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Q9CS84 (NRX1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurexin-1
Alternative name(s):
Neurexin I-alpha
Neurexin-1-alpha
Gene names
Name:Nrxn1
Synonyms:Kiaa0578
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 Ca2+-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca2+-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 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. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18

Subunit structure

The cytoplasmic C-terminal region binds to CASK, CASKIN1 and APBA1. Interacts (via laminin G-like domain 2) with NXPH1 and NXPH3 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. Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4 By similarity. 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 and NLGN4L; these interactions are calcium-dependent. Interacts with SYT13 and SYTL1. Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4. Ref.8 Ref.9 Ref.10 Ref.16 Ref.18 Ref.19 Ref.20

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell junctionsynapse. Note: Localized on the pre-synaptic membrane By similarity. Ref.18

Post-translational modification

N-glycosylated By similarity.

O-glycosylated By similarity.

Disruption phenotype

No visible phenotype, but mice display subtle behavorial deficits. Females show deficits in nest building and taking care of pups. Mice lacking the alpha-type isoforms of NRXN1, NRXN2 and NRXN3 are born at the expected Mendelian rate, but die during the first day after birth, probably due to neurological defects in the brainstem that impair normal breathing. These mice express normal levels of the beta-type isoforms of NRXN1, NRXN2 and NRXN3. Mice show reduced density of synapses in the brainstem, especially a reduction in the numbers of GABA-releasing synapses. Their brains display a reduced frequency of spontaneous neurotransmitter release, and decreased neurotransmitter release in response to an action potential. Likewise, the activity of voltage-gated calcium channels is strongly decreased. A small proportion (5-10%) of mice lacking the alpha-type isoforms of both NRXN1 and NRXN2 survive to adulthood; these mice do not show any gross anatomical defects in their brains or changes in the distribution of synaptic proteins, but they have fewer synapses in the neocortex and show defects in neurotransmitter release at neuromuscular junctions. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Sequence similarities

Belongs to the neurexin family.

Contains 3 EGF-like domains.

Contains 6 laminin G-like domains.

Sequence caution

The sequence BAC41433.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult behavior

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

gephyrin clustering

Inferred from direct assay PubMed 21424692. Source: BHF-UCL

learning

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

neuroligin clustering

Inferred from direct assay PubMed 21424692. Source: BHF-UCL

neuromuscular process controlling balance

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

neurotransmitter secretion

Inferred from genetic interaction Ref.11. Source: MGI

positive regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

positive regulation of synapse assembly

Inferred from genetic interaction PubMed 21356198. Source: MGI

positive regulation of synapse maturation

Inferred from direct assay PubMed 19567877. Source: MGI

positive regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

postsynaptic density protein 95 clustering

Inferred from direct assay PubMed 21424692. Source: BHF-UCL

postsynaptic membrane assembly

Inferred from direct assay PubMed 21424692. Source: BHF-UCL

prepulse inhibition

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

regulation of grooming behavior

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 22235116. Source: MGI

social behavior

Inferred from electronic annotation. Source: Ensembl

synapse assembly

Inferred from genetic interaction Ref.11. Source: MGI

synaptic transmission

Inferred from genetic interaction Ref.11. Source: MGI

vocal learning

Inferred from electronic annotation. Source: Ensembl

vocalization behavior

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 21424692. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

presynaptic membrane

Inferred from direct assay Ref.11. Source: MGI

   Molecular_functionacetylcholine receptor binding

Inferred from direct assay PubMed 19567877. Source: MGI

calcium channel regulator activity

Inferred from genetic interaction Ref.11. Source: MGI

calcium ion binding

Inferred from sequence or structural similarity. Source: BHF-UCL

cell adhesion molecule binding

Inferred from physical interaction PubMed 21424692. Source: BHF-UCL

neuroligin family protein binding

Inferred from physical interaction PubMed 21424692. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 19816407. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPRTO145222EBI-399696,EBI-728180From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1a (identifier: Q9CS84-1)

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.
Isoform 2a (identifier: Q9CS84-2)

Also known as: Alpha-2B;

