Q63372 · NRX1A_RAT

Function

function

Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission (By similarity).
Function is isoform-specific (By similarity).
Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission (By similarity).
Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca2+-triggered neurotransmitter release at synapses and at neuromuscular junctions (By similarity).
They play an important role in Ca2+-triggered exocytosis of secretory granules in pituitary gland (By similarity).
They may affect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery (By similarity).
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 (By similarity).
In vitro, triggers the de novo formation of presynaptic structures (PubMed:20064387, PubMed:20064388).
May be involved in specification of excitatory synapses (PubMed:20064387, PubMed:20064388).
Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom (PubMed:20064387, PubMed:20064388).

Miscellaneous

Alpha-latrotoxin competes with alpha-dystroglycan for binding.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site345Ca2+ 1 (UniProtKB | ChEBI)
Binding site362Ca2+ 1 (UniProtKB | ChEBI)
Binding site430Ca2+ 1 (UniProtKB | ChEBI)
Binding site788Ca2+ 2 (UniProtKB | ChEBI)
Binding site805Ca2+ 2 (UniProtKB | ChEBI)
Binding site864Ca2+ 2 (UniProtKB | ChEBI)
Binding site1199Ca2+ 3 (UniProtKB | ChEBI)
Binding site1216Ca2+ 3 (UniProtKB | ChEBI)
Binding site1298Ca2+ 3 (UniProtKB | ChEBI)
Binding site1300Ca2+ 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaxonal growth cone
Cellular Componentcell surface
Cellular Componentendoplasmic reticulum
Cellular ComponentGABA-ergic synapse
Cellular Componentglutamatergic synapse
Cellular Componentneuronal cell body
Cellular Componentnuclear membrane
Cellular Componentplasma membrane
Cellular Componentpresynaptic active zone membrane
Cellular Componentpresynaptic membrane
Cellular Componentprotein complex involved in cell-cell adhesion
Cellular Componentprotein-containing complex
Cellular ComponentSchaffer collateral - CA1 synapse
Cellular Componentslit diaphragm
Cellular Componentvesicle
Molecular Functionacetylcholine receptor binding
Molecular Functioncalcium channel regulator activity
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent protein binding
Molecular Functioncell adhesion molecule binding
Molecular Functionneuroligin family protein binding
Molecular Functionprotein-containing complex binding
Molecular Functiontransmembrane signaling receptor activity
Molecular Functiontype 1 fibroblast growth factor receptor binding
Biological Processadult behavior
Biological Processcalcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules
Biological Processcerebellar granule cell differentiation
Biological Processchemical synaptic transmission
Biological Processcircadian rhythm
Biological Processestablishment of protein localization
Biological Processfilopodium assembly
Biological Processgamma-aminobutyric acid receptor clustering
Biological Processgephyrin clustering involved in postsynaptic density assembly
Biological Processguanylate kinase-associated protein clustering
Biological Processheterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
Biological Processlearning
Biological Processnegative regulation of filopodium assembly
Biological Processnegative regulation of gene expression
Biological Processneuroligin clustering involved in postsynaptic membrane assembly
Biological Processneuromuscular process controlling balance
Biological Processneuron cell-cell adhesion
Biological Processneuron maturation
Biological Processneuron projection development
Biological Processneurotransmitter secretion
Biological ProcessNMDA glutamate receptor clustering
Biological Processpositive regulation of ERK1 and ERK2 cascade
Biological Processpositive regulation of excitatory postsynaptic potential
Biological Processpositive regulation of fibroblast growth factor receptor signaling pathway
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of peptidyl-serine phosphorylation
Biological Processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processpositive regulation of protein kinase A signaling
Biological Processpositive regulation of protein localization to plasma membrane
Biological Processpositive regulation of synapse assembly
Biological Processpositive regulation of synapse maturation
Biological Processpositive regulation of synaptic transmission, glutamatergic
Biological Processpostsynaptic density protein 95 clustering
Biological Processpostsynaptic membrane assembly
Biological Processprepulse inhibition
Biological Processpresynapse assembly
Biological Processpresynaptic membrane assembly
Biological Processprotein localization to synapse
Biological Processprotein-containing complex assembly involved in synapse maturation
Biological Processreceptor localization to synapse
Biological Processregulation of grooming behavior
Biological Processregulation of postsynaptic density assembly
Biological Processregulation of postsynaptic specialization assembly
Biological Processregulation of presynapse assembly
Biological Processregulation of synaptic vesicle cycle
Biological Processregulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission
Biological Processsignal transduction
Biological Processsocial behavior
Biological Processsynapse assembly
Biological Processsynaptic membrane adhesion
Biological Processsynaptic vesicle clustering
Biological Processtrans-synaptic signaling, modulating synaptic transmission
Biological Processvesicle docking involved in exocytosis
Biological Processvocal learning
Biological Processvocalization behavior

