Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Neurexin-1-alpha  

UniProtKB / Swiss-Prot ID :  NRX1A_BOVIN

Gene Name (Synonyms) : 
NRXN1  

Species :  Bos taurus (Bovine). 

Subcellular Localization :  Cell membrane; Single-pass type I membrane protein (Probable). Cell junction, synapse, presynaptic cell membrane (By similarity). 

Protein Function :  Cell surface protein involved in cell-cell-interactions, excytosis 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-latroxin from spider venom. 

Transmembrane Topology (topPTM) : NRX1A_BOVIN 

Protein Sequence MGTALLQRGGCFLLCLSLLLLGCWAELGSGLEFPGAEGQWTRFPKWNACCESEMSFQLKTRSARGLVLYF...
Predicted Secondary Structure CCCCEEECCCEEEEECCCCCCCCCCCCCCEEEECCCCCCCEECCCCCCCCEEEEEEEEEEECCCEEEEEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
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Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
705O-linked (GlcNAc...).KPCLSNPCK
CCCCCCCCC
45.50UniProtKB
Link-
1246N-linked (GlcNAc...).RSGGNATLQ
EECCEEEEE
33.02UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis for variant-specific neuroligin-binding by alpha-neurexin.";
Tanaka H., Nogi T., Yasui N., Iwasaki K., Takagi J.;
PLoS ONE 6:E19411-E19411(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 923-1353, GLYCOSYLATION ATASN-1246, INTERACTION WITH NLGN1, ELECTRON MICROSCOPY, AND DISULFIDEBONDS.
"The crystal structure of the alpha-neurexin-1 extracellular regionreveals a hinge point for mediating synaptic adhesion and function.";
Miller M.T., Mileni M., Comoletti D., Stevens R.C., Harel M.,Taylor P.;
Structure 19:767-778(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 296-1349, GLYCOSYLATION ATSER-705 AND ASN-1246, INTERACTION WITH NLGN1, AND DISULFIDE BONDS.
"The structure of neurexin 1alpha reveals features promoting a role assynaptic organizer.";
Chen F., Venugopal V., Murray B., Rudenko G.;
Structure 19:779-789(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 31-1355, GLYCOSYLATION ATASN-1246, AND DISULFIDE BONDS.
O-linked Glycosylation
ReferencePubMed
"The crystal structure of the alpha-neurexin-1 extracellular regionreveals a hinge point for mediating synaptic adhesion and function.";
Miller M.T., Mileni M., Comoletti D., Stevens R.C., Harel M.,Taylor P.;
Structure 19:767-778(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 296-1349, GLYCOSYLATION ATSER-705 AND ASN-1246, INTERACTION WITH NLGN1, AND DISULFIDE BONDS.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures