ID   NR1AB_DANRE             Reviewed;         449 AA.
AC   A1XQX1;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Neurexin-1a-beta;
DE   AltName: Full=Neurexin Ia-beta;
DE   Flags: Precursor;
GN   Name=nrxn1a;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RX   PubMed=17041151; DOI=10.1093/molbev/msl147;
RA   Rissone A., Monopoli M., Beltrame M., Bussolino F., Cotelli F., Arese M.;
RT   "Comparative genome analysis of the neurexin gene family in Danio rerio:
RT   insights into their functions and evolution.";
RL   Mol. Biol. Evol. 24:236-252(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Masuda Y., Yoshida T., Mishina M.;
RT   "Regulation by beta-neurexin of synaptic vesicle accumulation in axon
RT   terminals of zebrafish olfactory sensory neurons.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC       recognition and cell adhesion. May play a role in formation or
CC       maintenance of synaptic junctions.
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=2;
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.;
CC       Name=Beta;
CC         IsoId=A1XQX1-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=A1XQX0-1; Sequence=External;
CC   -!- DEVELOPMENTAL STAGE: After the very early developmental stages, the
CC       expression levels decrease and remain relatively constant until around
CC       24 h, with the onset of an increase of expression that continues till
CC       the larval stages. {ECO:0000269|PubMed:17041151}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR   EMBL; DQ641425; ABG25162.1; -; mRNA.
DR   EMBL; AB214179; BAG81979.1; -; mRNA.
DR   RefSeq; NP_001333852.1; NM_001346923.1. [A1XQX1-1]
DR   AlphaFoldDB; A1XQX1; -.
DR   SMR; A1XQX1; -.
DR   Ensembl; ENSDART00000088159; ENSDARP00000082592; ENSDARG00000061647. [A1XQX1-1]
DR   GeneID; 565531; -.
DR   CTD; 565531; -.
DR   ZFIN; ZDB-GENE-070206-1; nrxn1a.
DR   GeneTree; ENSGT00940000163749; -.
DR   HOGENOM; CLU_025785_1_0_1; -.
DR   OrthoDB; 35129at2759; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000061647; Expressed in brain and 7 other tissues.
DR   ExpressionAtlas; A1XQX1; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0002040; P:sprouting angiogenesis; IMP:ZFIN.
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   2: Evidence at transcript level;
KW   Alternative promoter usage; Alternative splicing; Cell adhesion; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..449
FT                   /note="Neurexin-1a-beta"
FT                   /id="PRO_0000412538"
FT   TOPO_DOM        39..373
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..449
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          71..272
FT                   /note="Laminin G-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          276..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  48706 MW;  6C828D06A1EA0BF1 CRC64;
     MLRLWPGGAP GGLASILLRI SLRLALWLPP LTLGSALAEG PGELYVPQHM PHHLVPAARS
     HAPLRAGHAG TTYIFGRDGG LIVYTWPPND RPSTRADRLA VGFSTQQKDA VLVRVDSSSG
     LGDYLQLQIE RGNIKVVFNV GTDDINIEET SKFVNDGKYH IVRFTRSGGN ATLQVDDLPV
     IERYPSGNID NERLAIARQR IPYRLGRVVD DWLLDKGRQL TIFNSQTTIK IGGWEKGSRP
     FQGQLSGLYY NGLKVLNMAA EGDPNVRVEG SARLVGDMPS SSITPQSSVS AAGNRSETSP
     SITDITTTTA SNRQGKQTTT PQDDLLVASA ECPSDDEDID PCDPSSGGLA HPPLPEAKGY
     PSPEVIRESS STTGMVVGIV AAAALCILIL LYAMYKYRNR DEGSYHVDES RNYISNSATQ
     PNGAAVKEKP IGVPKNKKDK KNKDKEYYV