Q9CS84 (NRX1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 120.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Neurexin-1 Alternative name(s): Neurexin I-alpha Neurexin-1-alpha | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1514 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca2+-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca2+-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 |
| Subunit structure | The cytoplasmic C-terminal region binds to CASK, CASKIN1 and APBA1. Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3 By similarity. Alpha-type isoforms (neurexin-1-alpha) interact (via laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via alpha-dystroglycan chain). Alpha-type isoforms interact with alpha-latrotoxin from spider venom. Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 By similarity. Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer interacts with one NRXN1 dimer. Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN1, NLGN2, NLGN3 and NLGN4L; these interactions are calcium-dependent. Interacts with SYT13 and SYTL1. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4. Ref.8 Ref.9 Ref.10 Ref.16 Ref.18 Ref.19 Ref.20 |
| Subcellular location | Cell membrane; Single-pass type I membrane protein. Cell junction › synapse. Note: Localized on the pre-synaptic membrane By similarity. Ref.18 |
| Post-translational modification | N-glycosylated By similarity. O-glycosylated By similarity. |
| Disruption phenotype | No visible phenotype, but mice display subtle behavorial deficits. Females show deficits in nest building and taking care of pups. Mice lacking the alpha-type isoforms of NRXN1, NRXN2 and NRXN3 are born at the expected Mendelian rate, but die during the first day after birth, probably due to neurological defects in the brainstem that impair normal breathing. These mice express normal levels of the beta-type isoforms of NRXN1, NRXN2 and NRXN3. Mice show reduced density of synapses in the brainstem, especially a reduction in the numbers of GABA-releasing synapses. Their brains display a reduced frequency of spontaneous neurotransmitter release, and decreased neurotransmitter release in response to an action potential. Likewise, the activity of voltage-gated calcium channels is strongly decreased. A small proportion (5-10%) of mice lacking the alpha-type isoforms of both NRXN1 and NRXN2 survive to adulthood; these mice do not show any gross anatomical defects in their brains or changes in the distribution of synaptic proteins, but they have fewer synapses in the neocortex and show defects in neurotransmitter release at neuromuscular junctions. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 |
| Sequence similarities | Belongs to the neurexin family. Contains 3 EGF-like domains. Contains 6 laminin G-like domains. |
| Sequence caution | The sequence BAC41433.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
Alternative products
| This entry describes 6 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1a (identifier: Q9CS84-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2a (identifier: Q9CS84-2) Also known as: Alpha-2B; The sequence of this isoform differs from the canonical sequence as follows: 387-393: Missing. | ||||||
| Isoform 3a (identifier: Q9CS84-3) Also known as: Alpha-2C; The sequence of this isoform differs from the canonical sequence as follows: 379-393: Missing. | ||||||
| Isoform 4a (identifier: Q9CS84-4) The sequence of this isoform differs from the canonical sequence as follows: 1-320: Missing. 379-393: Missing. 1410-1412: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 1b (identifier: P0DI97-1) The sequence of this isoform can be found in the external entry P0DI97. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. | ||||||
| Isoform 5a (identifier: Q9CS84-5) The sequence of this isoform differs from the canonical sequence as follows: 387-393: Missing. 1247-1276: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 30 | 30 | Potential | ||||||||||||||||||||||||||||||||||||||
| Chain | 31 – 1514 | 1484 | Neurexin-1 | PRO_0000043164 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Topological domain | 31 – 1438 | 1408 | Extracellular Potential | ||||||||||||||||||||||||||||||||||||||
| Transmembrane | 1439 – 1459 | 21 | Helical; Potential | ||||||||||||||||||||||||||||||||||||||
