CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020603
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Neurexin-1 
Protein Synonyms/Alias
 Neurexin I-alpha; Neurexin-1-alpha 
Gene Name
 Nrxn1 
Gene Synonyms/Alias
 Kiaa0578 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1491QSNGAVVKEKQPSSAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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 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. 
Sequence Annotation
 DOMAIN 31 217 Laminin G-like 1.
 DOMAIN 219 256 EGF-like 1.
 DOMAIN 283 480 Laminin G-like 2.
 DOMAIN 487 679 Laminin G-like 3.
 DOMAIN 683 720 EGF-like 2.
 DOMAIN 725 898 Laminin G-like 4.
 DOMAIN 912 1087 Laminin G-like 5.
 DOMAIN 1090 1127 EGF-like 3.
 DOMAIN 1133 1331 Laminin G-like 6.
 METAL 329 329 Calcium 1 (By similarity).
 METAL 346 346 Calcium 1; via carbonyl oxygen (By
 METAL 414 414 Calcium 1; via carbonyl oxygen (By
 METAL 772 772 Calcium 2 (By similarity).
 METAL 789 789 Calcium 2; via carbonyl oxygen (By
 METAL 848 848 Calcium 2; via carbonyl oxygen (By
 METAL 1183 1183 Calcium 3.
 METAL 1200 1200 Calcium 3; via carbonyl oxygen.
 METAL 1282 1282 Calcium 3; via carbonyl oxygen.
 METAL 1284 1284 Calcium 3.
 CARBOHYD 125 125 N-linked (GlcNAc...) (Potential).
 CARBOHYD 190 190 N-linked (GlcNAc...) (Potential).
 CARBOHYD 797 797 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1230 1230 N-linked (GlcNAc...) (Potential).
 DISULFID 228 243 By similarity.
 DISULFID 245 255 By similarity.
 DISULFID 444 480 By similarity.
 DISULFID 650 679 By similarity.
 DISULFID 687 698 By similarity.
 DISULFID 692 707 By similarity.
 DISULFID 709 719 By similarity.
 DISULFID 1059 1087 By similarity.
 DISULFID 1094 1105 By similarity.
 DISULFID 1099 1114 By similarity.
 DISULFID 1116 1126 By similarity.  
Keyword
 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal; Synapse; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1514 AA 
Protein Sequence
MGTALVQRGG CCLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT 60
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR 120
RQFRNTTLYI DRAEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF 180
KGWIRDVRVN SSQALPVDGG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ 240
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP 300
IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG 360
KFNDNAWHDV KVTRNLRQHS GIGHAMVNKL HCSVTISVDG ILTTTGYTQE DYTMLGSDDF 420
FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDVRLELS RLAKQGDPKM KIHGVVAFKC 480
ENVATLDPIT FETPESFISL PKWNAKKTGS ISFDFRTTEP NGLILFSHGK PRHQKDAKHP 540
QMIKVDFFAI EMLDGHLYLL LDMGSGTIKI KALQKKVNDG EWYHVDFQRD GRSGTISVNT 600
LRTPYTAPGE SEILDLDDEL YLGGLPENKA GLVFPTEVWT ALLNYGYVGC IRDLFIDGQS 660
KDIRQMAEIQ STAGVKPSCS KETAKPCLSN PCKNNGMCRD GWNRYVCDCS GTGYLGRSCE 720
REATVLSYDG SMFMKIQLPV VMHTEAEDVS LRFRSQRAYG ILMATTSRDS ADTLRLELDA 780
GRVKLTVNLD CIRINCNSSK GPETLFAGYN LNDNEWHTVR VVRRGKSLKL TVDDQQAMTG 840
QMAGDHTRLE FHNIETGIIT ERRYLSSVPS NFIGHLQSLT FNGMAYIDLC KNGDIDYCEL 900
NARFGFRNII ADPVTFKTKS SYVALATLQA YTSMHLFFQF KTTSLDGLIL YNSGDGNDFI 960
VVELVKGYLH YVFDLGNGAN LIKGSSNKPL NDNQWHNVMI SRDTSNLHTV KIDTKITTQI 1020
TAGARNLDLK SDLYIGGVAK ETYKSLPKLV HAKEGFQGCL ASVDLNGRLP DLISDALFCN 1080
GQIERGCEGP STTCQEDSCS NQGVCLQQWD GFSCDCSMTS FSGPLCNDPG TTYIFSKGGG 1140
QITYKWPPND RPSTRADRLA IGFSTVQKEA VLVRVDSSSG LGDYLELHIH QGKIGVKFNV 1200
GTDDIAIEES NAIINDGKYH VVRFTRSGGN ATLQVDSWPV IERYPAGNND NERLAIARQR 1260
IPYRLGRVVD EWLLDKGRQL TIFNSQATII IGGKEQGQPF QGQLSGLYYN GLKVLNMAAE 1320
NDANIAIVGN VRLVGEVPSS MTTESTATAM QSEMSTSIME TTTTLATSTA RRGKPPTKEP 1380
ISQTTDDILV ASAECPSDDE DIDPCEPSSG GLANPTRVGG REPYPGSAEV IRESSSTTGM 1440
VVGIVAAAAL CILILLYAMY KYRNRDEGSY HVDESRNYIS NSAQSNGAVV KEKQPSSAKS 1500
ANKNKKNKDK EYYV 1514 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0009986; C:cell surface; IDA:BHF-UCL.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IC:BHF-UCL.
 GO:0042734; C:presynaptic membrane; IDA:MGI.
 GO:0033130; F:acetylcholine receptor binding; IDA:MGI.
 GO:0005246; F:calcium channel regulator activity; IGI:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0030534; P:adult behavior; IMP:BHF-UCL.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0097116; P:gephyrin clustering; IDA:BHF-UCL.
 GO:0007612; P:learning; IMP:BHF-UCL.
 GO:0097118; P:neuroligin clustering; IDA:BHF-UCL.
 GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
 GO:0007269; P:neurotransmitter secretion; IGI:MGI.
 GO:2000463; P:positive regulation of excitatory postsynaptic membrane potential; IMP:BHF-UCL.
 GO:0051965; P:positive regulation of synapse assembly; IGI:MGI.
 GO:0090129; P:positive regulation of synapse maturation; IDA:MGI.
 GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
 GO:0097119; P:postsynaptic density protein 95 clustering; IDA:BHF-UCL.
 GO:0097104; P:postsynaptic membrane assembly; IDA:BHF-UCL.
 GO:0060134; P:prepulse inhibition; IMP:BHF-UCL.
 GO:2000821; P:regulation of grooming behavior; IMP:BHF-UCL.
 GO:0035176; P:social behavior; IEA:Compara.
 GO:0071625; P:vocalization behavior; IEA:Compara. 
Interpro
 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.
 IPR027158; NRXN1-alpha. 
Pfam
 PF02210; Laminin_G_2 
SMART
 SM00294; 4.1m
 SM00181; EGF
 SM00282; LamG 
PROSITE
 PS00010; ASX_HYDROXYL
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS50025; LAM_G_DOMAIN 
PRINTS