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Neurexin-1 (Neurexin I-alpha) (Neurexin-1-alpha)

 NRX1A_HUMAN             Reviewed;        1477 AA.
Q9ULB1; A7KRL9; O60323; Q53TJ9; Q53TQ1; Q5HYI0; Q9C079; Q9C080;
Q9C081; Q9H3M2; Q9UDM6;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 184.
RecName: Full=Neurexin-1;
AltName: Full=Neurexin I-alpha;
AltName: Full=Neurexin-1-alpha;
Flags: Precursor;
Name=NRXN1; Synonyms=KIAA0578;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3A).
PubMed=18179900; DOI=10.1016/j.ajhg.2007.09.011;
Kim H.G., Kishikawa S., Higgins A.W., Seong I.S., Donovan D.J.,
Shen Y., Lally E., Weiss L.A., Najm J., Kutsche K., Descartes M.,
Holt L., Braddock S., Troxell R., Kaplan L., Volkmar F., Klin A.,
Tsatsanis K., Harris D.J., Noens I., Pauls D.L., Daly M.J.,
MacDonald M.E., Morton C.C., Quade B.J., Gusella J.F.;
"Disruption of neurexin 1 associated with autism spectrum disorder.";
Am. J. Hum. Genet. 82:199-207(2008).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
TISSUE=Brain;
Seki N., Yoshikawa T., Azuma T., Saito T., Muramatsu M.;
"Human neurexin I-alpha.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[4]
SEQUENCE REVISION, AND ALTERNATIVE SPLICING.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Heart;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
ALTERNATIVE SPLICING.
PubMed=11944992; DOI=10.1006/geno.2002.6734;
Rowen L., Young J., Birditt B., Kaur A., Madan A., Philipps D.L.,
Qin S., Minx P., Wilson R.K., Hood L., Graveley B.R.;
"Analysis of the human neurexin genes: alternative splicing and the
generation of protein diversity.";
Genomics 79:587-597(2002).
[8]
INVOLVEMENT IN PTHSL2.
PubMed=19896112; DOI=10.1016/j.ajhg.2009.10.004;
Zweier C., de Jong E.K., Zweier M., Orrico A., Ousager L.B.,
Collins A.L., Bijlsma E.K., Oortveld M.A., Ekici A.B., Reis A.,
Schenck A., Rauch A.;
"CNTNAP2 and NRXN1 are mutated in autosomal-recessive Pitt-Hopkins-
like mental retardation and determine the level of a common synaptic
protein in Drosophila.";
Am. J. Hum. Genet. 85:655-666(2009).
[9]
VARIANT ALA-28.
PubMed=22892527; DOI=10.1038/ejhg.2012.175;
Boccuto L., Lauri M., Sarasua S.M., Skinner C.D., Buccella D.,
Dwivedi A., Orteschi D., Collins J.S., Zollino M., Visconti P.,
Dupont B., Tiziano D., Schroer R.J., Neri G., Stevenson R.E.,
Gurrieri F., Schwartz C.E.;
"Prevalence of SHANK3 variants in patients with different subtypes of
autism spectrum disorders.";
Eur. J. Hum. Genet. 21:310-316(2013).
-!- FUNCTION: Cell surface protein involved in cell-cell-interactions,
exocytosis 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. Both alpha-type and beta-type
isoforms may play a role in the formation or maintenance of
synaptic junctions via their calcium-dependent 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-latrotoxin from spider venom (By similarity).
{ECO:0000250}.