| Topological domain | 1460 – 1514 | 55 | Cytoplasmic Potential | ||||||||||||||||||||||||||||||||||||||
| Domain | 31 – 217 | 187 | Laminin G-like 1 | ||||||||||||||||||||||||||||||||||||||
| Domain | 219 – 256 | 38 | EGF-like 1 | ||||||||||||||||||||||||||||||||||||||
| Domain | 283 – 480 | 198 | Laminin G-like 2 | ||||||||||||||||||||||||||||||||||||||
| Domain | 487 – 679 | 193 | Laminin G-like 3 | ||||||||||||||||||||||||||||||||||||||
| Domain | 683 – 720 | 38 | EGF-like 2 | ||||||||||||||||||||||||||||||||||||||
| Domain | 725 – 898 | 174 | Laminin G-like 4 | ||||||||||||||||||||||||||||||||||||||
| Domain | 912 – 1087 | 176 | Laminin G-like 5 | ||||||||||||||||||||||||||||||||||||||
| Domain | 1090 – 1127 | 38 | EGF-like 3 | ||||||||||||||||||||||||||||||||||||||
| Domain | 1133 – 1331 | 199 | Laminin G-like 6 | ||||||||||||||||||||||||||||||||||||||
| Compositional bias | 13 – 21 | 9 | Poly-Leu | ||||||||||||||||||||||||||||||||||||||
| Compositional bias | 1361 – 1364 | 4 | Poly-Thr | ||||||||||||||||||||||||||||||||||||||
| Compositional bias | 1446 – 1449 | 4 | Poly-Ala | ||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||
| Metal binding | 329 | 1 | Calcium 1 By similarity | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 346 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 414 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 772 | 1 | Calcium 2 By similarity | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 789 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 848 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 1183 | 1 | Calcium 3 | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 1200 | 1 | Calcium 3; via carbonyl oxygen | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 1282 | 1 | Calcium 3; via carbonyl oxygen | ||||||||||||||||||||||||||||||||||||||
| Metal binding | 1284 | 1 | Calcium 3 | ||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 125 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||
| Glycosylation | 190 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||
| Glycosylation | 797 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||
| Glycosylation | 1230 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 228 ↔ 243 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 245 ↔ 255 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 444 ↔ 480 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 650 ↔ 679 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 687 ↔ 698 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 692 ↔ 707 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 709 ↔ 719 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 1059 ↔ 1087 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 1094 ↔ 1105 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 1099 ↔ 1114 | By similarity | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 1116 ↔ 1126 | By similarity | |||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 320 | 320 | Missing in isoform 4a. | VSP_016400 | |||||||||||||||||||||||||||||||||||||
| Alternative sequence | 379 – 393 | 15 | Missing in isoform 3a and isoform 4a. | VSP_003485 | |||||||||||||||||||||||||||||||||||||
| Alternative sequence | 387 – 393 | 7 | Missing in isoform 2a and isoform 5a. | VSP_003484 | |||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1247 – 1276 | 30 | Missing in isoform 5a. | VSP_043946 | |||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1410 – 1412 | 3 | Missing in isoform 4a. | VSP_016401 | |||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 1132 – 1145 | 14 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1154 – 1164 | 11 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1168 – 1181 | 14 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1184 – 1190 | 7 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1193 – 1202 | 10 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1205 – 1208 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1216 – 1218 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1220 – 1227 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1230 – 1235 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1241 – 1243 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1265 – 1277 | 13 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1286 – 1292 | 7 | |||||||||||||||||||||||||||||||||||||||
