR GO; GO:1904861; P:excitatory synapse assembly; ISS:ARUK-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR GO; GO:0099558; P:maintenance of synapse structure; IC:ComplexPortal.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:ARUK-UCL.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IGI:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0097115; P:neurexin clustering involved in presynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0140058; P:neuron projection arborization; ISS:ARUK-UCL.
DR GO; GO:0031175; P:neuron projection development; IDA:CACAO.
DR GO; GO:0048812; P:neuron projection morphogenesis; IC:ComplexPortal.
DR GO; GO:0023041; P:neuronal signal transduction; TAS:BHF-UCL.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; ISS:BHF-UCL.
DR GO; GO:0010841; P:positive regulation of circadian sleep/wake cycle, wakefulness; ISS:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IGI:BHF-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:BHF-UCL.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISS:BHF-UCL.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IC:ComplexPortal.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IC:ComplexPortal.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISS:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISS:BHF-UCL.
DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; ISS:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; 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:0035418; P:protein localization to synapse; ISS:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:0097120; P:receptor localization to synapse; ISS:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IGI:BHF-UCL.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR GO; GO:0060074; P:synapse maturation; IC:ComplexPortal.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISS:BHF-UCL.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0016080; P:synaptic vesicle targeting; ISS:UniProtKB.
DR GO; GO:0072553; P:terminal button organization; ISS:BHF-UCL.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000460; Nlgn.
DR InterPro; IPR030022; NLGN1.
DR PANTHER; PTHR43903:SF2; PTHR43903:SF2; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR01090; NEUROLIGIN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autism; Autism spectrum disorder;
KW Biological rhythms; Cell adhesion; Cell membrane; Disease variant;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Secreted;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..863
FT /note="Neuroligin-1"
FT /id="PRO_0000008640"
FT TOPO_DOM 46..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 183..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 703
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 706
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 117..153
FT /evidence="ECO:0000250"
FT DISULFID 362..373
FT /evidence="ECO:0000250"
FT DISULFID 532..566
FT /evidence="ECO:0000250"
FT VAR_SEQ 165..204
FT /note="Missing (in isoform 2)"
FT /id="VSP_060231"
FT VARIANT 25..863
FT /note="Missing (in AUTS20; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30460678"
FT /id="VAR_084195"
FT VARIANT 89
FT /note="P -> L (in AUTS20; risk factor for disease
FT development; decreased function in dendritic spine
FT formation; decreased protein abundance; does not localize
FT to the plasma membrane but is retained in the endoplasmic
FT reticulum)"
FT /evidence="ECO:0000269|PubMed:28841651"
FT /id="VAR_084196"
FT VARIANT 90
FT /note="T -> I (in AUTS20; unknown pathological
FT significance; does not affect dendritic spine formation; no
FT effect on protein abundance; no effect on subcellular
FT localization)"
FT /evidence="ECO:0000269|PubMed:28841651"
FT /id="VAR_084197"
FT VARIANT 309
FT /note="L -> P (in AUTS20; risk factor for disease
FT development; decreased function in dendritic spine
FT formation; decreased protein abundance; does not localize
FT to the plasma membrane but is retained in the endoplasmic
FT reticulum)"
FT /evidence="ECO:0000269|PubMed:28841651"
FT /id="VAR_084198"
FT VARIANT 337
FT /note="G -> E (in AUTS20; risk factor for disease
FT development; decreased function in dendritic spine
FT formation; decreased protein abundance; does not localize
FT to the plasma membrane but is retained in the endoplasmic
FT reticulum)"
FT /evidence="ECO:0000269|PubMed:28841651"
FT /id="VAR_084199"
FT VARIANT 756
FT /note="R -> H (likely benign variant; does not affect
FT dendritic spine formation; does not affect localization to
FT plasma membrane)"
FT /evidence="ECO:0000269|PubMed:28841651"
FT /id="VAR_084200"
FT VARIANT 835
FT /note="H -> Y (in AUTS20; risk factor for disease
FT development; decreased function in dendritic spine
FT formation; decreased protein abundance; does not affect
FT subcellular location)"
FT /evidence="ECO:0000269|PubMed:28841651"
FT /id="VAR_084201"
FT CONFLICT 734
FT /note="F -> L (in Ref. 5; BAC11039)"
FT /evidence="ECO:0000305"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5OJ6"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5OJ6"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 269..284
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 290..300
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 327..336
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:5OJK"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:5OJK"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 448..462
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:5OJ6"
FT HELIX 469..479
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 489..504
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 506..518
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:5OJK"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 570..589
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:5OJ6"
FT TURN 609..612
FT /evidence="ECO:0007829|PDB:5OJ6"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 624..631
FT /evidence="ECO:0007829|PDB:5OJK"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 640..647
FT /evidence="ECO:0007829|PDB:5OJK"
FT HELIX 649..652
FT /evidence="ECO:0007829|PDB:5OJK"
FT TURN 653..655
FT /evidence="ECO:0007829|PDB:5OJ6"
SQ SEQUENCE 863 AA; 96368 MW; FDF64A8325A075E2 CRC64;
MALPRCTWPN YVWRAVMACL VHRGLGAPLT LCMLGCLLQA GHVLSQKLDD VDPLVATNFG
KIRGIKKELN NEILGPVIQF LGVPYAAPPT GERRFQPPEP PSPWSDIRNA TQFAPVCPQN
IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDVKRISK ECARKPGKKI
CRKGGPLTKK QTDDLGDNDG AEDEDIRDSG GPKPVMVYIH GGSYMEGTGN LYDGSVLASY
GNVIVITVNY RLGVLGFLST GDQAAKGNYG LLDLIQALRW TSENIGFFGG DPLRITVFGS
GAGGSCVNLL TLSHYSEGNR WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARMLATKV
GCNVSDTVEL VECLQKKPYK ELVDQDIQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN
YDIMLGVNQG EGLKFVENIV DSDDGISASD FDFAVSNFVD NLYGYPEGKD VLRETIKFMY
TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG SPTYFYAFYH HCQTDQVPAW
ADAAHGDEVP YVLGIPMIGP TELFPCNFSK NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT
KFIHTKPNRF EEVAWTRYSQ KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS
QYTSTTTKVP STDITFRPTR KNSVPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI
AVGASLLFLN ILAFAALYYK KDKRRHDVHR RCSPQRTTTN DLTHAQEEEI MSLQMKHTDL
DHECESIHPH EVVLRTACPP DYTLAMRRSP DDVPLMTPNT ITMIPNTIPG IQPLHTFNTF
TGGQNNTLPH PHPHPHSHST TRV
