NRXN1

NRXN1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3B3Q
Identifiers
Aliases	NRXN1, Hs.22998, PTHSL2, SCZD17, neurexin 1
External IDs	MGI: 1096391 HomoloGene: 21005 GeneCards: NRXN1
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	51,225,575 bp[1]
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)[2]
End	91,093,071 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• metal ion binding; • calcium-dependent protein binding; • neuroligin family protein binding; • receptor binding; • transmembrane signaling receptor activity; • cell adhesion molecule binding; • protein binding; • calcium ion binding; • acetylcholine receptor binding; • calcium channel regulator activity; • signaling receptor activity;
Cellular component	• integral component of membrane; • vesicle; • nuclear membrane; • membrane; • endocytic vesicle; • axonal growth cone; • synapse; • cell surface; • cell junction; • neuronal cell body; • endoplasmic reticulum; • presynaptic membrane; • plasma membrane; • integral component of presynaptic membrane; • integral component of plasma membrane; • nucleolus; • macromolecular complex; • Schaffer collateral - CA1 synapse; • glutamatergic synapse; • GABA-ergic synapse; • integral component of presynaptic active zone membrane;
Biological process	• calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; • receptor localization to synapse; • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; • NMDA glutamate receptor clustering; • establishment of protein localization; • neuron cell-cell adhesion; • gamma-aminobutyric acid receptor clustering; • neuronal signal transduction; • gephyrin clustering involved in postsynaptic density assembly; • postsynaptic density protein 95 clustering; • learning; • regulation of AMPA receptor activity; • negative regulation of filopodium assembly; • presynaptic membrane assembly; • regulation of NMDA receptor activity; • vocalization behavior; • neuroligin clustering involved in postsynaptic membrane assembly; • adult behavior; • positive regulation of synaptic transmission, glutamatergic; • postsynaptic membrane assembly; • cell adhesion; • angiogenesis; • positive regulation of excitatory postsynaptic potential; • social organism behavior; • guanylate kinase-associated protein clustering; • synapse assembly; • protein complex assembly involved in synapse maturation; • synaptic vesicle clustering; • protein localization to synapse; • signal transduction; • cerebellar granule cell differentiation; • positive regulation of synapse assembly; • positive regulation of presynaptic active zone assembly; • positive regulation of protein localization to plasma membrane; • vocal learning; • chemical synaptic transmission; • regulation of insulin secretion involved in cellular response to glucose stimulus; • axon guidance; • prepulse inhibition; • neuromuscular process controlling balance; • positive regulation of synapse maturation; • neurotransmitter secretion; • regulation of grooming behavior; • synaptic membrane adhesion; • regulation of synaptic vesicle cycle; • regulation of postsynaptic specialization assembly; • regulation of presynapse assembly; • regulation of postsynaptic density assembly; • trans-synaptic signaling by endocannabinoid;
	Sources:Amigo / QuickGO
Orthologs
	9378
	18189
	ENSG00000179915
	ENSMUSG00000024109
	P58400; Q9ULB1; Q49A31
	P0DI97; Q9CS84
NM_001135659; NM_004801; NM_138735; NM_001320156; NM_001320157;
	NM_001330077; NM_001330078; NM_001330079; NM_001330081; NM_001330082; NM_001330083; NM_001330084; NM_001330085; NM_001330086; NM_001330087; NM_001330088; NM_001330089; NM_001330090; NM_001330091; NM_001330092; NM_001330093; NM_001330094; NM_001330095; NM_001330096; NM_001330097
NM_020252; NM_177284; NM_001346957; NM_001346958; NM_001346959;
	NM_001346960; NM_001346961; NM_001346962; NM_001347419
NP_001129131; NP_001307085; NP_001307086; NP_001317006; NP_001317007;
	NP_001317008; NP_001317010; NP_001317011; NP_001317012; NP_001317013; NP_001317014; NP_001317015; NP_001317016; NP_001317017; NP_001317018; NP_001317019; NP_001317020; NP_001317021; NP_001317022; NP_001317023; NP_001317024; NP_001317025; NP_001317026; NP_004792; NP_620072; NP_001129131.1; NP_004792.1; NP_620072.1; NP_004792.1; NP_004792.1; NP_620072.1
NP_001333886; NP_001333887; NP_001333888; NP_001333889; NP_001333890;
	NP_001333891; NP_001334348; NP_064648; NP_796258; NP_064648.3; NP_796258.2
	Wikidata
View/Edit Human	View/Edit Mouse

Neurexin-1-alpha is a protein that in humans is encoded by the NRXN1 gene.^[5]

Neurexins are a family of proteins that function in the vertebrate nervous system as cell adhesion molecules and receptors. They are encoded by several unlinked genes of which two, NRXN1 and NRXN3, are among the largest known human genes. Three of the genes (NRXN1-3) utilize two alternate promoters and include numerous alternatively spliced exons to generate thousands of distinct mRNA transcripts and protein isoforms. The majority of transcripts are produced from the upstream promoter and encode alpha-neurexin isoforms; a much smaller number of transcripts are produced from the downstream promoter and encode beta-neurexin isoforms. The alpha-neurexins contain epidermal growth factor-like (EGF-like) sequences and laminin G domains, and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins.^[5]

Genomics

The gene is found in a single copy on the short arm of chromosome 2 (2p16.3). The gene is 1,112,187 bases in length, is located on the Crick (minus) strand and encodes a protein of 1,477 amino acids (molecular weight 161.883 kDa).