| Helix | 1294 – 1296 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1302 – 1309 | 8 | |||||||||||||||||||||||||||||||||||||||
| Helix | 1314 – 1319 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 1325 – 1333 | 9 | |||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H. DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A). Tissue: Brain. |
| [2] | Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: C57BL/6J. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4A). Tissue: Eye. |
| [5] | "Sequencing of the neurexin genes." Graveley B.R., Philipps D.L. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 298-437 (ISOFORMS 1A; 2A AND 3A/4A). Strain: CD-1. Tissue: Brain. |
| [6] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1126-1514 (ISOFORMS 1A/2A/3A). Strain: C57BL/6J. Tissue: Embryo. |
| [7] | "Differential seizure-induced and developmental changes of neurexin expression." Gorecki D.C., Szklarczyk A., Lukasiuk K., Kaczmarek L., Simons J.P. Mol. Cell. Neurosci. 13:218-227(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1463-1505 (ISOFORMS 1A/2A/3A/4A). Strain: C57BL/10. Tissue: Brain. |
| [8] | "Neurexin I alpha is a major alpha-latrotoxin receptor that cooperates in alpha-latrotoxin action." Geppert M., Khvotchev M., Krasnoperov V., Goda Y., Missler M., Hammer R.E., Ichtchenko K., Petrenko A.G., Sudhof T.C. J. Biol. Chem. 273:1705-1710(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, CALCIUM-DEPENDENT INTERACTION WITH ALPHA-LATROTOXIN. |
| [9] | "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins." Fukuda M., Mikoshiba K. Biochem. Biophys. Res. Commun. 281:1226-1233(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYTL1. |
| [10] | "Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII)." Fukuda M., Mikoshiba K. Biochem. J. 354:249-257(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYT13. |
| [11] | "Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis." Missler M., Zhang W., Rohlmann A., Kattenstroth G., Hammer R.E., Gottmann K., Sudhof T.C. Nature 423:939-948(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN NEUROTRANSMITTER RELEASE. |
| [12] | "Postsynaptic N-methyl-D-aspartate receptor function requires alpha-neurexins." Kattenstroth G., Tantalaki E., Sudhof T.C., Gottmann K., Missler M. Proc. Natl. Acad. Sci. U.S.A. 101:2607-2612(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION. |
| [13] | "Important contribution of alpha-neurexins to Ca2+-triggered exocytosis of secretory granules." Dudanova I., Sedej S., Ahmad M., Masius H., Sargsyan V., Zhang W., Riedel D., Angenstein F., Schild D., Rupnik M., Missler M. J. Neurosci. 26:10599-10613(2006) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION. |
| [14] | "alpha-Neurexins are required for efficient transmitter release and synaptic homeostasis at the mouse neuromuscular junction." Sons M.S., Busche N., Strenzke N., Moser T., Ernsberger U., Mooren F.C., Zhang W., Ahmad M., Steffens H., Schomburg E.D., Plomp J.J., Missler M. Neuroscience 138:433-446(2006) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION. |
| [15] | "Deletion of alpha-neurexins does not cause a major impairment of axonal pathfinding or synapse formation." Dudanova I., Tabuchi K., Rohlmann A., Sudhof T.C., Missler M. J. Comp. Neurol. 502:261-274(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE. |
| [16] | "Unusually rapid evolution of neuroligin-4 in mice." Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V., Sudhof T.C. Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLGN4L. |
| [17] | "Mouse neurexin-1alpha deletion causes correlated electrophysiological and behavioral changes consistent with cognitive impairments." Etherton M.R., Blaiss C.A., Powell C.M., Sudhof T.C. Proc. Natl. Acad. Sci. U.S.A. 106:17998-18003(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE. |
| [18] | "Cbln family proteins promote synapse formation by regulating distinct neurexin signaling pathways in various brain regions." Matsuda K., Yuzaki M. Eur. J. Neurosci. 33:1447-1461(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBLN1; CBLN2 AND CBLN4. |
