| Gene |
Nrxn1
|
| Protein Name |
NRX1A_RAT |
| Organism |
Rattus norvegicus (Rat) |
| Alternative name(s) |
Neurexin-1 (Neurexin I-alpha) (Neurexin-1-alpha) |
| Protein Family |
Neurexin family |
| NCBI Gene ID |
60391
|
| UniProt ID |
Q63372
|
| Enzyme Class |
- |
| Molecular Weight |
167923 |
| Protein Length |
1530 |
| Protein Domain |
InterPro |
Pfam
|
| 3D Structure |
PDBe |
PDBj |
RCSB PDB |
DrugPort
ModBase |
SwissModel
|
| Gene Expression |
Gene Expression Atlas
|
| Function and Disease |
OMIM |
| Protein-protein Interaction Database |
STRING |
IntAct |
MINT
|
| Kinase Database |
Phospho.ELM
|
PhosphoSite
| NetworKIN
|
| Catalytic Activity (UniProt annotation) |
- |
| Localization |
Cell membrane; Single-pass type I membrane protein. Cell junction, synapse, presynaptic cell membrane. |
| Function (UniProt annotation) |
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 Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-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 (By similarity). 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. |
| Gene Ontology |
GO:0005246; GO:0005509; GO:0005783; GO:0005886; GO:0006904; GO:0007155; GO:0007268; GO:0007269; GO:0007416; GO:0007612; GO:0007623; GO:0009986; GO:0016021; GO:0030054; GO:0030534; GO:0031965; GO:0031982; GO:0033130; GO:0042734; GO:0043025; GO:0050839; GO:0050885; GO:0051290; GO:0051965; GO:0051968; GO:0060134; GO:0090129; GO:0097104; GO:0097109; GO:0097116; GO:0097118; GO:0097119; GO:0099054; GO:2000463; GO:2000821 |
