NRX1A_HUMAN
ID NRX1A_HUMAN Reviewed; 1477 AA.
AC Q9ULB1; A7KRL9; O60323; Q53TJ9; Q53TQ1; Q5HYI0; Q9C079; Q9C080; Q9C081;
AC Q9H3M2; Q9UDM6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Neurexin-1;
DE AltName: Full=Neurexin I-alpha;
DE AltName: Full=Neurexin-1-alpha;
DE Flags: Precursor;
GN Name=NRXN1; Synonyms=KIAA0578;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3A).
RX PubMed=18179900; DOI=10.1016/j.ajhg.2007.09.011;
RA Kim H.G., Kishikawa S., Higgins A.W., Seong I.S., Donovan D.J., Shen Y.,
RA Lally E., Weiss L.A., Najm J., Kutsche K., Descartes M., Holt L.,
RA Braddock S., Troxell R., Kaplan L., Volkmar F., Klin A., Tsatsanis K.,
RA Harris D.J., Noens I., Pauls D.L., Daly M.J., MacDonald M.E., Morton C.C.,
RA Quade B.J., Gusella J.F.;
RT "Disruption of neurexin 1 associated with autism spectrum disorder.";
RL Am. J. Hum. Genet. 82:199-207(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RC TISSUE=Brain;
RA Seki N., Yoshikawa T., Azuma T., Saito T., Muramatsu M.;
RT "Human neurexin I-alpha.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP SEQUENCE REVISION, AND ALTERNATIVE SPLICING.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Heart;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=11944992; DOI=10.1006/geno.2002.6734;
RA Rowen L., Young J., Birditt B., Kaur A., Madan A., Philipps D.L., Qin S.,
RA Minx P., Wilson R.K., Hood L., Graveley B.R.;
RT "Analysis of the human neurexin genes: alternative splicing and the
RT generation of protein diversity.";
RL Genomics 79:587-597(2002).
RN [8]
RP INVOLVEMENT IN PTHSL2.
RX PubMed=19896112; DOI=10.1016/j.ajhg.2009.10.004;
RA Zweier C., de Jong E.K., Zweier M., Orrico A., Ousager L.B., Collins A.L.,
RA Bijlsma E.K., Oortveld M.A., Ekici A.B., Reis A., Schenck A., Rauch A.;
RT "CNTNAP2 and NRXN1 are mutated in autosomal-recessive Pitt-Hopkins-like
RT mental retardation and determine the level of a common synaptic protein in
RT Drosophila.";
RL Am. J. Hum. Genet. 85:655-666(2009).
RN [9]
RP INVOLVEMENT IN SCZD17.
RX PubMed=21424692; DOI=10.1007/s00439-011-0975-z;
RA Gauthier J., Siddiqui T.J., Huashan P., Yokomaku D., Hamdan F.F.,
RA Champagne N., Lapointe M., Spiegelman D., Noreau A., Lafreniere R.G.,
RA Fathalli F., Joober R., Krebs M.O., DeLisi L.E., Mottron L., Fombonne E.,
RA Michaud J.L., Drapeau P., Carbonetto S., Craig A.M., Rouleau G.A.;
RT "Truncating mutations in NRXN2 and NRXN1 in autism spectrum disorders and
RT schizophrenia.";
RL Hum. Genet. 130:563-573(2011).
RN [10]
RP VARIANT ALA-28.
RX PubMed=22892527; DOI=10.1038/ejhg.2012.175;
RA Boccuto L., Lauri M., Sarasua S.M., Skinner C.D., Buccella D., Dwivedi A.,
RA Orteschi D., Collins J.S., Zollino M., Visconti P., Dupont B., Tiziano D.,
RA Schroer R.J., Neri G., Stevenson R.E., Gurrieri F., Schwartz C.E.;
RT "Prevalence of SHANK3 variants in patients with different subtypes of
RT autism spectrum disorders.";
RL Eur. J. Hum. Genet. 21:310-316(2013).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions,
CC exocytosis of secretory granules and regulation of signal transmission.
