NRX1B_MOUSE
ID NRX1B_MOUSE Reviewed; 468 AA.
AC P0DI97;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Neurexin-1-beta {ECO:0000305};
DE AltName: Full=Neurexin I-beta;
DE Flags: Precursor;
GN Name=Nrxn1 {ECO:0000312|MGI:MGI:1096391};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP INTERACTION WITH CBLN1, AND MUTAGENESIS OF ASP-137 AND ASN-238.
RX PubMed=21410790; DOI=10.1111/j.1460-9568.2011.07638.x;
RA Matsuda K., Yuzaki M.;
RT "Cbln family proteins promote synapse formation by regulating distinct
RT neurexin signaling pathways in various brain regions.";
RL Eur. J. Neurosci. 33:1447-1461(2011).
RN [4]
RP INTERACTION WITH CBLN1; CBLN2 AND CBLN4.
RX PubMed=22220752; DOI=10.1111/j.1471-4159.2012.07648.x;
RA Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V.,
RA Deutch A.Y., Parris J., Morgan J.I.;
RT "The Cbln family of proteins interact with multiple signaling pathways.";
RL J. Neurochem. 121:717-729(2012).
RN [5]
RP ALTERNATIVE PROMOTER USAGE (ISOFORM 6), AND ALTERNATIVE SPLICING.
RX PubMed=25737549; DOI=10.1073/pnas.1502849112;
RA Yan Q., Weyn-Vanhentenryck S.M., Wu J., Sloan S.A., Zhang Y., Chen K.,
RA Wu J.Q., Barres B.A., Zhang C.;
RT "Systematic discovery of regulated and conserved alternative exons in the
RT mammalian brain reveals NMD modulating chromatin regulators.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3445-3450(2015).
RN [6]
RP INTERACTION WITH CBLN1; CBLN2 AND CBLN4.
RX PubMed=29782851; DOI=10.1016/j.brainres.2018.05.022;
RA Rong Y., Bansal P.K., Wei P., Guo H., Correia K., Parris J., Morgan J.I.;
RT "Glycosylation of Cblns attenuates their receptor binding.";
RL Brain Res. 1694:129-139(2018).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion by forming intracellular junctions
CC through binding to neuroligins. May play a role in formation or
CC maintenance of synaptic junctions. May mediate intracellular signaling.
CC May play a role in angiogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The cytoplasmic C-terminal region binds to CASK. Binds NLGN1,
CC NLGN2 and NLGN3, DAG1 (alpha-dystroglycan) and alpha-latrotoxin.
CC Binding to neuroligins is calcium-dependent, and the binding preference
CC ranks as follow: NLGN1 > NLGN4 >> NLGN3 > NLGN2 (By similarity).
CC Interacts with CBLN2 and more weakly with CBLN4 (PubMed:22220752,
CC PubMed:29782851). Interacts with CBLN1; interaction is CBLN1 hexamer
CC form-dependent; CBLN1-binding is calcium-independent; isoform 1b does
CC not interact with CBLN1 (PubMed:21410790, PubMed:22220752,
CC PubMed:29782851). {ECO:0000250|UniProtKB:Q63373,
CC ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752,
CC ECO:0000269|PubMed:29782851}.
CC -!- INTERACTION:
CC P0DI97; Q9R171: Cbln1; NbExp=4; IntAct=EBI-2794440, EBI-2794140;
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q63373}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q63373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC Comment=A number of isoforms, alpha-type and beta-type are produced
CC by alternative promoter usage. Beta-type isoforms differ from
CC alpha-type isoforms in their N-terminus.;
CC Name=1b;
CC IsoId=P0DI97-1; Sequence=Displayed;
CC Name=1a;
CC IsoId=Q9CS84-1; Sequence=External;
CC Name=2a; Synonyms=Alpha-2B;
CC IsoId=Q9CS84-2; Sequence=External;
CC Name=3a; Synonyms=Alpha-2C;
CC IsoId=Q9CS84-3; Sequence=External;
CC Name=4a;
CC IsoId=Q9CS84-4; Sequence=External;
CC Name=5a;
CC IsoId=Q9CS84-5; Sequence=External;
CC Name=6;
CC IsoId=Q9CS84-6; Sequence=External;
CC -!- PTM: Highly O-glycosylated and minor N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; CH466537; EDL38657.1; -; Genomic_DNA.
DR CCDS; CCDS84341.1; -. [P0DI97-1]
DR RefSeq; NP_001333888.1; NM_001346959.1. [P0DI97-1]
DR AlphaFoldDB; P0DI97; -.
DR SMR; P0DI97; -.
DR ComplexPortal; CPX-4083; NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex.
DR ComplexPortal; CPX-4122; NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex.
DR CORUM; P0DI97; -.
DR IntAct; P0DI97; 2.
DR STRING; 10090.ENSMUSP00000134402; -.
DR PeptideAtlas; P0DI97; -.
DR PRIDE; P0DI97; -.
DR ProteomicsDB; 293750; -. [P0DI97-1]
DR ABCD; P0DI97; 1 sequenced antibody.
DR Antibodypedia; 30173; 296 antibodies from 37 providers.
