NRX1B_CHICK
ID NRX1B_CHICK Reviewed; 466 AA.
AC D0PRN2;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Neurexin-1-beta;
DE AltName: Full=Neurexin I-beta;
DE Flags: Precursor;
GN Name=NRXN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19926856; DOI=10.1073/pnas.0809510106;
RA Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B.,
RA Cera M.R., Mascia L., Bussolino F., Arese M.;
RT "The synaptic proteins neurexins and neuroligins are widely expressed in
RT the vascular system and contribute to its functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion by forming intracellular junctions
CC through binding to neuroligins. May play a role in formation or
CC maintenance of synaptic junctions. May mediate intracellular signaling
CC (By similarity). Plays a role in angiogenesis. {ECO:0000250,
CC ECO:0000269|PubMed:19926856}.
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=10;
CC Comment=A number of isoforms, beta-type and alpha-type are produced
CC by alternative promoter usage. Beta-type isoforms differ from
CC alpha-type isoforms in their N-terminus. Additional isoforms seem to
CC exist. There are probably more than 60 isoforms. There is a
CC combination of five alternatively spliced domains at sites 1 to 5,
CC each consisting of modular sequences that seem to be used
CC independently. Experimental confirmation may be lacking for some
CC isoforms.;
CC Name=1b;
CC IsoId=D0PRN2-1; Sequence=Displayed;
CC Name=1a; Synonyms=Alpha;
CC IsoId=Q9DDD0-1; Sequence=External;
CC Name=2a; Synonyms=Alpha-1,2;
CC IsoId=Q9DDD0-2; Sequence=External;
CC Name=3a; Synonyms=Alpha-1,3;
CC IsoId=Q9DDD0-3; Sequence=External;
CC Name=4a; Synonyms=Alpha-1,4;
CC IsoId=Q9DDD0-4; Sequence=External;
CC Name=5a; Synonyms=Alpha-1,5;
CC IsoId=Q9DDD0-5; Sequence=External;
CC Name=6a; Synonyms=Alpha-2,5;
CC IsoId=Q9DDD0-6; Sequence=External;
CC Name=7a; Synonyms=Alpha-2,8;
CC IsoId=Q9DDD0-7; Sequence=External;
CC Name=8a; Synonyms=Alpha-4,10;
CC IsoId=Q9DDD0-8; Sequence=External;
CC Name=9a; Synonyms=Alpha-5,13;
CC IsoId=Q9DDD0-9; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain and arteries (at protein level).
CC {ECO:0000269|PubMed:19926856}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; EU702427; ACF35428.1; -; mRNA.
DR RefSeq; NP_001185905.1; NM_001198976.1. [D0PRN2-1]
DR AlphaFoldDB; D0PRN2; -.
DR SMR; D0PRN2; -.
DR Ensembl; ENSGALT00000074723; ENSGALP00000049061; ENSGALG00000009107. [D0PRN2-1]
DR GeneID; 395398; -.
DR KEGG; gga:395398; -.
DR CTD; 9378; -.
DR VEuPathDB; HostDB:geneid_395398; -.
DR GeneTree; ENSGT00940000154292; -.
DR OrthoDB; 35129at2759; -.
DR PhylomeDB; D0PRN2; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000009107; Expressed in brain and 9 other tissues.
DR ExpressionAtlas; D0PRN2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 Alternative promoter usage; Alternative splicing; Angiogenesis;
KW Cell adhesion; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..466
FT /note="Neurexin-1-beta"
FT /id="PRO_0000412536"
FT TOPO_DOM 45..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 85..283
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 347..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 49956 MW; E4394F949886C824 CRC64;
MGGFLRGSPE PGPAGGSGGS AGGRLALLWI VPLTLSGLLG VAWGASSLGA HHIHHFHGSS
KHHSVPIAIY RSPASLRGGH AGTTYIFSKG GGQITYTWPP NDRPSTRADR LAIGFSTVQK
EAVLVRVDSS TGLGDYLELH IHQGKIGVKF NVGTDDIAIE EINAIINDGK YHVVRFTRSG
GNATLQVDNW PVIERYPAGN NDNERLAIAR QRIPYRLGRV VDEWLLDKGR QLTIFNSQAT
IKIGGKERGH PFQGQLSGLY YNGLKVLNMA AENDANIVIE GNVRLVGEVP SSMTTESTAT
AMQSEMSTSV METTTTLATS TARRGKAPTK EPIGQTTDDI LVASAECPSD DEDIDPCEPS
SGGLANPTRA GGGREYPGSS EVIRESSSTT GMVVGIVAAA ALCILILLYA MYKYRNRDEG
SYHVDESRNY ISNSAQSNGA VIKEKQPNSA KSSNKNKKNK DKEYYV