CC Function is isoform-specific. Alpha-type isoforms have a long N-
CC terminus with six laminin G-like domains and play an important role in
CC synaptic signal transmission. Alpha-type isoforms play a role in the
CC regulation of calcium channel activity and Ca(2+)-triggered
CC neurotransmitter release at synapses and at neuromuscular junctions.
CC They play an important role in Ca(2+)-triggered exocytosis of secretory
CC granules in pituitary gland. They may affect their functions at
CC synapses and in endocrine cells via their interactions with proteins
CC from the exocytotic machinery. Likewise, alpha-type isoforms play a
CC role in regulating the activity of postsynaptic NMDA receptors, a
CC subtype of glutamate-gated ion channels. Both alpha-type and beta-type
CC isoforms may play a role in the formation or maintenance of synaptic
CC junctions via their calcium-dependent interactions (via the
CC extracellular domains) with neuroligin family members, CBLN1 or CBLN2.
CC In vitro, triggers the de novo formation of presynaptic structures. May
CC be involved in specification of excitatory synapses. Alpha-type
CC isoforms were first identified as receptors for alpha-latrotoxin from
CC spider venom (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via laminin G-like domain 2 and/or laminin G-like
CC domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer
CC interacts with one NRXN1 dimer (By similarity). Interacts (via
CC cytoplasmic C-terminal region) with CASK (via the PDZ, SH3 and
CC guanylate kinase-like domains) (By similarity). Interacts (via
CC cytoplasmic C-terminus) with CASKIN1 and APBA1 (By similarity).
CC Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6)
CC with NLGN1, NLGN2, NLGN3, NLGN4X and NLGN4Y; these interactions are
CC calcium-dependent. Interacts (via laminin G-like domain 2) with NXPH1
CC and NXPH3. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 (By
CC similarity). Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 (By
CC similarity). Alpha-type isoforms (neurexin-1-alpha) interact (via
CC laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via
CC alpha-dystroglycan chain). Alpha-type isoforms interact with alpha-
CC latrotoxin from spider venom. Interacts with SYT13 and SYTL1 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q28146,
CC ECO:0000250|UniProtKB:Q63372}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC Comment=A number of isoforms are produced by alternative promoter
CC usage including the alpha-type and beta-type isoforms which differ in
CC their N-terminus. Additional isoforms may be produced by alternative
CC splicing. {ECO:0000269|PubMed:11944992, ECO:0000269|PubMed:12168954};
CC Name=1a;
CC IsoId=Q9ULB1-1; Sequence=Displayed;
CC Name=2a;
CC IsoId=Q9ULB1-2; Sequence=VSP_014541, VSP_041355, VSP_058202;
CC Name=3a;
CC IsoId=Q9ULB1-3; Sequence=VSP_041353, VSP_041354, VSP_041355;
CC Name=3b;
CC IsoId=P58400-1; Sequence=External;
CC Name=4;
CC IsoId=Q9ULB1-4; Sequence=VSP_058200, VSP_058201, VSP_058202;
CC Name=1b;
CC IsoId=P58400-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:9628581}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Pitt-Hopkins-like syndrome 2 (PTHSL2) [MIM:614325]: A syndrome
CC characterized by severe intellectual disability and variable additional
CC symptoms, such as impaired speech development, autistic behavior,
CC breathing anomalies and a broad mouth, resembling Pitt-Hopkins
CC syndrome. Other features include decreased reflexes in the upper
CC extremities, constipation, strabismus, and protruding tongue with
CC drooling. In contrast to patients with Pitt-Hopkins syndrome, PTHSL2
CC patients present with normal or only mildly to moderately delayed motor
CC milestones. {ECO:0000269|PubMed:19896112}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Schizophrenia 17 (SCZD17) [MIM:614332]: A complex,
CC multifactorial psychotic disorder or group of disorders characterized
CC by disturbances in the form and content of thought (e.g. delusions,
CC hallucinations), in mood (e.g. inappropriate affect), in sense of self
CC and relationship to the external world (e.g. loss of ego boundaries,
CC withdrawal), and in behavior (e.g bizarre or apparently purposeless
CC behavior). Although it affects emotions, it is distinguished from mood
CC disorders in which such disturbances are primary. Similarly, there may
CC be mild impairment of cognitive function, and it is distinguished from
CC the dementias in which disturbed cognitive function is considered
CC primary. Some patients manifest schizophrenic as well as bipolar
CC disorder symptoms and are often given the diagnosis of schizoaffective
CC disorder. {ECO:0000269|PubMed:21424692}. Note=Disease susceptibility
CC may be associated with variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2a]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3a]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25504.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EF539882; ABS86974.1; -; mRNA.