Mutations of this gene that interrupt its expression have been associated with schizophrenia, autism, and intellectual disability (NRXN1 mutations and brain disorders).

Interactions

NRXN1 has been shown to interact with NLGN1.^[6]^[7]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000179915 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024109 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "Entrez Gene: NRXN1 neurexin 1".
↑ Comoletti, Davide; Flynn Robyn; Jennings Lori L; Chubykin Alexander; Matsumura Takehito; Hasegawa Hana; Südhof Thomas C; Taylor Palmer (Dec 2003). "Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta". J. Biol. Chem. United States. 278 (50): 50497–50505. doi:10.1074/jbc.M306803200. ISSN 0021-9258. PMID 14522992.
↑ Ichtchenko, K; Nguyen T; Südhof T C (Feb 1996). "Structures, alternative splicing, and neurexin binding of multiple neuroligins". J. Biol. Chem. UNITED STATES. 271 (5): 2676–2682. doi:10.1074/jbc.271.5.2676. ISSN 0021-9258. PMID 8576240.

Missler M, Südhof TC (1998). "Neurexins: three genes and 1001 products". Trends Genet. 14 (1): 20–26. doi:10.1016/S0168-9525(97)01324-3. PMID 9448462.
Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
Ushkaryov YA, Petrenko AG, Geppert M, Südhof TC (1992). "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin". Science. 257 (5066): 50–56. Bibcode:1992Sci...257...50U. doi:10.1126/science.1621094. PMID 1621094.
Ichtchenko K, Nguyen T, Südhof TC (1996). "Structures, alternative splicing, and neurexin binding of multiple neuroligins". J. Biol. Chem. 271 (5): 2676–2682. doi:10.1074/jbc.271.5.2676. PMID 8576240.
Petrenko AG, Ullrich B, Missler M, et al. (1996). "Structure and evolution of neurexophilin". J. Neurosci. 16 (14): 4360–9. PMID 8699246.
Hata Y, Butz S, Südhof TC (1996). "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins". J. Neurosci. 16 (8): 2488–94. PMID 8786425.
Perin MS (1996). "Mirror image motifs mediate the interaction of the COOH terminus of multiple synaptotagmins with the neurexins and calmodulin". Biochemistry. 35 (43): 13808–13816. doi:10.1021/bi960853x. PMID 8901523.
Nguyen T, Südhof TC (1997). "Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules". J. Biol. Chem. 272 (41): 26032–26039. doi:10.1074/jbc.272.41.26032. PMID 9325340.
Nagase T, Ishikawa K, Miyajima N, et al. (1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (1): 31–39. doi:10.1093/dnares/5.1.31. PMID 9628581.
Missler M, Hammer RE, Südhof TC (1999). "Neurexophilin binding to alpha-neurexins. A single LNS domain functions as an independently folding ligand-binding unit". J. Biol. Chem. 273 (52): 34716–34723. doi:10.1074/jbc.273.52.34716. PMID 9856994.
Kleiderlein JJ, Nisson PE, Jessee J, et al. (1999). "CCG repeats in cDNAs from human brain". Hum. Genet. 103 (6): 666–673. doi:10.1007/s004390050889. PMID 9921901.
Biederer T, Südhof TC (2001). "Mints as adaptors. Direct binding to neurexins and recruitment of munc18". J. Biol. Chem. 275 (51): 39803–39806. doi:10.1074/jbc.C000656200. PMID 11036064.
Koroll M, Rathjen FG, Volkmer H (2001). "The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity". J. Biol. Chem. 276 (14): 10646–10654. doi:10.1074/jbc.M010647200. PMID 11152476.
Fukuda M, Mikoshiba K (2001). "Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII)". Biochem. J. 354 (Pt 2): 249–57. doi:10.1042/0264-6021:3540249. PMC 1221650. PMID 11171101.
Fukuda M, Mikoshiba K (2001). "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins". Biochem. Biophys. Res. Commun. 281 (5): 1226–1233. doi:10.1006/bbrc.2001.4512. PMID 11243866.
Rowen L, Young J, Birditt B, et al. (2002). "Analysis of the human neurexin genes: alternative splicing and the generation of protein diversity". Genomics. 79 (4): 587–597. doi:10.1006/geno.2002.6734. PMID 11944992.
Tabuchi K, Südhof TC (2002). "Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing". Genomics. 79 (6): 849–859. doi:10.1006/geno.2002.6780. PMID 12036300.
Nakayama M, Kikuno R, Ohara O (2003). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Res. 12 (11): 1773–1784. doi:10.1101/gr.406902. PMC 187542. PMID 12421765.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000179915 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024109 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[entrez-5] 1 2 "Entrez Gene: NRXN1 neurexin 1".

[pmid14522992-6] Comoletti, Davide; Flynn Robyn; Jennings Lori L; Chubykin Alexander; Matsumura Takehito; Hasegawa Hana; Südhof Thomas C; Taylor Palmer (Dec 2003). "Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta". J. Biol. Chem. United States. 278 (50): 50497–50505. doi:10.1074/jbc.M306803200. ISSN 0021-9258. PMID 14522992.

[pmid8576240-7] Ichtchenko, K; Nguyen T; Südhof T C (Feb 1996). "Structures, alternative splicing, and neurexin binding of multiple neuroligins". J. Biol. Chem. UNITED STATES. 271 (5): 2676–2682. doi:10.1074/jbc.271.5.2676. ISSN 0021-9258. PMID 8576240.

NRXN1

Genomics

Interactions

References

Further reading