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Neurexin-1
  • Alternative names
    • Neurexin I-alpha
    • Neurexin-1-alpha

Gene names

    • Name
      Nrxn1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q63372

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain31-1454Extracellular
Transmembrane1455-1475Helical
Topological domain1476-1530Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-30
ChainPRO_000001949131-1530Neurexin-1
Glycosylation125N-linked (GlcNAc...) asparagine
Glycosylation190N-linked (GlcNAc...) asparagine
Disulfide bond228↔243
Disulfide bond245↔255
Disulfide bond460↔496
Disulfide bond666↔695
Disulfide bond703↔714
Disulfide bond708↔723
Disulfide bond725↔735
Glycosylation813N-linked (GlcNAc...) asparagine
Disulfide bond906↔914
Disulfide bond1075↔1103
Disulfide bond1110↔1121
Disulfide bond1115↔1130
Disulfide bond1132↔1142
Glycosylation1246N-linked (GlcNAc...) asparagine
Glycosylation1408O-linked (Xyl...) (heparan sulfate) serine

Post-translational modification

O-glycosylated; contains heparan sulfate. Heparan sulfate attachment is required for synapse development by mediating interactions with neuroligins and LRRTM2.

Keywords

PTM databases

Expression

Tissue specificity

Brain (neuronal synapse).

Interaction

Subunit

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 (By similarity).
Also interacts (via laminin G-like domain 2 and/or laminin G-like domain 6) with NLGN2, NLGN3 and NLGN4L; interactions with NLGN1, NLGN2, NLGN3 and NLGN4L are calcium-dependent (PubMed:18093522).
Interacts (via cytoplasmic C-terminal region) with CASK (via the PDZ, SH3 and guanylate kinase-like domains) (PubMed:12040031, PubMed:8786425).
Interacts (via cytoplasmic C-terminus) with CASKIN1 and APBA1 (PubMed:12040031).
Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3 (PubMed:9856994).
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) (PubMed:11470830).
Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 (PubMed:20064387, PubMed:20064388).
Interacts with SYT13 and SYTL1 (By similarity).
Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 (By similarity).
Interacts with CLSTN3 (By similarity).
Alpha-type isoforms interact with alpha-latrotoxin from spider venom (PubMed:10197529, PubMed:1621094).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain31-217Laminin G-like 1
Region196-219Disordered
Domain213-255EGF-like 1
Domain299-496Laminin G-like 2
Domain503-695Laminin G-like 3
Domain699-736EGF-like 2
Domain741-914Laminin G-like 4
Domain928-1103Laminin G-like 5
Domain1106-1143EGF-like 3
Domain1149-1347Laminin G-like 6
Region1412-1443Disordered
Compositional bias1497-1513Polar residues
Region1497-1523Interaction with CASK
Region1497-1530Disordered
Compositional bias1514-1530Basic and acidic residues

Sequence similarities

Belongs to the neurexin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 17 isoforms produced by Alternative promoter usage & Alternative splicing. Two isoform types, alpha-type and beta-type are produced by alternative promoter usage. In addition there are at least five alternatively spliced sites, each of which may be spliced in up to seven different ways. Combinatorial splicing at each of these five sites may lead to the generation of at least 96 isoforms but for simplicity only individual splice events or observed combinations are explicitly described below. Beta-type isoforms share the possibility of alternative splicing at sites 4 and 5. Experimental confirmation may be lacking for some isoforms.

Q63372-2

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.