The sequence of this isoform differs from the canonical sequence as follows:
     387-393: Missing.
Isoform 3a (identifier: Q9CS84-3)

Also known as: Alpha-2C;

The sequence of this isoform differs from the canonical sequence as follows:
     379-393: Missing.
Isoform 4a (identifier: Q9CS84-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-320: Missing.
     379-393: Missing.
     1410-1412: Missing.
Note: No experimental confirmation available.
Isoform 1b (identifier: P0DI97-1)

The sequence of this isoform can be found in the external entry P0DI97.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 5a (identifier: Q9CS84-5)

The sequence of this isoform differs from the canonical sequence as follows:
     387-393: Missing.
     1247-1276: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 15141484Neurexin-1
PRO_0000043164

Regions

Topological domain31 – 14381408Extracellular Potential
Transmembrane1439 – 145921Helical; Potential
Topological domain1460 – 151455Cytoplasmic Potential
Domain31 – 217187Laminin G-like 1
Domain219 – 25638EGF-like 1
Domain283 – 480198Laminin G-like 2
Domain487 – 679193Laminin G-like 3
Domain683 – 72038EGF-like 2
Domain725 – 898174Laminin G-like 4
Domain912 – 1087176Laminin G-like 5
Domain1090 – 112738EGF-like 3
Domain1133 – 1331199Laminin G-like 6
Compositional bias13 – 219Poly-Leu
Compositional bias1361 – 13644Poly-Thr
Compositional bias1446 – 14494Poly-Ala

Sites

Metal binding3291Calcium 1 By similarity
Metal binding3461Calcium 1; via carbonyl oxygen By similarity
Metal binding4141Calcium 1; via carbonyl oxygen By similarity
Metal binding7721Calcium 2 By similarity
Metal binding7891Calcium 2; via carbonyl oxygen By similarity
Metal binding8481Calcium 2; via carbonyl oxygen By similarity
Metal binding11831Calcium 3
Metal binding12001Calcium 3; via carbonyl oxygen
Metal binding12821Calcium 3; via carbonyl oxygen
Metal binding12841Calcium 3

Amino acid modifications

Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation7971N-linked (GlcNAc...) Potential
Glycosylation12301N-linked (GlcNAc...) Potential
Disulfide bond228 ↔ 243 By similarity
Disulfide bond245 ↔ 255 By similarity
Disulfide bond444 ↔ 480 By similarity
Disulfide bond650 ↔ 679 By similarity
Disulfide bond687 ↔ 698 By similarity
Disulfide bond692 ↔ 707 By similarity
Disulfide bond709 ↔ 719 By similarity
Disulfide bond1059 ↔ 1087 By similarity
Disulfide bond1094 ↔ 1105 By similarity
Disulfide bond1099 ↔ 1114 By similarity
Disulfide bond1116 ↔ 1126 By similarity

Natural variations

Alternative sequence1 – 320320Missing in isoform 4a.
VSP_016400
Alternative sequence379 – 39315Missing in isoform 3a and isoform 4a.
VSP_003485
Alternative sequence387 – 3937Missing in isoform 2a and isoform 5a.
VSP_003484
Alternative sequence1247 – 127630Missing in isoform 5a.
VSP_043946
Alternative sequence1410 – 14123Missing in isoform 4a.
VSP_016401

Secondary structure

................................. 1514
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1a [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: 412281FE441F0EFC

FASTA1,514166,169
        10         20         30         40         50         60 
MGTALVQRGG CCLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT 

        70         80         90        100        110        120 
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR 

       130        140        150        160        170        180 
RQFRNTTLYI DRAEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF 

       190        200        210        220        230        240 
KGWIRDVRVN SSQALPVDGG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ 

       250        260        270        280        290        300 
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP 

       310        320        330        340        350        360 
IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG 

       370        380        390        400        410        420 
KFNDNAWHDV KVTRNLRQHS GIGHAMVNKL HCSVTISVDG ILTTTGYTQE DYTMLGSDDF 

       430        440        450        460        470        480 
FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDVRLELS RLAKQGDPKM KIHGVVAFKC 

