NRX2B_RAT
ID NRX2B_RAT Reviewed; 662 AA.
AC Q63376;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Neurexin-2-beta;
DE AltName: Full=Neurexin II-beta;
DE Flags: Precursor;
GN Name=Nrxn2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1621094; DOI=10.1126/science.1621094;
RA Ushkaryov Y.A., Petrenko A.G., Geppert M., Suedhof T.C.;
RT "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin
RT receptor and laminin.";
RL Science 257:50-56(1992).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS.
RC TISSUE=Brain;
RX PubMed=8163501; DOI=10.1016/s0021-9258(17)32671-6;
RA Ushkaryov Y.A., Hata Y., Ichtchenko K., Moomaw C., Afendis S.,
RA Slaughter C.A., Suedhof T.C.;
RT "Conserved domain structure of beta-neurexins. Unusual cleaved signal
RT sequences in receptor-like neuronal cell-surface proteins.";
RL J. Biol. Chem. 269:11987-11992(1994).
RN [3]
RP INTERACTION WITH CASK.
RX PubMed=8786425; DOI=10.1523/jneurosci.16-08-02488.1996;
RA Hata Y., Butz S., Suedhof T.C.;
RT "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent
RT protein kinase domain identified by interaction with neurexins.";
RL J. Neurosci. 16:2488-2494(1996).
RN [4]
RP INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
RX PubMed=8576240; DOI=10.1074/jbc.271.5.2676;
RA Ichtchenko K., Nguyen T., Suedhof T.C.;
RT "Structures, alternative splicing, and neurexin binding of multiple
RT neuroligins.";
RL J. Biol. Chem. 271:2676-2682(1996).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion.
CC -!- SUBUNIT: The cytoplasmic C-terminal region binds to CASK. Isoforms Beta
CC 4b bind alpha-dystroglycan and neuroligins NLGN1, NLGN2 and NLGN3.
CC Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=18;
CC Comment=Two isoform types, alpha-type and beta-type are produced by
CC alternative promoter usage. In addition there are at least five major
CC alternatively spliced sites, each of which may be spliced in up to
CC three different ways. Additional isoforms may derive from a minor
CC cytoplasmic splice site 6. Combinatorial splicing at each of these
CC six sites may lead to the generation of at least 216 isoforms but for
CC simplicity only individual splice events are explicitly described
CC below. Beta-type isoforms share the possibility of alternative
CC splicing at sites 4, 5 and 6. Experimental confirmation may be
CC lacking for some isoforms.;
CC Name=1b; Synonyms=Beta-4A5A;
CC IsoId=Q63376-1; Sequence=Displayed;
CC Name=2b; Synonyms=Beta-4A5B;
CC IsoId=Q63376-2; Sequence=VSP_003519;
CC Name=3b; Synonyms=Beta-4B5A;
CC IsoId=Q63376-3; Sequence=VSP_003518;
CC Name=4b; Synonyms=Beta-4B5B;
CC IsoId=Q63376-4; Sequence=VSP_003518, VSP_003519;
CC Name=5b; Synonyms=Beta-4A5A6;
CC IsoId=Q63376-5; Sequence=VSP_003520;
CC Name=6b; Synonyms=Beta-4A5B6;
CC IsoId=Q63376-6; Sequence=VSP_003519, VSP_003520;
CC Name=7b; Synonyms=Beta-4B5A6;
CC IsoId=Q63376-7; Sequence=VSP_003518, VSP_003520;
CC Name=8b; Synonyms=Beta-4B5B6;
CC IsoId=Q63376-8; Sequence=VSP_003518, VSP_003519, VSP_003520;
CC Name=1a; Synonyms=Alpha-1A2A3A4A5A;
CC IsoId=Q63374-1; Sequence=External;
CC Name=2a; Synonyms=Alpha-1B;
CC IsoId=Q63374-2; Sequence=External;
CC Name=3a; Synonyms=Alpha-1C;
CC IsoId=Q63374-3; Sequence=External;
CC Name=4a; Synonyms=Alpha-2B;
CC IsoId=Q63374-4; Sequence=External;
CC Name=5a; Synonyms=Alpha-2C;
CC IsoId=Q63374-5; Sequence=External;
CC Name=6a; Synonyms=Alpha-3B;
CC IsoId=Q63374-6; Sequence=External;
CC Name=7a; Synonyms=Alpha-3C;
CC IsoId=Q63374-7; Sequence=External;
CC Name=8a; Synonyms=Alpha-4B;
CC IsoId=Q63374-8; Sequence=External;
CC Name=9a; Synonyms=Alpha-5B;
CC IsoId=Q63374-9; Sequence=External;
CC Name=10a; Synonyms=Alpha-6;
CC IsoId=Q63374-10; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain (neuronal synapse).
