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NRXN2 Membrane Protein Introduction

Introduction of NRXN2

NRXN2, encoded by the NRXN2 gene, belongs to the neurexin family. The proteins of the neurexin family act as receptors and cell adhesion molecules in the vertebrate nervous system. NRXN2 is predominantly expressed in brain. There are three isoforms of NRXN2 (isoform 1a, isoform 1b, isoform 2a) have been found, which are produced by alternative splicing and alternative promoter usage. Isoform 1a is chosen as the 'canonical' sequence.

Basic Information of NRXN2
Protein Name Neurexin-2
Gene Name NRXN2
Aliases Neurexin II-alpha, Neurexin-2-alpha
Organism Homo sapiens (Human)
UniProt ID Q9P2S2
Transmembrane Times 1
Length (aa) 1712
Sequence MASGSRWRPTPPPLLLLLLLALAARADGLEFGGGPGQWARYARWAGAASSGELSFSLRTNATRALLLYLDDGGDCDFLELLLVDGRLRLRFTLSCAEPATLQLDTPVADDRWHMVLLTRDARRTALAVDGEARAAEVRSKRREMQVASDLFVGGIPPDVRLSALTLSTVKYEPPFRGLLANLKLGERPPALLGSQGLRGATADPLCAPARNPCANGGLCTVLAPGEVGCDCSHTGFGGKFCSEEEHPMEGPAHLTLNSEVGSLLFSEGGAGRGGAGDVHQPTKGKEEFVATFKGNEFFCYDLSHNPIQSSTDEITLAFRTLQRNGLMLHTGKSADYVNLSLKSGAVWLVINLGSGAFEALVEPVNGKFNDNAWHDVRVTRNLRQHAGIGHAMVNKLHYLVTISVDGILTTTGYTQEDYTMLGSDDFFYIGGSPNTADLPGSPVSNNFMGCLKDVVYKNNDFKLELSRLAKEGDPKMKLQGDLSFRCEDVAALDPVTFESPEAFVALPRWSAKRTGSISLDFRTTEPNGLLLFSQGRRAGGGAGSHSSAQRADYFAMELLDGHLYLLLDMGSGGIKLRASSRKVNDGEWCHVDFQRDGRKGSISVNSRSTPFLATGDSEILDLESELYLGGLPEGGRVDLPLPPEVWTAALRAGYVGCVRDLFIDGRSRDLRGLAEAQGAVGVAPFCSRETLKQCASAPCRNGGVCREGWNRFICDCIGTGFLGRVCEREATVLSYDGSMYMKIMLPNAMHTEAEDVSLRFMSQRAYGLMMATTSRESADTLRLELDGGQMKLTVNLDCLRVGCAPSKGPETLFAGHKLNDNEWHTVRVVRRGKSLQLSVDNVTVEGQMAGAHMRLEFHNIETGIMTERRFISVVPSNFIGHLSGLVFNGQPYMDQCKDGDITYCELNARFGLRAIVADPVTFKSRSSYLALATLQAYASMHLFFQFKTTAPDGLLLFNSGNGNDFIVIELVKGYIHYVFDLGNGPSLMKGNSDKPVNDNQWHNVVVSRDPGNVHTLKIDSRTVTQHSNGARNLDLKGELYIGGLSKNMFSNLPKLVASRDGFQGCLASVDLNGRLPDLIADALHRIGQVERGCDGPSTTCTEESCANQGVCLQQWDGFTCDCTMTSYGGPVCNDPGTTYIFGKGGALITYTWPPNDRPSTRMDRLAVGFSTHQRSAVLVRVDSASGLGDYLQLHIDQGTVGVIFNVGTDDITIDEPNAIVSDGKYHVVRFTRSGGNATLQVDSWPVNERYPAGNFDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQAAIKIGGRDQGRPFQGQVSGLYYNGLKVLALAAESDPNVRTEGHLRLVGEGPSVLLSAETTATTLLADMATTIMETTTTMATTTTRRGRSPTLRDSTTQNTDDLLVASAECPSDDEDLEECEPSTGGELILPIITEDSLDPPPVATRSPFVPPPPTFYPFLTGVGATQDTLPPPAARRPPSGGPCQAERDDSDCEEPIEASGFASGEVFDSSLPPTDDEDFYTTFPLVTDRTTLLSPRKPAPRPNLRTDGATGAPGVLFAPSAPAPNLPAGKMNHRDPLQPLLENPPLGPGAPTSFEPRRPPPLRPGVTSAPGFPHLPTANPTGPGERGPPGAVEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV

Function of NRXN2 Membrane Protein

NRXN2 utilize two alternate promoters (α and β) and numerous alternatively spliced exons to produce extensive alternative splicing, resulting in distinct mRNA transcripts and protein isoforms (α- and β-neurexin isoforms). The α-neurexins possess laminin G domains and epidermal growth factor-like (EGF-like) sequences and is proved able to interact with neurexophilins. NRXN2 is shown to possess two principal functions in brain cells, cell recognition, and cell adhesion. And NRXN2 may also play a role in regulating intracellular signaling. NRXN2 has three calcium binding sites (335, 352, 420), which are associated with the normal activity of NRXN2. There is no experimental structure of NRXN2 available so far.

Predicted structure of NRXN2. Fig.1 Predicted structure of NRXN2. (Bienert, 2017)

Application of NRXN2 Membrane Protein in Literature

  1. Born G., et al. Genetic targeting of NRXN2 in mice unveils role in excitatory cortical synapse function and social behaviors. Hum Genet. 2011, 130(4): 563-73. PubMed ID: 21424692

    This article validates that mice without Nrxn2α gene show abnormalities of behavior identified by increased anxiety-like behavior and social interaction deficits, which partially differ from behaviors of Nrxn1α mutant, partially overlap.

  2. Gauthier J., et al. Truncating mutations in NRXN2 and NRXN1 in autism spectrum disorders and schizophrenia. Hum Genet. 2011, 130(4): 563-73. PubMed ID: 21424692

    This article firstly finds that NRXN2 disruption is associated with the pathogenesis of autism spectrum disorders, and further confirms the role of NRXN1 in SCZ, suggesting that these disorders are caused by the genetic mechanism.

  3. See K., et al. SMN deficiency alters Nrxn2 expression and splicing in zebrafish and mouse models of spinal muscular atrophy. Hum Mol Genet. 2014, 23(7): 1754-70. PubMed ID: 24218366

    This article proposes that deficiency of survival motor neuron can affect abundance and splicing of nrxn2a. It explains the pre-synaptic defects at neuromuscular endplates in spinal muscular atrophy pathophysiology.

  4. Tserel L., et al. CpG sites associated with NRP1, NRXN2 and miR-29b-2 are hypomethylated in monocytes during aging. Immun Ageing. 2014, 11(1):1. PubMed ID: 24405718

    This article identifies evident age-related hypomethylation at CpG sites within the regions of miR-29b-2, NRXN2 and NRP1 genes in human purified monocytes.

  5. Dachtler J., et al. Deletion of α-neurexin II results in autism-related behaviors in mice. Transl Psychiatry. 2014, 4: e484. PubMed ID: 25423136

    This article demonstrates a causal role for the lack of Nrxn2α in the genesis of autism-related behaviors in mice.

NRXN2 Preparation Options

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Reference

  1. Bienert S. (2017). The SWISS-MODEL Repository - new features and functionality. Nucleic Acids Res. 45: D313-D319.

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