DR DNASU; 18189; -.
DR Ensembl; ENSMUST00000174337; ENSMUSP00000133724; ENSMUSG00000024109. [P0DI97-1]
DR GeneID; 18189; -.
DR KEGG; mmu:18189; -.
DR CTD; 9378; -.
DR MGI; MGI:1096391; Nrxn1.
DR VEuPathDB; HostDB:ENSMUSG00000024109; -.
DR eggNOG; KOG3514; Eukaryota.
DR GeneTree; ENSGT00940000154292; -.
DR HOGENOM; CLU_025785_1_0_1; -.
DR OrthoDB; 35129at2759; -.
DR TreeFam; TF334142; -.
DR BioGRID-ORCS; 18189; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Nrxn1; mouse.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000024109; Expressed in medial dorsal nucleus of thalamus and 178 other tissues.
DR ExpressionAtlas; P0DI97; baseline and differential.
DR Genevisible; P0DI97; MM.
DR GO; GO:0044295; C:axonal growth cone; IDA:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030139; C:endocytic vesicle; ISS:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IC:BHF-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IC:BHF-UCL.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; IC:ComplexPortal.
DR GO; GO:0098984; C:neuron to neuron synapse; IC:ComplexPortal.
DR GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0042734; C:presynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0098635; C:protein complex involved in cell-cell adhesion; IC:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0036057; C:slit diaphragm; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0033130; F:acetylcholine receptor binding; IDA:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0097109; F:neuroligin family protein binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0090125; P:cell-cell adhesion involved in synapse maturation; IC:ComplexPortal.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IGI:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IDA:BHF-UCL.
DR GO; GO:0046847; P:filopodium assembly; IMP:CACAO.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IDA:BHF-UCL.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; IDA:BHF-UCL.
DR GO; GO:0097117; P:guanylate kinase-associated protein clustering; IDA:BHF-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0099558; P:maintenance of synapse structure; IC:ComplexPortal.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; IDA:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0042551; P:neuron maturation; IDA:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IC:ComplexPortal.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IC:ComplexPortal.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IC:ComplexPortal.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IGI:MGI.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IDA:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IC:ComplexPortal.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IDA:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0099054; P:presynapse assembly; ISO:MGI.
DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0035418; P:protein localization to synapse; IDA:BHF-UCL.
DR GO; GO:0090126; P:protein-containing complex assembly involved in synapse maturation; IDA:BHF-UCL.
DR GO; GO:0097120; P:receptor localization to synapse; IDA:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IDA:BHF-UCL.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IDA:BHF-UCL.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IMP:SynGO.
DR GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR GO; GO:0060074; P:synapse maturation; IC:ComplexPortal.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:BHF-UCL.
DR GO; GO:0099542; P:trans-synaptic signaling by endocannabinoid; IMP:SynGO.
DR GO; GO:0042297; P:vocal learning; ISO:MGI.
DR GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Angiogenesis; Calcium;
KW Cell adhesion; Cell membrane; Cell projection; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..46
FT /evidence="ECO:0000255"
FT CHAIN 47..468
FT /note="Neurexin-1-beta"
FT /id="PRO_0000412630"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 87..285
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 201..230
FT /note="Essential for interaction with CBLN1; modulates
FT interaction affinity with NLGN1, NLGN2 and NLGN3; prevents
FT interaction with DAG1/alpha-dystroglycan; modulates
FT interaction with alpha-latrotoxin"
FT /evidence="ECO:0000250|UniProtKB:P58400,
FT ECO:0000250|UniProtKB:Q63373"
FT REGION 350..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT MUTAGEN 137
FT /note="D->A: Loss of NLGN1-binding. No effect on CBLN1-
FT binding."
FT /evidence="ECO:0000269|PubMed:21410790"
FT MUTAGEN 238
FT /note="N->A: Loss of NLGN1-binding. No effect on CBLN1-
FT binding."
FT /evidence="ECO:0000269|PubMed:21410790"
SQ SEQUENCE 468 AA; 50223 MW; F118A9053BAB4E21 CRC64;
MYQRMLRCGA DLGSPGGGSG GGAGGRLALI WIVPLTLSGL LGVAWGASSL GAHHIHHFHG
SSKHHSVPIA IYRSPASLRG GHAGTTYIFS KGGGQITYKW PPNDRPSTRA DRLAIGFSTV
QKEAVLVRVD SSSGLGDYLE LHIHQGKIGV KFNVGTDDIA IEESNAIIND GKYHVVRFTR
SGGNATLQVD SWPVIERYPA GNNDNERLAI ARQRIPYRLG RVVDEWLLDK GRQLTIFNSQ
ATIIIGGKEQ GQPFQGQLSG LYYNGLKVLN MAAENDANIA IVGNVRLVGE VPSSMTTEST
ATAMQSEMST SIMETTTTLA TSTARRGKPP TKEPISQTTD DILVASAECP SDDEDIDPCE
PSSGGLANPT RVGGREPYPG SAEVIRESSS TTGMVVGIVA AAALCILILL YAMYKYRNRD
EGSYHVDESR NYISNSAQSN GAVVKEKQPS SAKSANKNKK NKDKEYYV