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; M96377; AAA41708.1; -; mRNA.
DR PIR; D40228; D40228.
DR RefSeq; XP_008758286.1; XM_008760064.2. [Q63376-1]
DR PDB; 3MW3; X-ray; 2.33 A; A=87-290.
DR PDBsum; 3MW3; -.
DR AlphaFoldDB; Q63376; -.
DR SMR; Q63376; -.
DR BioGRID; 250509; 4.
DR IntAct; Q63376; 1.
DR MINT; Q63376; -.
DR PRIDE; Q63376; -.
DR Ensembl; ENSRNOT00000028651; ENSRNOP00000028651; ENSRNOG00000021103. [Q63376-1]
DR GeneID; 116595; -.
DR UCSC; RGD:620211; rat. [Q63376-1]
DR CTD; 9379; -.
DR RGD; 620211; Nrxn2.
DR GeneTree; ENSGT00940000155978; -.
DR HOGENOM; CLU_025785_2_0_1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021103; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; Q63376; baseline and differential.
DR Genevisible; Q63376; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0097109; F:neuroligin family protein binding; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISO:RGD.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISO:RGD.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0042297; P:vocal learning; ISO:RGD.
DR GO; GO:0071625; P:vocalization behavior; ISO:RGD.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Cell adhesion; Direct protein sequencing; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..46
FT /evidence="ECO:0000269|PubMed:8163501"
FT CHAIN 47..662
FT /note="Neurexin-2-beta"
FT /id="PRO_0000019498"
FT TOPO_DOM 47..586
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 87..295
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 203..232
FT /note="Missing (in isoform 3b, isoform 4b, isoform 7b and
FT isoform 8b)"
FT /evidence="ECO:0000305"
FT /id="VSP_003518"
FT VAR_SEQ 368..385
FT /note="Missing (in isoform 2b, isoform 4b, isoform 6b and
FT isoform 8b)"
FT /evidence="ECO:0000305"
FT /id="VSP_003519"
FT VAR_SEQ 614..662
FT /note="DEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV ->
FT CRKSPREEKLLPGSAQGLGLDLAKACCVCRCRATCIAGKPLEERGGGRGEGERQMQIYI
FT KNK (in isoform 5b, isoform 6b, isoform 7b and isoform 8b)"
FT /evidence="ECO:0000305"
FT /id="VSP_003520"
SQ SEQUENCE 662 AA; 70547 MW; A362EFF185F2B56E CRC64;
MPPGGSGQGG CPRRPPALAG PLPPPPPPPP LPLLLGLLLL LGAAEGARVS SSLSTTHHVH
HFHSKHGTVP IAINRMPFLT RSGHAGTTYI 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
KPAPRPNLRT DGATGAPGVL LAPSAPAPNL PAGKMNHRDP LQPLLENPPL GPGVPTAFEP
RRPPPLRPGV TSVPGFPRLP TANPTGPGER GPPGAVEVIR ESSSTTGMVV GIVAAAALCI
LILLYAMYKY RNRDEGSYQV DQSRNYISNS AQSNGAVVKE KAPAAPKTPS KAKKNKDKEY
YV