       490        500        510        520        530        540 
ENVATLDPIT FETPESFISL PKWNAKKTGS ISFDFRTTEP NGLILFSHGK PRHQKDAKHP 

       550        560        570        580        590        600 
QMIKVDFFAI EMLDGHLYLL LDMGSGTIKI KALQKKVNDG EWYHVDFQRD GRSGTISVNT 

       610        620        630        640        650        660 
LRTPYTAPGE SEILDLDDEL YLGGLPENKA GLVFPTEVWT ALLNYGYVGC IRDLFIDGQS 

       670        680        690        700        710        720 
KDIRQMAEIQ STAGVKPSCS KETAKPCLSN PCKNNGMCRD GWNRYVCDCS GTGYLGRSCE 

       730        740        750        760        770        780 
REATVLSYDG SMFMKIQLPV VMHTEAEDVS LRFRSQRAYG ILMATTSRDS ADTLRLELDA 

       790        800        810        820        830        840 
GRVKLTVNLD CIRINCNSSK GPETLFAGYN LNDNEWHTVR VVRRGKSLKL TVDDQQAMTG 

       850        860        870        880        890        900 
QMAGDHTRLE FHNIETGIIT ERRYLSSVPS NFIGHLQSLT FNGMAYIDLC KNGDIDYCEL 

       910        920        930        940        950        960 
NARFGFRNII ADPVTFKTKS SYVALATLQA YTSMHLFFQF KTTSLDGLIL YNSGDGNDFI 

       970        980        990       1000       1010       1020 
VVELVKGYLH YVFDLGNGAN LIKGSSNKPL NDNQWHNVMI SRDTSNLHTV KIDTKITTQI 

      1030       1040       1050       1060       1070       1080 
TAGARNLDLK SDLYIGGVAK ETYKSLPKLV HAKEGFQGCL ASVDLNGRLP DLISDALFCN 

      1090       1100       1110       1120       1130       1140 
GQIERGCEGP STTCQEDSCS NQGVCLQQWD GFSCDCSMTS FSGPLCNDPG TTYIFSKGGG 

      1150       1160       1170       1180       1190       1200 
QITYKWPPND RPSTRADRLA IGFSTVQKEA VLVRVDSSSG LGDYLELHIH QGKIGVKFNV 

      1210       1220       1230       1240       1250       1260 
GTDDIAIEES NAIINDGKYH VVRFTRSGGN ATLQVDSWPV IERYPAGNND NERLAIARQR 

      1270       1280       1290       1300       1310       1320 
IPYRLGRVVD EWLLDKGRQL TIFNSQATII IGGKEQGQPF QGQLSGLYYN GLKVLNMAAE 

      1330       1340       1350       1360       1370       1380 
NDANIAIVGN VRLVGEVPSS MTTESTATAM QSEMSTSIME TTTTLATSTA RRGKPPTKEP 

      1390       1400       1410       1420       1430       1440 
ISQTTDDILV ASAECPSDDE DIDPCEPSSG GLANPTRVGG REPYPGSAEV IRESSSTTGM 

      1450       1460       1470       1480       1490       1500 
VVGIVAAAAL CILILLYAMY KYRNRDEGSY HVDESRNYIS NSAQSNGAVV KEKQPSSAKS 

      1510 
ANKNKKNKDK EYYV 

« Hide

Isoform 2a (Alpha-2B) [UniParc].

Checksum: B3372630D1BD0606
Show »

FASTA1,507165,387
Isoform 3a (Alpha-2C) [UniParc].

Checksum: 5574E00C647EAD9E
Show »

FASTA1,499164,596
Isoform 4a [UniParc].

Checksum: 9AA6E9F48CF994CE
Show »

FASTA1,176129,340
Isoform 1b [UniParc].

See P0DI97.

Isoform 5a [UniParc].

