SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9CS84

- NRX1A_MOUSE

UniProt

Q9CS84 - NRX1A_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Neurexin-1
Gene
Nrxn1, Kiaa0578
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi346 – 3461Calcium 1; via carbonyl oxygen By similarity
Metal bindingi414 – 4141Calcium 1; via carbonyl oxygen By similarity
Metal bindingi772 – 7721Calcium 2 By similarity
Metal bindingi789 – 7891Calcium 2; via carbonyl oxygen By similarity
Metal bindingi848 – 8481Calcium 2; via carbonyl oxygen By 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. vocal learning Source: Ensembl
  21. vocalization behavior Source: Ensembl
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 14381408Extracellular Reviewed prediction
Add
BLAST
Transmembranei1439 – 145921Helical; Reviewed prediction
Add
BLAST
Topological domaini1460 – 151455Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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 – 3030 Reviewed prediction
Add
BLAST
Chaini31 – 15141484Neurexin-1
PRO_0000043164Add
BLAST

Amino acid modifications

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

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 CBLN4.7 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

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.

Miscellaneous databases

EvolutionaryTraceiQ9CS84.

Family & Domainsi

Domains and Repeats

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

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.
VSP_016400Add
BLAST
Alternative sequencei379 – 39315Missing in isoform 3a and isoform 4a.
VSP_003485Add
BLAST
Alternative sequencei387 – 3937Missing in isoform 2a and isoform 5a.
VSP_003484
Alternative sequencei1247 – 127630Missing in isoform 5a.
VSP_043946Add
BLAST
Alternative sequencei1410 – 14123Missing in isoform 4a.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 134 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

Similar proteinsi