DR EMBL; AB035356; BAA87821.1; -; mRNA.
DR EMBL; AB011150; BAA25504.2; ALT_INIT; mRNA.
DR EMBL; BX647616; CAI46085.1; -; mRNA.
DR EMBL; AC007462; AAF03536.1; -; Genomic_DNA.
DR EMBL; AC007682; AAY14894.1; -; Genomic_DNA.
DR EMBL; AC009234; AAY14944.1; -; Genomic_DNA.
DR EMBL; AC068725; AAG59602.1; -; Genomic_DNA.
DR EMBL; AC069550; AAG38120.1; -; Genomic_DNA.
DR EMBL; AC078994; AAK06387.1; -; Genomic_DNA.
DR EMBL; AC068715; AAG59642.1; -; Genomic_DNA.
DR CCDS; CCDS46282.1; -. [Q9ULB1-3]
DR CCDS; CCDS54360.1; -. [Q9ULB1-1]
DR CCDS; CCDS82445.1; -. [Q9ULB1-4]
DR CCDS; CCDS82450.1; -. [Q9ULB1-2]
DR RefSeq; NP_001129131.1; NM_001135659.2. [Q9ULB1-3]
DR RefSeq; NP_001317011.1; NM_001330082.1. [Q9ULB1-2]
DR RefSeq; NP_004792.1; NM_004801.5. [Q9ULB1-1]
DR PDB; 6NID; X-ray; 1.86 A; D/E/F=1468-1477.
DR PDBsum; 6NID; -.
DR AlphaFoldDB; Q9ULB1; -.
DR SASBDB; Q9ULB1; -.
DR SMR; Q9ULB1; -.
DR BioGRID; 114779; 16.
DR CORUM; Q9ULB1; -.
DR IntAct; Q9ULB1; 6.
DR STRING; 9606.ENSP00000385142; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR TCDB; 8.A.74.1.2; the tm9 or phg1 targeting receptor (ppg1) family.
DR GlyConnect; 1548; 1 N-Linked glycan (1 site).
DR GlyGen; Q9ULB1; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9ULB1; -.
DR PhosphoSitePlus; Q9ULB1; -.
DR SwissPalm; Q9ULB1; -.
DR BioMuta; NRXN1; -.
DR DMDM; 17369704; -.
DR EPD; Q9ULB1; -.
DR MassIVE; Q9ULB1; -.
DR MaxQB; Q9ULB1; -.
DR PaxDb; Q9ULB1; -.
DR PeptideAtlas; Q9ULB1; -.
DR PRIDE; Q9ULB1; -.
DR ProteomicsDB; 84967; -. [Q9ULB1-1]
DR ProteomicsDB; 84968; -. [Q9ULB1-2]
DR ProteomicsDB; 84969; -. [Q9ULB1-3]
DR Antibodypedia; 30173; 296 antibodies from 37 providers.
DR DNASU; 9378; -.
DR Ensembl; ENST00000404971.5; ENSP00000385142.1; ENSG00000179915.25. [Q9ULB1-3]
DR Ensembl; ENST00000406316.6; ENSP00000384311.2; ENSG00000179915.25. [Q9ULB1-1]
DR Ensembl; ENST00000625672.2; ENSP00000485887.1; ENSG00000179915.25. [Q9ULB1-2]
DR GeneID; 9378; -.
DR UCSC; uc061jbb.1; human. [Q9ULB1-1]
DR CTD; 9378; -.
DR DisGeNET; 9378; -.
DR GeneCards; NRXN1; -.
DR HGNC; HGNC:8008; NRXN1.
