NRX2B_HUMAN
ID NRX2B_HUMAN Reviewed; 666 AA.
AC P58401;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Neurexin-2-beta;
DE AltName: Full=Neurexin II-beta;
DE Flags: Precursor;
GN Name=NRXN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-666.
RA Rowen L., Madan A., Qin S., Baradarani L., Birditt B., Bloom S., Burke J.,
RA Dors M., Fleetwood P., Kaur A., Madan A., Nesbitt R., Pate D., Hood L.;
RT "Sequencing of human neurexin II gene.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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. Specific
CC isoforms bind alpha-dystroglycan and neuroligins NLGN1, NLGN2 and NLGN3
CC (By similarity). Interacts with CBLN1, CBLN2 and, less avidly, with
CC CBLN4 (By 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=3;
CC Comment=A number of isoforms, alpha-type and beta-type are produced
CC by alternative promoter usage. Beta-type isoforms differ from
CC alpha-type isoforms in their N-terminus. Additional isoforms produced
CC by alternative splicing seem to exist.;
CC Name=1b;
CC IsoId=P58401-1; Sequence=Displayed;
CC Name=1a;
CC IsoId=Q9P2S2-1; Sequence=External;
CC Name=2a; Synonyms=Alpha-2B;
CC IsoId=Q9P2S2-2; Sequence=External;
CC -!- DOMAIN: Alternative splicing in the laminin G-like domain regulates
CC binding to alpha-dystroglycan.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; AP001092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC044790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS8078.1; -. [P58401-1]
DR RefSeq; NP_620063.1; NM_138734.2. [P58401-1]
DR PDB; 4NXR; X-ray; 1.90 A; B=659-666.
DR PDBsum; 4NXR; -.
DR AlphaFoldDB; P58401; -.
DR SMR; P58401; -.
DR BioGRID; 114780; 6.
DR IntAct; P58401; 1.
DR MINT; P58401; -.
DR BioMuta; NRXN2; -.
DR DMDM; 17368287; -.
DR MassIVE; P58401; -.
DR PeptideAtlas; P58401; -.
DR PRIDE; P58401; -.
DR ProteomicsDB; 57072; -. [P58401-1]
DR TopDownProteomics; P58401-1; -. [P58401-1]
DR Antibodypedia; 63686; 48 antibodies from 7 providers.
DR DNASU; 9379; -.
DR Ensembl; ENST00000301894.6; ENSP00000301894.2; ENSG00000110076.20. [P58401-1]
DR GeneID; 9379; -.
DR UCSC; uc001oap.3; human. [P58401-1]
DR CTD; 9379; -.
DR DisGeNET; 9379; -.
DR GeneCards; NRXN2; -.
DR HGNC; HGNC:8009; NRXN2.
DR HPA; ENSG00000110076; Tissue enhanced (brain).
DR MIM; 600566; gene.
DR neXtProt; NX_P58401; -.
DR OpenTargets; ENSG00000110076; -.
DR PharmGKB; PA31787; -.
DR VEuPathDB; HostDB:ENSG00000110076; -.
DR GeneTree; ENSGT00940000155978; -.
DR HOGENOM; CLU_025785_2_0_1; -.
DR OrthoDB; 35129at2759; -.
DR PathwayCommons; P58401; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; P58401; -.
DR SIGNOR; P58401; -.
DR BioGRID-ORCS; 9379; 12 hits in 1069 CRISPR screens.
DR ChiTaRS; NRXN2; human.
DR GeneWiki; NRXN2; -.
DR GenomeRNAi; 9379; -.
DR Pharos; P58401; Tbio.
DR Proteomes; UP000005640; Chromosome 11.
DR Bgee; ENSG00000110076; Expressed in right hemisphere of cerebellum and 137 other tissues.
DR ExpressionAtlas; P58401; baseline and differential.
DR Genevisible; P58401; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0050839; F:cell adhesion molecule binding; TAS:BHF-UCL.
DR GO; GO:0097109; F:neuroligin family protein binding; TAS:BHF-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; TAS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; NAS:BHF-UCL.
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; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..50
FT /evidence="ECO:0000250"
FT CHAIN 51..666
FT /note="Neurexin-2-beta"
FT /id="PRO_0000019497"
FT TOPO_DOM 51..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 91..299
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 660..665
FT /evidence="ECO:0007829|PDB:4NXR"
SQ SEQUENCE 666 AA; 70927 MW; FD0B2FD353F63C6C CRC64;
MPPGGSGPGG CPRRPPALAG PLPPPPPPPP PPLLPLLPLL LLLLLGAAEG ARVSSSLSTT
HHVHHFHSKH GTVPIAINRM PFLTRGGHAG TTYIFGKGGA LITYTWPPND RPSTRMDRLA
VGFSTHQRSA VLVRVDSASG LGDYLQLHID QGTVGVIFNV GTDDITIDEP NAIVSDGKYH
VVRFTRSGGN ATLQVDSWPV NERYPAGNFD NERLAIARQR IPYRLGRVVD EWLLDKGRQL
TIFNSQAAIK IGGRDQGRPF QGQVSGLYYN GLKVLALAAE SDPNVRTEGH LRLVGEGPSV
LLSAETTATT LLADMATTIM ETTTTMATTT TRRGRSPTLR DSTTQNTDDL LVASAECPSD
DEDLEECEPS TGGELILPII TEDSLDPPPV ATRSPFVPPP PTFYPFLTGV GATQDTLPPP
AARRPPSGGP CQAERDDSDC EEPIEASGFA SGEVFDSSLP PTDDEDFYTT FPLVTDRTTL
LSPRKPAPRP NLRTDGATGA PGVLFAPSAP APNLPAGKMN HRDPLQPLLE NPPLGPGAPT
SFEPRRPPPL RPGVTSAPGF PHLPTANPTG PGERGPPGAV EVIRESSSTT GMVVGIVAAA
ALCILILLYA MYKYRNRDEG SYQVDQSRNY ISNSAQSNGA VVKEKAPAAP KTPSKAKKNK
DKEYYV
