NRX3B_CHICK
ID NRX3B_CHICK Reviewed; 668 AA.
AC D0PRN4; D0PRN5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Neurexin-3-beta;
DE AltName: Full=Neurexin III-beta;
DE Contains:
DE RecName: Full=Neurexin-3-beta, soluble form;
DE Contains:
DE RecName: Full=Neurexin-3-beta, C-terminal fragment;
DE Short=NRXN3-CTF;
DE Flags: Precursor;
GN Name=NRXN3;
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] (ISOFORMS 1B AND 2B), FUNCTION, AND TISSUE
RP 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 similarity). Plays a role in
CC angiogenesis. {ECO:0000250, 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=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.;
CC Name=1b;
CC IsoId=D0PRN4-1; Sequence=Displayed;
CC Name=2b;
CC IsoId=D0PRN4-2; Sequence=VSP_041705;
CC Name=1a;
CC IsoId=D0PRN3-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain and arteries (at protein level).
CC {ECO:0000269|PubMed:19926856}.
CC -!- PTM: Proccessed by alpha-secretase leading to the formation of an
CC extracellular soluble protein as well as a C-terminal membrane-embedded
CC fragment (CTF). Proteolysis of these CTFs by gamma-secretase releases
CC intracellular domains (ICDs) and extracellular peptides (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1b]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2b]: Produced by alternative splicing of
CC isoform 1b. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; EU702429; ACF35430.1; -; mRNA.
DR EMBL; EU702430; ACF35431.1; -; mRNA.
DR RefSeq; NP_001258853.1; NM_001271924.1. [D0PRN4-1]
DR RefSeq; NP_001258854.1; NM_001271925.1. [D0PRN4-2]
DR AlphaFoldDB; D0PRN4; -.
DR SMR; D0PRN4; -.
DR STRING; 9031.ENSGALP00000017108; -.
DR Ensembl; ENSGALT00000059499; ENSGALP00000052761; ENSGALG00000027255. [D0PRN4-1]
DR GeneID; 423385; -.
DR CTD; 9369; -.
DR VEuPathDB; HostDB:geneid_423385; -.
DR eggNOG; KOG3514; Eukaryota.
DR GeneTree; ENSGT00940000154618; -.
DR InParanoid; D0PRN4; -.
DR OrthoDB; 35129at2759; -.
DR PhylomeDB; D0PRN4; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000027255; Expressed in cerebellum and 3 other tissues.
DR ExpressionAtlas; D0PRN4; 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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..668
FT /note="Neurexin-3-beta"
FT /id="PRO_0000412546"
FT CHAIN 36..578
FT /note="Neurexin-3-beta, soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412547"
FT CHAIN 579..668
FT /note="Neurexin-3-beta, C-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000412548"
FT TOPO_DOM 36..593
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 84..284
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 358..360
FT /note="Missing (in isoform 2b)"
FT /evidence="ECO:0000303|PubMed:19926856"
FT /id="VSP_041705"
SQ SEQUENCE 668 AA; 72893 MW; F215CBB466C57E69 CRC64;
MHLRTNPSIC PGRRPAWTLW MCSLFWGCIV SSVWSSSNVA SSASSSSSVS QAQYEHHFHG
SKHHSVPISI YRSPVSLRGG HAGATYIFGK SGGLILYTWP ANDRPSTRTD RLAVGFSTTV
KDGILVRIDS APGLGDFLQL HIEQGKIGVV FNIGTVDISI KEESTPVNDG KYHVVRFTRN
GGNATLQVDS WPVNEHYPTG NTDSERFQMV KQKIPFKYNR PVEEWLQEKG RQLTIFNTQA
QIAIGGKDRG RLFQGQLSGL YYNGLKVLNM AAENNPNIKI NGSVRLVGEV PSILGTTPTT
SVPPEMSTTV METTTTMATT TTRKNRSPPS IQTTDDIVSS AECSSDDEDF IDCEPSTGKS
GGELVIPLLV EDPLDIPPIA TRAPFITLPP TFRPLLTIIE TTKDSLSMTS EAGLPCLSDQ
GSDGCDDDGL VISGYGSGET FDSNLPPTDD EDFYTTFSLV TDKSLSTSIF EGGYKAHAPK
WESKDFRPNK VSETGRTTTT SLSPELIRST ASSSTGMVPK LPAGKMNNRE LKPQPDIVLL
PLPTAYELDS TKLKSPLITS PMFRNVPTAN PTEPGIRRVP GASEVVRESS STTGMVVGIV
AAAALCILIL LYAMYKYRNR DEGSYQVDET RNYISNSAQS NGTLMKEKQQ SSKSGHKKQK
NKDKEYYV