DR HPA; ENSG00000179915; Tissue enriched (brain).
DR MalaCards; NRXN1; -.
DR MIM; 600565; gene.
DR MIM; 614325; phenotype.
DR MIM; 614332; phenotype.
DR neXtProt; NX_Q9ULB1; -.
DR OpenTargets; ENSG00000179915; -.
DR Orphanet; 106; NON RARE IN EUROPE: Autism.
DR Orphanet; 600663; NRXN1-related severe neurodevelopmental disorder-motor stereotypies-chronic constipation-sleep-wake cycle disturbance.
DR PharmGKB; PA31786; -.
DR VEuPathDB; HostDB:ENSG00000179915; -.
DR eggNOG; KOG3514; Eukaryota.
DR GeneTree; ENSGT00940000154292; -.
DR HOGENOM; CLU_001710_0_1_1; -.
DR InParanoid; Q9ULB1; -.
DR OMA; PYDVYVA; -.
DR OrthoDB; 35129at2759; -.
DR PhylomeDB; Q9ULB1; -.
DR TreeFam; TF321302; -.
DR PathwayCommons; Q9ULB1; -.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q9ULB1; -.
DR SIGNOR; Q9ULB1; -.
DR BioGRID-ORCS; 9378; 10 hits in 1062 CRISPR screens.
DR ChiTaRS; NRXN1; human.
DR GenomeRNAi; 9378; -.
DR Pharos; Q9ULB1; Tbio.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9ULB1; protein.
DR Bgee; ENSG00000179915; Expressed in sural nerve and 162 other tissues.
DR ExpressionAtlas; Q9ULB1; baseline and differential.
DR Genevisible; Q9ULB1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; ISS:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0031982; C:vesicle; ISS:BHF-UCL.
DR GO; GO:0033130; F:acetylcholine receptor binding; ISS:BHF-UCL.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR GO; GO:0097109; F:neuroligin family protein binding; ISS:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; TAS:BHF-UCL.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:BHF-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISS:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0042297; P:vocal learning; IMP:BHF-UCL.
DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR CDD; cd00110; LamG; 6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing; Calcium;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW EGF-like domain; Glycoprotein; Intellectual disability; Membrane;
KW Metal-binding; Reference proteome; Repeat; Schizophrenia; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..1477
FT /note="Neurexin-1"
FT /id="PRO_0000019490"
FT TOPO_DOM 31..1401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1402..1422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1423..1477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..217
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 213..256
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 283..473
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 480..672
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 676..713
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 718..891
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 905..1080
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1083..1120
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1126..1294
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 198..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1470
FT /note="Interaction with CASK"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT COMPBIAS 1444..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 765
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 782
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 841
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..243