| [19] | "Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4." Koehnke J., Jin X., Trbovic N., Katsamba P.S., Brasch J., Ahlsen G., Scheiffele P., Honig B., Palmer A.G. III, Shapiro L. Structure 16:410-421(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1132-1334 (ISOFORM 5A) IN COMPLEX WITH CALCIUM, SUBUNIT, INTERACTION WITH NLGN1 AND NLGN2, ALTERNATIVE SPLICING. |
| [20] | "Splice form dependence of beta-neurexin/neuroligin binding interactions." Koehnke J., Katsamba P.S., Ahlsen G., Bahna F., Vendome J., Honig B., Shapiro L., Jin X. Neuron 67:61-74(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 1132-1334, INTERACTION WITH NLGN1; NLGN2 AND NLGN3. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AB093249 mRNA. Translation: BAC41433.2. Different initiation. AC101872 Genomic DNA. No translation available. AC131326 Genomic DNA. No translation available. AC151286 Genomic DNA. No translation available. AC154325 Genomic DNA. No translation available. AC154599 Genomic DNA. No translation available. AC167814 Genomic DNA. No translation available. AC170901 Genomic DNA. No translation available. AC171209 Genomic DNA. No translation available. CT025708 Genomic DNA. No translation available. CT486002 Genomic DNA. No translation available. BC047146 mRNA. Translation: AAH47146.1. AF387674 Genomic DNA. Translation: AAK70469.1. AF387674 Genomic DNA. Translation: AAK70470.1. AF387674 Genomic DNA. Translation: AAK70471.1. AK017578 mRNA. Translation: BAB30815.1. AJ006802 mRNA. Translation: CAA07257.1. | ||||||||||||||||||
| IPI | IPI00230050. IPI00230051. IPI00468539. IPI00970455. | ||||||||||||||||||
| RefSeq | NP_064648.3. NM_020252.3. NP_796258.2. NM_177284.2. | ||||||||||||||||||
| UniGene | Mm.312068. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | Q9CS84. | ||||||||||||||||||
| SMR | Q9CS84. Positions 56-1335. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | Q9CS84. 5 interactions. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q9CS84. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PaxDb | Q9CS84. | ||||||||||||||||||
| PRIDE | Q9CS84. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSMUST00000054059; ENSMUSP00000057294; ENSMUSG00000024109. ENSMUST00000160844; ENSMUSP00000125407; ENSMUSG00000024109. ENSMUST00000161402; ENSMUSP00000124116; ENSMUSG00000024109. ENSMUST00000174331; ENSMUSP00000133491; ENSMUSG00000024109. | ||||||||||||||||||
| GeneID | 18189. | ||||||||||||||||||
| KEGG | mmu:18189. | ||||||||||||||||||
| UCSC | uc008dvz.2. mouse. uc008dwa.2. mouse. uc012ayq.1. mouse. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 9378. | ||||||||||||||||||
| MGI | MGI:1096391. Nrxn1. | ||||||||||||||||||
| Rouge | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | NOG302266. | ||||||||||||||||||
| GeneTree | ENSGT00560000076996. | ||||||||||||||||||
| HOGENOM | HOG000230481. | ||||||||||||||||||
| HOVERGEN | HBG052670. | ||||||||||||||||||
| InParanoid | Q9CS84. | ||||||||||||||||||
| KO | K07377. | ||||||||||||||||||
| OMA | NAYACEC. | ||||||||||||||||||
| OrthoDB | EOG41G339. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q9CS84. | ||||||||||||||||||
| Bgee | Q9CS84. | ||||||||||||||||||
| CleanEx | MM_NRXN1. | ||||||||||||||||||
| Genevestigator | Q9CS84. | ||||||||||||||||||
| GermOnline | ENSMUSG00000024109. Mus musculus. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 2.60.120.200. 6 hits. | ||||||||||||||||||
| InterPro | IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000742. EG-like_dom. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR001791. Laminin_G. IPR003585. Neurexin-like. IPR027158. NRXN1-alpha. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR10127:SF309. PTHR10127:SF309. 1 hit. | ||||||||||||||||||
| Pfam | PF02210. Laminin_G_2. 6 hits. [Graphical view] | ||||||||||||||||||
| SMART | SM00294. 4.1m. 1 hit. SM00181. EGF. 3 hits. SM00282. LamG. 6 hits. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF49899. ConA_like_lec_gl. 6 hits. | ||||||||||||||||||
| PROSITE | PS00010. ASX_HYDROXYL. 1 hit. PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. 3 hits. PS50025. LAM_G_DOMAIN. 6 hits. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| ChiTaRS | NRXN1. mouse. | ||||||||||||||||||
| EvolutionaryTrace | Q9CS84. | ||||||||||||||||||
| NextBio | 293528. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | NRX1A_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9CS84 Secondary accession number(s): G3UWZ9 Q8CHE6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