Checksum: 31E076AB249810B5
Show »

FASTA1,477161,824

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A).
Tissue: Brain.
[2]Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4A).
Tissue: Eye.
[5]"Sequencing of the neurexin genes."
Graveley B.R., Philipps D.L.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 298-437 (ISOFORMS 1A; 2A AND 3A/4A).
Strain: CD-1.
Tissue: Brain.
[6]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1126-1514 (ISOFORMS 1A/2A/3A).
Strain: C57BL/6J.
Tissue: Embryo.
[7]"Differential seizure-induced and developmental changes of neurexin expression."
Gorecki D.C., Szklarczyk A., Lukasiuk K., Kaczmarek L., Simons J.P.
Mol. Cell. Neurosci. 13:218-227(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1463-1505 (ISOFORMS 1A/2A/3A/4A).
Strain: C57BL/10.
Tissue: Brain.
[8]"Neurexin I alpha is a major alpha-latrotoxin receptor that cooperates in alpha-latrotoxin action."
Geppert M., Khvotchev M., Krasnoperov V., Goda Y., Missler M., Hammer R.E., Ichtchenko K., Petrenko A.G., Sudhof T.C.
J. Biol. Chem. 273:1705-1710(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, CALCIUM-DEPENDENT INTERACTION WITH ALPHA-LATROTOXIN.
[9]"Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins."
Fukuda M., Mikoshiba K.
Biochem. Biophys. Res. Commun. 281:1226-1233(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYTL1.
[10]"Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII)."
Fukuda M., Mikoshiba K.
Biochem. J. 354:249-257(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYT13.
[11]"Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis."
Missler M., Zhang W., Rohlmann A., Kattenstroth G., Hammer R.E., Gottmann K., Sudhof T.C.
Nature 423:939-948(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN NEUROTRANSMITTER RELEASE.
[12]"Postsynaptic N-methyl-D-aspartate receptor function requires alpha-neurexins."
Kattenstroth G., Tantalaki E., Sudhof T.C., Gottmann K., Missler M.
Proc. Natl. Acad. Sci. U.S.A. 101:2607-2612(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[13]"Important contribution of alpha-neurexins to Ca2+-triggered exocytosis of secretory granules."
Dudanova I., Sedej S., Ahmad M., Masius H., Sargsyan V., Zhang W., Riedel D., Angenstein F., Schild D., Rupnik M., Missler M.
J. Neurosci. 26:10599-10613(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[14]"alpha-Neurexins are required for efficient transmitter release and synaptic homeostasis at the mouse neuromuscular junction."
Sons M.S., Busche N., Strenzke N., Moser T., Ernsberger U., Mooren F.C., Zhang W., Ahmad M., Steffens H., Schomburg E.D., Plomp J.J., Missler M.
Neuroscience 138:433-446(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[15]"Deletion of alpha-neurexins does not cause a major impairment of axonal pathfinding or synapse formation."
Dudanova I., Tabuchi K., Rohlmann A., Sudhof T.C., Missler M.
J. Comp. Neurol. 502:261-274(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[16]"Unusually rapid evolution of neuroligin-4 in mice."
Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V., Sudhof T.C.
Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLGN4L.
[17]"Mouse neurexin-1alpha deletion causes correlated electrophysiological and behavioral changes consistent with cognitive impairments."
Etherton M.R., Blaiss C.A., Powell C.M., Sudhof T.C.
Proc. Natl. Acad. Sci. U.S.A. 106:17998-18003(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[18]"Cbln family proteins promote synapse formation by regulating distinct neurexin signaling pathways in various brain regions."
Matsuda K., Yuzaki M.
Eur. J. Neurosci. 33:1447-1461(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBLN1; CBLN2 AND CBLN4.
[19]"Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4."
Koehnke J., Jin X., Trbovic N., Katsamba P.S., Brasch J., Ahlsen G., Scheiffele P., Honig B., Palmer A.G. III, Shapiro L.
Structure 16:410-421(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1132-1334 (ISOFORM 5A) IN COMPLEX WITH CALCIUM, SUBUNIT, INTERACTION WITH NLGN1 AND NLGN2, ALTERNATIVE SPLICING.
[20]"Splice form dependence of beta-neurexin/neuroligin binding interactions."
Koehnke J., Katsamba P.S., Ahlsen G., Bahna F., Vendome J., Honig B., Shapiro L., Jin X.
Neuron 67:61-74(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 1132-1334, INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB093249 mRNA. Translation: BAC41433.2. Different initiation.
AC101872 Genomic DNA. No translation available.
AC131326 Genomic DNA. No translation available.
AC151286 Genomic DNA. No translation available.
AC154325 Genomic DNA. No translation available.
AC154599 Genomic DNA. No translation available.
AC167814 Genomic DNA. No translation available.
AC170901 Genomic DNA. No translation available.
AC171209 Genomic DNA. No translation available.
CT025708 Genomic DNA. No translation available.
CT486002 Genomic DNA. No translation available.
BC047146 mRNA. Translation: AAH47146.1.
AF387674 Genomic DNA. Translation: AAK70469.1.
AF387674 Genomic DNA. Translation: AAK70470.1.
AF387674 Genomic DNA. Translation: AAK70471.1.
AK017578 mRNA. Translation: BAB30815.1.
AJ006802 mRNA. Translation: CAA07257.1.
CCDSCCDS57113.1. [Q9CS84-2]
RefSeqNP_064648.3. NM_020252.3. [Q9CS84-2]
NP_796258.2. NM_177284.2.
XP_006523869.1. XM_006523806.1. [Q9CS84-1]
XP_006523874.1. XM_006523811.1. [Q9CS84-3]
XP_006523879.1. XM_006523816.1. [Q9CS84-5]
UniGeneMm.491332.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BODX-ray1.70A1132-1334[»]
3MW2X-ray2.69A/B1132-1334[»]
ProteinModelPortalQ9CS84.
SMRQ9CS84. Positions 56-1335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201851. 1 interaction.
IntActQ9CS84. 6 interactions.
MINTMINT-7989270.