FT /evidence="ECO:0000250"
FT DISULFID 245..255
FT /evidence="ECO:0000250"
FT DISULFID 437..473
FT /evidence="ECO:0000250"
FT DISULFID 643..672
FT /evidence="ECO:0000250"
FT DISULFID 680..691
FT /evidence="ECO:0000250"
FT DISULFID 685..700
FT /evidence="ECO:0000250"
FT DISULFID 702..712
FT /evidence="ECO:0000250"
FT DISULFID 1052..1080
FT /evidence="ECO:0000250"
FT DISULFID 1087..1098
FT /evidence="ECO:0000250"
FT DISULFID 1092..1107
FT /evidence="ECO:0000250"
FT DISULFID 1109..1119
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1335
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_058200"
FT VAR_SEQ 258
FT /note="E -> EIKFGLQCVLPVLLHDNDQGKYCCINTAKPLTEK (in isoform
FT 3a)"
FT /evidence="ECO:0000303|PubMed:18179900"
FT /id="VSP_041353"
FT VAR_SEQ 379..386
FT /note="Missing (in isoform 2a)"
FT /evidence="ECO:0000303|PubMed:9628581"
FT /id="VSP_014541"
FT VAR_SEQ 386
FT /note="M -> MVNKLHCS (in isoform 3a)"
FT /evidence="ECO:0000303|PubMed:18179900"
FT /id="VSP_041354"
FT VAR_SEQ 1239
FT /note="A -> AGNNDNERLAIARQRIPYRLGRVVDEWLLDK (in isoform 3a
FT and isoform 2a)"
FT /evidence="ECO:0000303|PubMed:18179900,
FT ECO:0000303|PubMed:9628581"
FT /id="VSP_041355"
FT VAR_SEQ 1336..1344
FT /note="GKPPTKEPI -> MDMRWHCEN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_058201"
FT VAR_SEQ 1373..1375
FT /note="Missing (in isoform 4 and isoform 2a)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:9628581"
FT /id="VSP_058202"
FT VARIANT 28
FT /note="G -> A (in dbSNP:rs199598542)"
FT /evidence="ECO:0000269|PubMed:22892527"
FT /id="VAR_070274"
FT VARIANT 400
FT /note="Y -> N (in dbSNP:rs17040901)"
FT /id="VAR_050265"
FT CONFLICT 1360
FT /note="S -> G (in Ref. 5; CAI46085)"
FT /evidence="ECO:0000305"
FT STRAND 1475..1477
FT /evidence="ECO:0007829|PDB:6NID"
SQ SEQUENCE 1477 AA; 161883 MW; FF845FB428B1A683 CRC64;
MGTALLQRGG CFLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR
RQFRNTTLFI DQVEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
KGWIRDVRVN SSQVLPVDSG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP
IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG
KFNDNAWHDV KVTRNLRQHS GIGHAMVTIS VDGILTTTGY TQEDYTMLGS DDFFYVGGSP
STADLPGSPV SNNFMGCLKE VVYKNNDVRL ELSRLAKQGD PKMKIHGVVA FKCENVATLD
PITFETPESF ISLPKWNAKK TGSISFDFRT TEPNGLILFS HGKPRHQKDA KHPQMIKVDF
FAIEMLDGHL YLLLDMGSGT IKIKALLKKV NDGEWYHVDF QRDGRSGTIS VNTLRTPYTA
PGESEILDLD DELYLGGLPE NKAGLVFPTE VWTALLNYGY VGCIRDLFID GQSKDIRQMA
EVQSTAGVKP SCSKETAKPC LSNPCKNNGM CRDGWNRYVC DCSGTGYLGR SCEREATVLS
YDGSMFMKIQ LPVVMHTEAE DVSLRFRSQR AYGILMATTS RDSADTLRLE LDAGRVKLTV
NLDCIRINCN SSKGPETLFA GYNLNDNEWH TVRVVRRGKS LKLTVDDQQA MTGQMAGDHT
RLEFHNIETG IITERRYLSS VPSNFIGHLQ SLTFNGMAYI DLCKNGDIDY CELNARFGFR
NIIADPVTFK TKSSYVALAT LQAYTSMHLF FQFKTTSLDG LILYNSGDGN DFIVVELVKG
YLHYVFDLGN GANLIKGSSN KPLNDNQWHN VMISRDTSNL HTVKIDTKIT TQITAGARNL
DLKSDLYIGG VAKETYKSLP KLVHAKEGFQ GCLASVDLNG RLPDLISDAL FCNGQIERGC
EGPSTTCQED SCSNQGVCLQ QWDGFSCDCS MTSFSGPLCN DPGTTYIFSK GGGQITYKWP
PNDRPSTRAD RLAIGFSTVQ KEAVLVRVDS SSGLGDYLEL HIHQGKIGVK FNVGTDDIAI
EESNAIINDG KYHVVRFTRS GGNATLQVDS WPVIERYPAG RQLTIFNSQA TIIIGGKEQG
QPFQGQLSGL YYNGLKVLNM AAENDANIAI VGNVRLVGEV PSSMTTESTA TAMQSEMSTS
IMETTTTLAT STARRGKPPT KEPISQTTDD ILVASAECPS DDEDIDPCEP SSGGLANPTR
AGGREPYPGS AEVIRESSST TGMVVGIVAA AALCILILLY AMYKYRNRDE GSYHVDESRN
YISNSAQSNG AVVKEKQPSS AKSSNKNKKN KDKEYYV