-!- 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. Interacts (via laminin
G-like domain 2 and/or laminin G-like domain 6) with NLGN1, NLGN2,
NLGN3, NLGN4X and NLGN4Y; these interactions are calcium-
dependent. Interacts (via laminin G-like domain 2) with NXPH1 and
NXPH3. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4
(By similarity). Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4
(By similarity). 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). Alpha-type isoforms interact
with alpha-latrotoxin from spider venom. The cytoplasmic C-
terminal region binds to CASK, CASKIN1 and APBA1. Interacts with
SYT13 and SYTL1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}. Cell junction, synapse
{ECO:0000305}. Note=Localized on the pre-synaptic membrane.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
Comment=A number of isoforms are produced by alternative
promoter usage including the alpha-type and beta-type isoforms
which differ in their N-terminus. Additional isoforms may be
produced by alternative splicing. {ECO:0000269|PubMed:11944992,
ECO:0000269|PubMed:12168954};
Name=1a;
IsoId=Q9ULB1-1; Sequence=Displayed;
Name=2a;
IsoId=Q9ULB1-2; Sequence=VSP_014541, VSP_041355, VSP_058202;
Note=Produced by alternative splicing. No experimental
confirmation available.;
Name=3a;
IsoId=Q9ULB1-3; Sequence=VSP_041353, VSP_041354, VSP_041355;
Note=Produced by alternative splicing.;
Name=3b;
IsoId=P58400-1; Sequence=External;
Name=4;
IsoId=Q9ULB1-4; Sequence=VSP_058200, VSP_058201, VSP_058202;
Note=Produced by alternative promoter usage and alternative
splicing. {ECO:0000305};
Name=1b;
IsoId=P58400-2; Sequence=External;
-!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:9628581}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- DISEASE: Pitt-Hopkins-like syndrome 2 (PTHSL2) [MIM:614325]: A
syndrome characterized by severe mental retardation and variable
additional symptoms, such as impaired speech development, autistic
behavior, breathing anomalies and a broad mouth, resembling Pitt-
Hopkins syndrome. Other features include decreased reflexes in the
upper extremities, constipation, strabismus, and protruding tongue
with drooling. In contrast to patients with Pitt-Hopkins syndrome,
PTHSL2 patients present with normal or only mildly to moderately
delayed motor milestones. {ECO:0000269|PubMed:19896112}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA25504.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; EF539882; ABS86974.1; -; mRNA.
EMBL; AB035356; BAA87821.1; -; mRNA.
EMBL; AB011150; BAA25504.2; ALT_INIT; mRNA.
EMBL; BX647616; CAI46085.1; -; mRNA.
EMBL; AC007462; AAF03536.1; -; Genomic_DNA.
EMBL; AC007682; AAY14894.1; -; Genomic_DNA.
EMBL; AC009234; AAY14944.1; -; Genomic_DNA.
EMBL; AC068725; AAG59602.1; -; Genomic_DNA.
EMBL; AC069550; AAG38120.1; -; Genomic_DNA.
EMBL; AC078994; AAK06387.1; -; Genomic_DNA.
EMBL; AC068715; AAG59642.1; -; Genomic_DNA.
CCDS; CCDS46282.1; -. [Q9ULB1-3]
CCDS; CCDS54360.1; -. [Q9ULB1-1]
CCDS; CCDS82445.1; -. [Q9ULB1-4]
CCDS; CCDS82450.1; -. [Q9ULB1-2]
RefSeq; NP_001129131.1; NM_001135659.2. [Q9ULB1-3]
RefSeq; NP_004792.1; NM_004801.5. [Q9ULB1-1]
UniGene; Hs.637685; -.
ProteinModelPortal; Q9ULB1; -.
SMR; Q9ULB1; -.
BioGrid; 114779; 15.
IntAct; Q9ULB1; 5.
STRING; 9606.ENSP00000385142; -.
TCDB; 8.A.74.1.2; the tm9 or phg1 targeting receptor (ppg1) family.
iPTMnet; Q9ULB1; -.
PhosphoSitePlus; Q9ULB1; -.
SwissPalm; Q9ULB1; -.
BioMuta; TTN; -.
DMDM; 17369704; -.
MaxQB; Q9ULB1; -.
PaxDb; Q9ULB1; -.
PeptideAtlas; Q9ULB1; -.
