NLGN1

Neuroligin-1 is a protein that in humans is encoded by the NLGN1 gene.[5][6][7]

NLGN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3B3Q
Identifiers
Aliases	NLGN1, NL1, neuroligin 1
External IDs	OMIM: 600568 MGI: 2179435 HomoloGene: 56690 GeneCards: NLGN1
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q26.31 Start 173,396,284 bp[1] End 174,286,644 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 A3 Start 25,426,215 bp[2] End 26,332,460 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • PDZ domain binding • protein dimerization activity • cell adhesion molecule binding • scaffold protein binding • GO:0004091 carboxylic ester hydrolase activity • neurexin family protein binding • receptor activity • amyloid-beta binding • signaling receptor activity Cellular component • synapse • integral component of membrane • NMDA selective glutamate receptor complex • Golgi apparatus • cell junction • dendritic shaft • filopodium tip • dendritic spine • postsynaptic membrane • membrane • dendrite • excitatory synapse • external side of plasma membrane • cell surface • presynapse • GO:0097483, GO:0097481 postsynaptic density • cell membrane • integral component of postsynaptic membrane • integral component of plasma membrane • spanning component of membrane • postsynapse • glutamatergic synapse • asymmetric, glutamatergic, excitatory synapse • integral component of postsynaptic specialization membrane Biological process • NMDA glutamate receptor clustering • positive regulation of ruffle assembly • positive regulation of synaptic vesicle exocytosis • regulation of AMPA receptor activity • rhythmic process • positive regulation of synaptic transmission, glutamatergic • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules • positive regulation of circadian sleep/wake cycle, wakefulness • regulation of respiratory gaseous exchange by neurological system process • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules • protein heterotetramerization • synaptic vesicle transport • terminal button organization • synapse organization • positive regulation of synaptic transmission, GABAergic • postsynaptic density protein 95 clustering • receptor localization to synapse • protein localization to synapse • neurexin clustering involved in presynaptic membrane assembly • positive regulation of synaptic vesicle endocytosis • synaptic vesicle targeting • protein homooligomerization • positive regulation of protein localization to synapse • neuron projection development • protein targeting • GO:0010740 positive regulation of intracellular signal transduction • long-term synaptic potentiation • nervous system development • AMPA glutamate receptor clustering • neuronal signal transduction • synaptic vesicle clustering • positive regulation of synaptic vesicle clustering • cytoskeletal matrix organization at active zone • synapse assembly • establishment of protein localization • modulation of chemical synaptic transmission • positive regulation of filopodium assembly • cell adhesion • regulation of neuron differentiation • neuron cell-cell adhesion • positive regulation of dendritic spine development • regulation of NMDA receptor activity • positive regulation of excitatory postsynaptic potential • negative regulation of dendritic spine morphogenesis • positive regulation of synapse assembly • excitatory synapse assembly • positive regulation of presynaptic active zone assembly • retrograde trans-synaptic signaling by trans-synaptic protein complex • synaptic vesicle endocytosis • postsynaptic membrane assembly • presynaptic membrane assembly • cellular response to calcium ion • postsynaptic specialization assembly • presynapse assembly • regulation of presynapse organization • synaptic membrane adhesion • neuron projection arborization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	22871	192167
Ensembl	ENSG00000169760	ENSMUSG00000063887
UniProt	Q8N2Q7	Q99K10
RefSeq (mRNA)	NM_014932 NM_001365923 NM_001365924 NM_001365925 NM_001365926 NM_001365927 NM_001365928 NM_001365929 NM_001365930 NM_001365931 NM_001365932 NM_001365933 NM_001365934 NM_001365935 NM_001365936	NM_001163387 NM_138666 NM_001357095 NM_001357096 NM_001357097
RefSeq (protein)	NP_055747 NP_001352852 NP_001352853 NP_001352854 NP_001352855 NP_001352856 NP_001352857 NP_001352858 NP_001352859 NP_001352860 NP_001352861 NP_001352862 NP_001352863 NP_001352864 NP_001352865	NP_001156859 NP_619607 NP_001344024 NP_001344025 NP_001344026
Location (UCSC)	Chr 3: 173.4 – 174.29 Mb	Chr 3: 25.43 – 26.33 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a member of the neuroligin family of neuronal cell surface proteins. Neuroligin-1 acts as splice site-specific ligand for β-neurexins and has been shown to localize to the postsynaptic compartment at excitatory synapses and is involved in the formation and remodeling of central nervous system synapses.[7][8]

