NRX2A_MOUSE
ID NRX2A_MOUSE Reviewed; 1710 AA.
AC E9Q7X7;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Neurexin-2 {ECO:0000305};
DE AltName: Full=Neurexin II-alpha;
DE AltName: Full=Neurexin-2-alpha {ECO:0000303|PubMed:28864826};
DE Flags: Precursor;
GN Name=Nrxn2 {ECO:0000312|MGI:MGI:1096362};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP INTERACTION WITH CBLN1.
RX PubMed=21410790; DOI=10.1111/j.1460-9568.2011.07638.x;
RA Matsuda K., Yuzaki M.;
RT "Cbln family proteins promote synapse formation by regulating distinct
RT neurexin signaling pathways in various brain regions.";
RL Eur. J. Neurosci. 33:1447-1461(2011).
RN [4]
RP INTERACTION WITH CBLN1; CBLN2 AND CBLN4.
RX PubMed=22220752; DOI=10.1111/j.1471-4159.2012.07648.x;
RA Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V.,
RA Deutch A.Y., Parris J., Morgan J.I.;
RT "The Cbln family of proteins interact with multiple signaling pathways.";
RL J. Neurochem. 121:717-729(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IGSF21.
RX PubMed=28864826; DOI=10.1038/s41467-017-00333-w;
RA Tanabe Y., Naito Y., Vasuta C., Lee A.K., Soumounou Y., Linhoff M.W.,
RA Takahashi H.;
RT "IgSF21 promotes differentiation of inhibitory synapses via binding to
RT neurexin2alpha.";
RL Nat. Commun. 8:408-408(2017).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion. May mediate intracellular signaling.
CC {ECO:0000250|UniProtKB:Q63374}.
CC -!- SUBUNIT: The laminin G-like domain 1 binds to NXPH1. Interacts with
CC PATJ (By similarity). Interacts with CBLN1, CBLN2 and, less avidly,
CC with CBLN4 (PubMed:22220752, PubMed:21410790). Isoforms alpha 2C bind
CC to alpha-dystroglycan (By similarity). Interacts (via Laminin G-like 1
CC domain) with IGSF21 (Ig-like 1 domain) in a trans-interaction manner
CC (PubMed:28864826). {ECO:0000250|UniProtKB:Q63374,
CC ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:22220752,
CC ECO:0000269|PubMed:28864826}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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DR EMBL; AC124394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS89327.1; -.
DR AlphaFoldDB; E9Q7X7; -.
DR SMR; E9Q7X7; -.
DR STRING; 10090.ENSMUSP00000109089; -.
DR GlyConnect; 2540; 2 N-Linked glycans (1 site).
DR GlyGen; E9Q7X7; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; E9Q7X7; -.
DR PhosphoSitePlus; E9Q7X7; -.
DR MaxQB; E9Q7X7; -.
DR PRIDE; E9Q7X7; -.
DR ProteomicsDB; 318986; -.
DR Antibodypedia; 63686; 48 antibodies from 7 providers.
DR Ensembl; ENSMUST00000137166; ENSMUSP00000119762; ENSMUSG00000033768.
DR MGI; MGI:1096362; Nrxn2.
DR VEuPathDB; HostDB:ENSMUSG00000033768; -.
DR GeneTree; ENSGT00940000155978; -.
DR HOGENOM; CLU_001710_1_0_1; -.
DR InParanoid; E9Q7X7; -.
DR OMA; XHAGIGH; -.
DR PhylomeDB; E9Q7X7; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR ChiTaRS; Nrxn2; mouse.
DR PRO; PR:E9Q7X7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; E9Q7X7; protein.
DR Bgee; ENSMUSG00000033768; Expressed in embryonic brain and 67 other tissues.
DR ExpressionAtlas; E9Q7X7; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; ISA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097109; F:neuroligin family protein binding; IPI:BHF-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0030534; P:adult behavior; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; IDA:BHF-UCL.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IDA:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR GO; GO:0042297; P:vocal learning; ISO:MGI.