PRIDE; Q9ULB1; -.
ProteomicsDB; 84967; -.
ProteomicsDB; 84968; -. [Q9ULB1-2]
ProteomicsDB; 84969; -. [Q9ULB1-3]
Ensembl; ENST00000404971; ENSP00000385142; ENSG00000179915. [Q9ULB1-3]
Ensembl; ENST00000406316; ENSP00000384311; ENSG00000179915. [Q9ULB1-1]
Ensembl; ENST00000625672; ENSP00000485887; ENSG00000179915. [Q9ULB1-2]
GeneID; 9378; -.
UCSC; uc061jbb.1; human. [Q9ULB1-1]
CTD; 9378; -.
DisGeNET; 9378; -.
EuPathDB; HostDB:ENSG00000179915.21; -.
GeneCards; NRXN1; -.
HGNC; HGNC:8008; NRXN1.
HPA; HPA071400; -.
MalaCards; NRXN1; -.
MIM; 600565; gene.
MIM; 614325; phenotype.
neXtProt; NX_Q9ULB1; -.
OpenTargets; ENSG00000179915; -.
PharmGKB; PA31786; -.
eggNOG; KOG3514; Eukaryota.
eggNOG; ENOG410XNU6; LUCA.
GeneTree; ENSGT00760000118991; -.
HOVERGEN; HBG052670; -.
InParanoid; Q9ULB1; -.
OMA; GVAKEMY; -.
OrthoDB; EOG091G00KC; -.
PhylomeDB; Q9ULB1; -.
TreeFam; TF321302; -.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-6794361; Neurexins and neuroligins.
SIGNOR; Q9ULB1; -.
ChiTaRS; NRXN1; human.
GenomeRNAi; 9378; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000179915; Expressed in 176 organ(s), highest expression level in corpus callosum.
CleanEx; HS_NRXN1; -.
ExpressionAtlas; Q9ULB1; baseline and differential.
Genevisible; Q9ULB1; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
GO; GO:0031965; C:nuclear membrane; ISS:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0031982; C:vesicle; ISS:BHF-UCL.
GO; GO:0033130; F:acetylcholine receptor binding; ISS:BHF-UCL.
GO; GO:0005246; F:calcium channel regulator activity; ISS:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:BHF-UCL.
GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
GO; GO:0097109; F:neuroligin family protein binding; ISS:BHF-UCL.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:ProtInc.
GO; GO:0007268; P:chemical synaptic transmission; ISS:BHF-UCL.
GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
GO; GO:0007612; P:learning; IMP:BHF-UCL.
GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISS:BHF-UCL.
GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
GO; GO:0007158; P:neuron cell-cell adhesion; TAS:BHF-UCL.
GO; GO:0007269; P:neurotransmitter secretion; ISS:BHF-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL.
GO; GO:0090129; P:positive regulation of synapse maturation; ISS:BHF-UCL.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISS:BHF-UCL.
GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
GO; GO:2000821; P:regulation of grooming behavior; IEA:Ensembl.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
GO; GO:0042297; P:vocal learning; IMP:BHF-UCL.
GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR001791; Laminin_G.
InterPro; IPR037440; Neurexin.
InterPro; IPR003585; Neurexin-like.
InterPro; IPR027789; Syndecan/Neurexin_dom.
PANTHER; PTHR44287; PTHR44287; 2.
Pfam; PF00008; EGF; 1.
Pfam; PF02210; Laminin_G_2; 6.
Pfam; PF01034; Syndecan; 1.
SMART; SM00294; 4.1m; 1.
SMART; SM00181; EGF; 3.
SMART; SM00282; LamG; 6.
SUPFAM; SSF49899; SSF49899; 6.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS50026; EGF_3; 3.
PROSITE; PS50025; LAM_G_DOMAIN; 6.