Interactions

NLGN1 has been shown to interact with NRXN1[9][10] and DLG4.[11]

See also

• Neurexins: NRXN1, NRXN2, NRXN3

References

1. GRCh38: Ensembl release 89: ENSG00000169760 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000063887 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Philibert RA, Winfield SL, Sandhu HK, Martin BM, Ginns EI (April 2000). "The structure and expression of the human neuroligin-3 gene". Gene. 246 (1–2): 303–10. doi:10.1016/S0378-1119(00)00049-4. PMID 10767552.
6. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O (April 2000). "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 7 (2): 143–50. doi:10.1093/dnares/7.2.143. PMID 10819331.
7. "Entrez Gene: NLGN1 neuroligin 1".
8. Scheiffele P, Fan J, Choih J, Fetter R, Serafini T (June 2000). "Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons". Cell. 101 (6): 657–69. doi:10.1016/S0092-8674(00)80877-6. PMID 10892652.
9. Comoletti D, Flynn R, Jennings LL, et al. (December 2003). "Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta". The Journal of Biological Chemistry. 278 (50): 50497–505. doi:10.1074/jbc.M306803200. PMID 14522992.
10. Ichtchenko K, Nguyen T, Südhof TC (February 1996). "Structures, alternative splicing, and neurexin binding of multiple neuroligins". The Journal of Biological Chemistry. 271 (5): 2676–82. doi:10.1074/jbc.271.5.2676. PMID 8576240.
11. Irie M, Hata Y, Takeuchi M, et al. (September 1997). "Binding of neuroligins to PSD-95". Science. 277 (5331): 1511–5. doi:10.1126/science.277.5331.1511. PMID 9278515.

Further reading

• Cantallops I, Cline HT (September 2000). "Synapse formation: if it looks like a duck and quacks like a duck .". Current Biology. 10 (17): R620–3. doi:10.1016/S0960-9822(00)00663-1. PMID 10996085.
• Ichtchenko K, Hata Y, Nguyen T, et al. (May 1995). "Neuroligin 1: a splice site-specific ligand for beta-neurexins". Cell. 81 (3): 435–43. doi:10.1016/0092-8674(95)90396-8. PMID 7736595.
• Ichtchenko K, Nguyen T, Südhof TC (February 1996). "Structures, alternative splicing, and neurexin binding of multiple neuroligins". The Journal of Biological Chemistry. 271 (5): 2676–82. doi:10.1074/jbc.271.5.2676. PMID 8576240.
• Irie M, Hata Y, Takeuchi M, et al. (September 1997). "Binding of neuroligins to PSD-95". Science. 277 (5331): 1511–5. doi:10.1126/science.277.5331.1511. PMID 9278515.
• Kikuno R, Nagase T, Ishikawa K, et al. (June 1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (3): 197–205. doi:10.1093/dnares/6.3.197. PMID 10470851.
• Scheiffele P, Fan J, Choih J, Fetter R, Serafini T (June 2000). "Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons". Cell. 101 (6): 657–69. doi:10.1016/S0092-8674(00)80877-6. PMID 10892652.
• Strausberg RL, Feingold EA, Grouse LH, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Comoletti D, Flynn R, Jennings LL, et al. (December 2003). "Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta". The Journal of Biological Chemistry. 278 (50): 50497–505. doi:10.1074/jbc.M306803200. PMID 14522992.
• Ota T, Suzuki Y, Nishikawa T, et al. (January 2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nature Genetics. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (October 2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Research. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Chubykin AA, Liu X, Comoletti D, Tsigelny I, Taylor P, Südhof TC (June 2005). "Dissection of synapse induction by neuroligins: effect of a neuroligin mutation associated with autism". The Journal of Biological Chemistry. 280 (23): 22365–74. doi:10.1074/jbc.M410723200. PMID 15797875.
• Muzny DM, Scherer SE, Kaul R, et al. (April 2006). "The DNA sequence, annotation and analysis of human chromosome 3". Nature. 440 (7088): 1194–8. doi:10.1038/nature04728. PMID 16641997.
• Li X, Zhang J, Cao Z, Wu J, Shi Y (September 2006). "Solution structure of GOPC PDZ domain and its interaction with the C-terminal motif of neuroligin". Protein Science. 15 (9): 2149–58. doi:10.1110/ps.062087506. PMC 2242614. PMID 16882988.