  • Name
    1a
  • Synonyms
    Alpha-1A2A3A4A5A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,530
  • Mass (Da)
    167,923
  • Last updated
    2007-01-23 v3
  • Checksum
    548109BAF05119FC
MGTALVQHGGCCLLCLSLLLLGCWAELGSGLEFPGAEGQWTRFPKWNACCESEMSFQLKTRSARGLVLYFDDEGFCDFLELILTRGGRLQLSFSIFCAEPATLLADTPVNDGAWHSVRIRRQFRNTTLYIDRAEAKWVEVKSKRRDMTVFSGLFVGGLPPELRAAALKLTLASVREREPFKGWIRDVRVNSSQALPVDGSEVKLDEEPPNSGGGSPCEAGDEGDGGVCLNGGVCSVVDDQAVCDCSRTGFRGKDCSQEDNNVEGLAHLMMGDQGKSKEDNNVEGLAHLMMGDQGKEEYIATFKGSEYFCYDLSQNPIQSSSDEITLSFKTLQRNGLMLHTGKSADYVNLALKNGAVSLVINLGSGAFEALVEPVNGKFNDNAWHDVKVTRNLRQHSGIGHAMVNKLHCSVTISVDGILTTTGYTQEDYTMLGSDDFFYVGGSPSTADLPGSPVSNNFMGCLKEVVYKNNDVRLELSRLAKQGDPKMKIHGVVAFKCENVATLDPITFETPESFISLPKWNAKKTGSISFDFRTTEPNGLILFSHGKPRHQKDAKHPQMIKVDFFAIEMLDGHLYLLLDMGSGTIKIKALQKKVNDGEWYHVDFQRDGRSGTISVNTLRTPYTAPGESEILDLDDELYLGGLPENKAGLVFPTEVWTALLNYGYVGCIRDLFIDGQSKDIRQMAEIQSTAGVKPSCSRETAKPCLSNPCKNNGMCRDGWNRYVCDCSGTGYLGRSCEREATVLSYDGSMFMKIQLPVVMHTEAEDVSLRFRSQRAYGILMATTSRDSADTLRLELDAGRVKLTVNLDCIRINCNSSKGPETLFAGYNLNDNEWHTVRVVRRGKSLKLTVDDQQAMTGQMAGDHTRLEFHNIETGIITERRYLSSVPSNFIGHLQSLTFNGMAYIDLCKNGDIDYCELNARFGFRNIIADPVTFKTKSSYVALATLQAYTSMHLFFQFKTTSLDGLILYNSGDGNDFIVVELVKGYLHYVFDLGNGANLIKGSSNKPLNDNQWHNVMISRDTSNLHTVKIDTKITTQITAGARNLDLKSDLYIGGVAKETYKSLPKLVHAKEGFQGCLASVDLNGRLPDLISDALFCNGQIERGCEGPSTTCQEDSCSNQGVCLQQWDGFSCDCSMTSFSGPLCNDPGTTYIFSKGGGQITHKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRGKPPTKEPISQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRVGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSANKNKKNKDKEYYV

Q63372-1

  • Name
    2a
  • Synonyms
    Alpha-1B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-3

  • Name
    3a
  • Synonyms
    Alpha-1C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-4

  • Name
    4a
  • Synonyms
    Alpha-1D
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-5

Q63372-6

  • Name
    6a
  • Synonyms
    Alpha-1F
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-7

  • Name
    7a
  • Synonyms
    Alpha-1G
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-8

  • Name
    8a
  • Synonyms
    Alpha-2B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-9

  • Name
    9a
  • Synonyms
    Alpha-2C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-10

  • Name
    10a
  • Synonyms
    Alpha-3B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-11

  • Name
    11a
  • Synonyms
    Alpha-4B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-12

  • Name
    12a
  • Synonyms
    Alpha-5B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63372-13

  • Name
    13a
  • Synonyms
    Alpha-1B2B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q63373-1

The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

View isoform
  • Name
    1b
  • Synonyms
    Beta-4A5A
  • See also
    sequence in UniParc or sequence clusters in UniRef

Q63373-2

The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

View isoform
  • Name
    2b
  • Synonyms
    Beta-4A5B
  • See also
    sequence in UniParc or sequence clusters in UniRef

Q63373-3

The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

View isoform
  • Name
    3b
  • Synonyms
    Beta-4B5A
  • See also
    sequence in UniParc or sequence clusters in UniRef

Q63373-4

The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

View isoform
  • Name
    4b
  • Synonyms
    Beta-4B5B
  • See also
    sequence in UniParc or sequence clusters in UniRef

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6GKK5A0A8I6GKK5_RATNrxn11496
A0A8I6GKH3A0A8I6GKH3_RATNrxn11504
A0A0U1RRR4A0A0U1RRR4_RATNrxn11500
M0RBN6M0RBN6_RATNrxn11484
A0A8I6A146A0A8I6A146_RATNrxn11466
A0A8I5ZTY7A0A8I5ZTY7_RATNrxn1468
A0A8I5ZU71A0A8I5ZU71_RATNrxn1139
Q63373NRX1B_RATNrxn1468

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_003486258in isoform 3a and isoform 5a
Alternative sequenceVSP_003487258-277in isoform 7a
Alternative sequenceVSP_022559264-273in isoform 6a
Alternative sequenceVSP_003488274-277in isoform 4a and isoform 5a
Alternative sequenceVSP_022560278-293in isoform 2a and isoform 13a
Alternative sequenceVSP_003489395-409in isoform 9a
Alternative sequenceVSP_003490403-409in isoform 8a and isoform 13a
Alternative sequenceVSP_003491806-815in isoform 10a
Alternative sequenceVSP_0034921263-1292in isoform 11a
Alternative sequenceVSP_0034931426-1427in isoform 12a
Compositional bias1497-1513Polar residues
Compositional bias1514-1530Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M96374
EMBL· GenBank· DDBJ
AAA41704.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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