DR GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR CDD; cd00110; LamG; 6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1710
FT /note="Neurexin-2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003244492"
FT TOPO_DOM 29..1634
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1635..1655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1656..1710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 29..206
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 202..242
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 289..486
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 493..686
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 690..727
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 732..904
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 918..1093
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1096..1133
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1137..1345
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1458..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1677..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 206..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 213..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 231..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 450..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 657..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 694..705
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 699..714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 716..726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1065..1093
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1100..1111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1105..1120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1122..1132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1710 AA; 184885 MW; FB3DB56946383587 CRC64;
MALGSRWQPP PQLPPLLLLL ALAAGVRGLE FGGGPGQWAR YARWAGAAST GELSFSLRTN
ATRALLLYLD DGGDCDFLEL LLVDGRLRLR FTLSCAEPAT LQLDTPVADD RWHMVLLTRD
ARRTALAVDG EARAAEVRSK RREMQVASDL FVGGIPPDVR LSALTLSTVK YEPPFRGLLA
NLKLGERPPA LLGSQGLRGA AADPLCAPAR NPCANGGLCT VLAPGEVGCD CSHTGFGGKF
CSEEEHPMEG PAHLTLNSEV GSLLFSEGGA GRGGAGDVHQ PTKGKEEFVA TFKGNEFFCY
DLSHNPIQSS TDEITLAFRT LQRNGLMLHT GKSADYVNLS LKSGAVWLVI NLGSGAFEAL
VEPVNGKFND NAWHDVRVTR NLRQHAGIGH AMVNKLHYLV TISVDGILTT TGYTQEDYTM
LGSDDFFYIG GSPNTADLPG SPVSNNFMGC LKDVVYKNND FKLELSRLAK EGDPKMKLQG
DLSFRCEDVA ALDPVTFESP EAFVALPRWS AKRTGSISLD FRTTEPNGLL LFSQGRRAGA
GVGSHSSTQR ADYFAMELLD GYLYLLLDMG SGGIKLRASS RKVNDGEWCH VDFQRDGRKG
SISVNSRSTP FLATGESEVL DLESELYLGG LPEGGRVDLP LPPEVWTAAL RAGYVGCVRD
LFIDGRSRDL RGLAEAQGAV GVAPFCSRET LKQCASAPCR NGGICREGWN RFVCDCIGTG
FLGRVCEREA TVLSYDGSMY MKIMLPTAMH TEAEDVSLRF MSQRAYGLMM ATTSRESADT
LRLELDGGQM RLTVNLDCLR VGCAPSKGPE TLFAGHKLND NEWHTVRVVR RGKSLQLSVD
NVTVEGQMAG AHTRLEFHNI ETGIMTERRF ISVVPSNFIG HLSGLVFNGQ PYMDQCKDGD
ITYCELNARF GLRAIVADPV TFKSRSSYLA LATLQAYASM HLFFQFKTTA PDGLLLFNSG
NGNDFIVIEL VKGYIHYVFD LGNGPSLMKG NSDKPVNDNQ WHNVVVSRDP GNVHTLKIDS
RTVTQHSNGA RNLDLKGELY IGGLSKNMFS NLPKLVASRD GFQGCLASVD LNGRLPDLIA
DALHRIGQVE RGCDGPSTTC TEESCANQGV CLQQWDGFTC DCTMTSYGGP VCNDPGTTYI
FGKGGALITY TWPPNDRPST RMDRLAVGFS THQRSAVLVR VDSASGLGDY LQLHIDQGTV
GVIFNVGTDD ITIDEPNAIV SDGKYHVVRF TRSGGNATLQ VDSWPVNERY PAGNFDNERL
AIARQRIPYR LGRVVDEWLL DKGRQLTIFN SQAAIKIGGR DQGRPFQGQV SGLYYNGLKV
LALAAESDPN VRTEGHLRLV GEGPSVLLSA ETTATTLLAD MATTIMETTT TMATTTTRRG
RSPTMRDSTT QNTDDLLVAS AECPSDDEDL EECEPSTGGE LILPIITEDS LDPPPVATRS
PFVPPPPTFY PFLTGVGATQ DTLPPPAARR PSSGGPCQAE RDDSDCEEPV EASGFASGEV
FDSSLPPTDD EDFYTTFPLV TDRTTLLSPR KPRPNLRTDG ATGAPGVLFA PSAPAPNLPA
GKMNHRDPLQ PLLENPPLGP GVPTAFEPRR PPPLRPGVTS APGFPRLPTA NPTGPGERGP
PGAVEVIRES SSTTGMVVGI VAAAALCILI LLYAMYKYRN RDEGSYQVDQ SRNYISNSAQ
SNGAVVKEKA PAAPKTPSKA KKNKDKEYYV