2: Evidence at transcript level;
Alternative promoter usage; Alternative splicing; Calcium;
Cell adhesion; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
Mental retardation; Metal-binding; Polymorphism; Reference proteome;
Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000250}.
CHAIN 31 1477 Neurexin-1.
/FTId=PRO_0000019490.
TOPO_DOM 31 1401 Extracellular. {ECO:0000255}.
TRANSMEM 1402 1422 Helical. {ECO:0000255}.
TOPO_DOM 1423 1477 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 217 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 213 256 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 283 473 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 480 672 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 676 713 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 718 891 Laminin G-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 905 1080 Laminin G-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1083 1120 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1126 1294 Laminin G-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
COMPBIAS 1324 1327 Poly-Thr.
COMPBIAS 1409 1412 Poly-Ala.
METAL 329 329 Calcium. {ECO:0000250}.
METAL 329 329 Calcium 1. {ECO:0000250}.
METAL 346 346 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 407 407 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 765 765 Calcium 2. {ECO:0000250}.
METAL 782 782 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 841 841 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 1176 1176 Calcium 3. {ECO:0000250}.
METAL 1193 1193 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 1245 1245 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 1247 1247 Calcium 3. {ECO:0000250}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 790 790 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1223 1223 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 228 243 {ECO:0000250}.
DISULFID 245 255 {ECO:0000250}.
DISULFID 437 473 {ECO:0000250}.
DISULFID 643 672 {ECO:0000250}.
DISULFID 680 691 {ECO:0000250}.
DISULFID 685 700 {ECO:0000250}.
DISULFID 702 712 {ECO:0000250}.
DISULFID 1052 1080 {ECO:0000250}.
DISULFID 1087 1098 {ECO:0000250}.
DISULFID 1092 1107 {ECO:0000250}.
DISULFID 1109 1119 {ECO:0000250}.
VAR_SEQ 1 1335 Missing (in isoform 4).
{ECO:0000303|PubMed:11230166}.
/FTId=VSP_058200.
VAR_SEQ 258 258 E -> EIKFGLQCVLPVLLHDNDQGKYCCINTAKPLTEK
(in isoform 3a).
{ECO:0000303|PubMed:18179900}.
/FTId=VSP_041353.
VAR_SEQ 379 386 Missing (in isoform 2a).
{ECO:0000303|PubMed:9628581}.
/FTId=VSP_014541.
VAR_SEQ 386 386 M -> MVNKLHCS (in isoform 3a).
{ECO:0000303|PubMed:18179900}.
/FTId=VSP_041354.
VAR_SEQ 1239 1239 A -> AGNNDNERLAIARQRIPYRLGRVVDEWLLDK (in
isoform 3a and isoform 2a).
{ECO:0000303|PubMed:18179900,
ECO:0000303|PubMed:9628581}.
/FTId=VSP_041355.
VAR_SEQ 1336 1344 GKPPTKEPI -> MDMRWHCEN (in isoform 4).
{ECO:0000303|PubMed:11230166}.
/FTId=VSP_058201.
VAR_SEQ 1373 1375 Missing (in isoform 4 and isoform 2a).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:9628581}.
/FTId=VSP_058202.
VARIANT 28 28 G -> A (in dbSNP:rs199598542).
{ECO:0000269|PubMed:22892527}.
/FTId=VAR_070274.
VARIANT 400 400 Y -> N (in dbSNP:rs17040901).
/FTId=VAR_050265.
CONFLICT 1360 1360 S -> G (in Ref. 5; CAI46085).
{ECO:0000305}.
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


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EIAAB27919 C14orf60,Homo sapiens,Human,KIAA0743,Neurexin III-alpha,Neurexin-3-alpha,NRXN3
EIAAB27907 Homo sapiens,Human,KIAA0578,Neurexin I-alpha,Neurexin-1-alpha,NRXN1
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EIAAB27904 Neurexin I-alpha,Neurexin-1-alpha,Nrxn1,Rat,Rattus norvegicus
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