PTM databases

PhosphoSiteQ9CS84.

Proteomic databases

MaxQBQ9CS84.
PaxDbQ9CS84.
PRIDEQ9CS84.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054059; ENSMUSP00000057294; ENSMUSG00000024109. [Q9CS84-3]
ENSMUST00000160844; ENSMUSP00000125407; ENSMUSG00000024109. [Q9CS84-2]
ENSMUST00000161402; ENSMUSP00000124116; ENSMUSG00000024109. [Q9CS84-1]
ENSMUST00000174331; ENSMUSP00000133491; ENSMUSG00000024109. [Q9CS84-5]
GeneID18189.
KEGGmmu:18189.
UCSCuc008dvz.2. mouse. [Q9CS84-2]
uc008dwa.2. mouse. [Q9CS84-4]

Organism-specific databases

CTD9378.
MGIMGI:1096391. Nrxn1.
RougeSearch...

Phylogenomic databases

eggNOGNOG302266.
GeneTreeENSGT00750000117263.
HOGENOMHOG000230481.
HOVERGENHBG052670.
InParanoidQ9CS84.
KOK07377.
OMADCSQEIK.
OrthoDBEOG7XWPMM.
PhylomeDBQ9CS84.

Gene expression databases

BgeeQ9CS84.
CleanExMM_NRXN1.
GenevestigatorQ9CS84.

Family and domain databases

Gene3D2.60.120.200. 6 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR001791. Laminin_G.
IPR003585. Neurexin-like.
IPR027789. Syndecan/Neurexin_dom.
[Graphical view]
PfamPF02210. Laminin_G_2. 6 hits.
PF01034. Syndecan. 1 hit.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
SM00181. EGF. 3 hits.
SM00282. LamG. 6 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 7 hits.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS50026. EGF_3. 3 hits.
PS50025. LAM_G_DOMAIN. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNRXN1. mouse.
EvolutionaryTraceQ9CS84.
NextBio293528.
PROQ9CS84.
SOURCESearch...

Entry information

Entry nameNRX1A_MOUSE
AccessionPrimary (citable) accession number: Q9CS84
Secondary accession number(s): G3UWZ9 expand/collapse secondary AC list , O88722, Q80Y87, Q8CHE6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot