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Q9CS84

- NRX1A_MOUSE

UniProt

Q9CS84 - NRX1A_MOUSE

Protein

Neurexin-1

Gene

Nrxn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi329 – 3291Calcium 1By similarity
    Metal bindingi346 – 3461Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi414 – 4141Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi772 – 7721Calcium 2By similarity
    Metal bindingi789 – 7891Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi848 – 8481Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi1183 – 11831Calcium 3
    Metal bindingi1200 – 12001Calcium 3; via carbonyl oxygen
    Metal bindingi1282 – 12821Calcium 3; via carbonyl oxygen
    Metal bindingi1284 – 12841Calcium 3

    GO - Molecular functioni

    1. acetylcholine receptor binding Source: MGI
    2. calcium channel regulator activity Source: MGI
    3. calcium ion binding Source: BHF-UCL
    4. cell adhesion molecule binding Source: BHF-UCL
    5. neuroligin family protein binding Source: BHF-UCL
    6. protein binding Source: IntAct

    GO - Biological processi

    1. adult behavior Source: BHF-UCL
    2. cell adhesion Source: UniProtKB-KW
    3. gephyrin clustering Source: BHF-UCL
    4. learning Source: BHF-UCL
    5. neuroligin clustering Source: BHF-UCL
    6. neuromuscular process controlling balance Source: BHF-UCL
    7. neurotransmitter secretion Source: MGI
    8. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    9. positive regulation of synapse assembly Source: MGI
    10. positive regulation of synapse maturation Source: MGI
    11. positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
    12. postsynaptic density protein 95 clustering Source: BHF-UCL
    13. postsynaptic membrane assembly Source: BHF-UCL
    14. prepulse inhibition Source: BHF-UCL
    15. regulation of grooming behavior Source: BHF-UCL
    16. regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
    17. social behavior Source: Ensembl
    18. synapse assembly Source: MGI
    19. synaptic transmission Source: MGI
    20. vocalization behavior Source: Ensembl
    21. vocal learning Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196607. Non-integrin membrane-ECM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurexin-1
    Alternative name(s):
    Neurexin I-alpha
    Neurexin-1-alpha
    Gene namesi
    Name:Nrxn1
    Synonyms:Kiaa0578
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1096391. Nrxn1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell junctionsynapse 1 Publication
    Note: Localized on the pre-synaptic membrane.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell surface Source: BHF-UCL
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: BHF-UCL
    5. presynaptic membrane Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse

    Pathology & Biotechi

    Disruption phenotypei

    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.7 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 15141484Neurexin-1PRO_0000043164Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi228 ↔ 243By similarity
    Disulfide bondi245 ↔ 255By similarity
    Disulfide bondi444 ↔ 480By similarity
    Disulfide bondi650 ↔ 679By similarity
    Disulfide bondi687 ↔ 698By similarity
    Disulfide bondi692 ↔ 707By similarity
    Disulfide bondi709 ↔ 719By similarity
    Glycosylationi797 – 7971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1059 ↔ 1087By similarity
    Disulfide bondi1094 ↔ 1105By similarity
    Disulfide bondi1099 ↔ 1114By similarity
    Disulfide bondi1116 ↔ 1126By similarity
    Glycosylationi1230 – 12301N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.By similarity
    O-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9CS84.
    PaxDbiQ9CS84.
    PRIDEiQ9CS84.

    PTM databases

    PhosphoSiteiQ9CS84.

    Expressioni

    Gene expression databases

    BgeeiQ9CS84.
    CleanExiMM_NRXN1.
    GenevestigatoriQ9CS84.

    Interactioni

    Subunit structurei

    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.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTPRTO145222EBI-399696,EBI-728180From a different organism.

    Protein-protein interaction databases

    BioGridi201851. 1 interaction.
    IntActiQ9CS84. 6 interactions.
    MINTiMINT-7989270.

    Structurei

    Secondary structure

    1
    1514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1132 – 114514
    Beta strandi1154 – 116411
    Beta strandi1168 – 118114
    Beta strandi1184 – 11907
    Beta strandi1193 – 120210
    Beta strandi1205 – 12084
    Beta strandi1216 – 12183
    Beta strandi1220 – 12278
    Beta strandi1230 – 12356
    Beta strandi1241 – 12433
    Beta strandi1265 – 127713
    Beta strandi1286 – 12927
    Helixi1294 – 12963
    Beta strandi1302 – 13098
    Helixi1314 – 13196
    Beta strandi1325 – 13339

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BODX-ray1.70A1132-1334[»]
    3MW2X-ray2.69A/B1132-1334[»]
    ProteinModelPortaliQ9CS84.
    SMRiQ9CS84. Positions 56-1335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CS84.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 14381408ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1460 – 151455CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1439 – 145921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 217187Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini219 – 25638EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 480198Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini487 – 679193Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini683 – 72038EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini725 – 898174Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini912 – 1087176Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1090 – 112738EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1133 – 1331199Laminin G-like 6PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 219Poly-Leu
    Compositional biasi1361 – 13644Poly-Thr
    Compositional biasi1446 – 14494Poly-Ala

    Sequence similaritiesi

    Belongs to the neurexin family.Curated
    Contains 3 EGF-like domains.PROSITE-ProRule annotation
    Contains 6 laminin G-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG302266.
    GeneTreeiENSGT00750000117263.
    HOGENOMiHOG000230481.
    HOVERGENiHBG052670.
    InParanoidiQ9CS84.
    KOiK07377.
    OMAiDCSQEIK.
    OrthoDBiEOG7XWPMM.
    PhylomeDBiQ9CS84.

    Family and domain databases

    Gene3Di2.60.120.200. 6 hits.
    InterProiIPR008985. 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]
    PfamiPF02210. Laminin_G_2. 6 hits.
    PF01034. Syndecan. 1 hit.
    [Graphical view]
    SMARTiSM00294. 4.1m. 1 hit.
    SM00181. EGF. 3 hits.
    SM00282. LamG. 6 hits.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 7 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
    PS50026. EGF_3. 3 hits.
    PS50025. LAM_G_DOMAIN. 6 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1a (identifier: Q9CS84-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGTALVQRGG CCLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC     50
    ESEMSFQLKT RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP 100
    ATLLADTPVN DGAWHSVRIR RQFRNTTLYI DRAEAKWVEV KSKRRDMTVF 150
    SGLFVGGLPP ELRAAALKLT LASVREREPF KGWIRDVRVN SSQALPVDGG 200
    EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ AVCDCSRTGF 250
    RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP 300
    IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA 350
    FEALVEPVNG KFNDNAWHDV KVTRNLRQHS GIGHAMVNKL HCSVTISVDG 400
    ILTTTGYTQE DYTMLGSDDF FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY 450
    KNNDVRLELS RLAKQGDPKM KIHGVVAFKC ENVATLDPIT FETPESFISL 500
    PKWNAKKTGS ISFDFRTTEP NGLILFSHGK PRHQKDAKHP QMIKVDFFAI 550
    EMLDGHLYLL LDMGSGTIKI KALQKKVNDG EWYHVDFQRD GRSGTISVNT 600
    LRTPYTAPGE SEILDLDDEL YLGGLPENKA GLVFPTEVWT ALLNYGYVGC 650
    IRDLFIDGQS KDIRQMAEIQ STAGVKPSCS KETAKPCLSN PCKNNGMCRD 700
    GWNRYVCDCS GTGYLGRSCE REATVLSYDG SMFMKIQLPV VMHTEAEDVS 750
    LRFRSQRAYG ILMATTSRDS ADTLRLELDA GRVKLTVNLD CIRINCNSSK 800
    GPETLFAGYN LNDNEWHTVR VVRRGKSLKL TVDDQQAMTG QMAGDHTRLE 850
    FHNIETGIIT ERRYLSSVPS NFIGHLQSLT FNGMAYIDLC KNGDIDYCEL 900
    NARFGFRNII ADPVTFKTKS SYVALATLQA YTSMHLFFQF KTTSLDGLIL 950
    YNSGDGNDFI VVELVKGYLH YVFDLGNGAN LIKGSSNKPL NDNQWHNVMI 1000
    SRDTSNLHTV KIDTKITTQI TAGARNLDLK SDLYIGGVAK ETYKSLPKLV 1050
    HAKEGFQGCL ASVDLNGRLP DLISDALFCN GQIERGCEGP STTCQEDSCS 1100
    NQGVCLQQWD GFSCDCSMTS FSGPLCNDPG TTYIFSKGGG QITYKWPPND 1150
    RPSTRADRLA IGFSTVQKEA VLVRVDSSSG LGDYLELHIH QGKIGVKFNV 1200
    GTDDIAIEES NAIINDGKYH VVRFTRSGGN ATLQVDSWPV IERYPAGNND 1250
    NERLAIARQR IPYRLGRVVD EWLLDKGRQL TIFNSQATII IGGKEQGQPF 1300
    QGQLSGLYYN GLKVLNMAAE NDANIAIVGN VRLVGEVPSS MTTESTATAM 1350
    QSEMSTSIME TTTTLATSTA RRGKPPTKEP ISQTTDDILV ASAECPSDDE 1400
    DIDPCEPSSG GLANPTRVGG REPYPGSAEV IRESSSTTGM VVGIVAAAAL 1450
    CILILLYAMY KYRNRDEGSY HVDESRNYIS NSAQSNGAVV KEKQPSSAKS 1500
    ANKNKKNKDK EYYV 1514
    Length:1,514
    Mass (Da):166,169
    Last modified:December 6, 2005 - v3
    Checksum:i412281FE441F0EFC
    GO
    Isoform 2a (identifier: Q9CS84-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-2B

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

    Show »
    Length:1,507
    Mass (Da):165,387
    Checksum:iB3372630D1BD0606
    GO
    Isoform 3a (identifier: Q9CS84-3) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-2C

    The sequence of this isoform differs from the canonical sequence as follows:
         379-393: Missing.

    Show »
    Length:1,499
    Mass (Da):164,596
    Checksum:i5574E00C647EAD9E
    GO
    Isoform 4a (identifier: Q9CS84-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,176
    Mass (Da):129,340
    Checksum:i9AA6E9F48CF994CE
    GO
    Isoform 1b (identifier: P0DI97-1) [UniParc]FASTAAdd to Basket

    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.
    Length:468
    Mass (Da):50,223
    GO
    Isoform 5a (identifier: Q9CS84-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,477
    Mass (Da):161,824
    Checksum:i31E076AB249810B5
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 320320Missing in isoform 4a. 1 PublicationVSP_016400Add
    BLAST
    Alternative sequencei379 – 39315Missing in isoform 3a and isoform 4a. 1 PublicationVSP_003485Add
    BLAST
    Alternative sequencei387 – 3937Missing in isoform 2a and isoform 5a. 2 PublicationsVSP_003484
    Alternative sequencei1247 – 127630Missing in isoform 5a. CuratedVSP_043946Add
    BLAST
    Alternative sequencei1410 – 14123Missing in isoform 4a. 1 PublicationVSP_016401

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS57113.1. [Q9CS84-2]
    RefSeqiNP_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]
    UniGeneiMm.491332.

    Genome annotation databases

    EnsembliENSMUST00000054059; ENSMUSP00000057294; ENSMUSG00000024109. [Q9CS84-3]
    ENSMUST00000160844; ENSMUSP00000125407; ENSMUSG00000024109. [Q9CS84-2]
    ENSMUST00000161402; ENSMUSP00000124116; ENSMUSG00000024109. [Q9CS84-1]
    ENSMUST00000174331; ENSMUSP00000133491; ENSMUSG00000024109. [Q9CS84-5]
    GeneIDi18189.
    KEGGimmu:18189.
    UCSCiuc008dvz.2. mouse. [Q9CS84-2]
    uc008dwa.2. mouse. [Q9CS84-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS57113.1. [Q9CS84-2 ]
    RefSeqi NP_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 ]
    UniGenei Mm.491332.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BOD X-ray 1.70 A 1132-1334 [» ]
    3MW2 X-ray 2.69 A/B 1132-1334 [» ]
    ProteinModelPortali Q9CS84.
    SMRi Q9CS84. Positions 56-1335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201851. 1 interaction.
    IntActi Q9CS84. 6 interactions.
    MINTi MINT-7989270.

    PTM databases

    PhosphoSitei Q9CS84.

    Proteomic databases

    MaxQBi Q9CS84.
    PaxDbi Q9CS84.
    PRIDEi Q9CS84.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000054059 ; ENSMUSP00000057294 ; ENSMUSG00000024109 . [Q9CS84-3 ]
    ENSMUST00000160844 ; ENSMUSP00000125407 ; ENSMUSG00000024109 . [Q9CS84-2 ]
    ENSMUST00000161402 ; ENSMUSP00000124116 ; ENSMUSG00000024109 . [Q9CS84-1 ]
    ENSMUST00000174331 ; ENSMUSP00000133491 ; ENSMUSG00000024109 . [Q9CS84-5 ]
    GeneIDi 18189.
    KEGGi mmu:18189.
    UCSCi uc008dvz.2. mouse. [Q9CS84-2 ]
    uc008dwa.2. mouse. [Q9CS84-4 ]

    Organism-specific databases

    CTDi 9378.
    MGIi MGI:1096391. Nrxn1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG302266.
    GeneTreei ENSGT00750000117263.
    HOGENOMi HOG000230481.
    HOVERGENi HBG052670.
    InParanoidi Q9CS84.
    KOi K07377.
    OMAi DCSQEIK.
    OrthoDBi EOG7XWPMM.
    PhylomeDBi Q9CS84.

    Enzyme and pathway databases

    Reactomei REACT_196607. Non-integrin membrane-ECM interactions.

    Miscellaneous databases

    ChiTaRSi NRXN1. mouse.
    EvolutionaryTracei Q9CS84.
    NextBioi 293528.
    PROi Q9CS84.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CS84.
    CleanExi MM_NRXN1.
    Genevestigatori Q9CS84.

    Family and domain databases

    Gene3Di 2.60.120.200. 6 hits.
    InterProi IPR008985. 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 ]
    Pfami PF02210. Laminin_G_2. 6 hits.
    PF01034. Syndecan. 1 hit.
    [Graphical view ]
    SMARTi SM00294. 4.1m. 1 hit.
    SM00181. EGF. 3 hits.
    SM00282. LamG. 6 hits.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 7 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
    PS50026. EGF_3. 3 hits.
    PS50025. LAM_G_DOMAIN. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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.

    Entry informationi

    Entry nameiNRX1A_MOUSE
    AccessioniPrimary (citable) accession number: Q9CS84
    Secondary accession number(s): G3UWZ9
    , O88722, Q80Y87, Q8CHE6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3