ID NRX3B_BOVIN Reviewed; 456 AA.
AC Q28143; Q28144;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 24-JAN-2024, entry version 142.
DE RecName: Full=Neurexin-3-beta;
DE AltName: Full=Neurexin III-beta;
DE Contains:
DE RecName: Full=Neurexin-3-beta, soluble form {ECO:0000250|UniProtKB:Q9HDB5};
DE Contains:
DE RecName: Full=Neurexin-3-beta, C-terminal fragment {ECO:0000250|UniProtKB:Q9HDB5};
DE Short=NRXN3-CTF;
DE Flags: Precursor;
GN Name=NRXN3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND PROTEIN SEQUENCE
RP 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).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion. May mediate intracellular signaling (By
CC similarity). {ECO:0000250|UniProtKB:Q9CS84}.
CC -!- SUBUNIT: Weakly interacts with CBLN1 and CBLN2 (By similarity). Very
CC weak binding, if any, with CBLN4 (By similarity). Specific isoforms
CC bind neuroligins NLGN1, NLGN2 and NLGN3 (By similarity). Interacts with
CC CLSTN3 (By similarity). {ECO:0000250|UniProtKB:Q63376,
CC ECO:0000250|UniProtKB:Q8C985}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Presynaptic cell membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Presynaptic cell membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist. There is a combination of
CC two alternatively spliced domains at sites 4 and 5, which seem to be
CC used independently. Experimental confirmation may be lacking for some
CC isoforms.;
CC Name=1;
CC IsoId=Q28143-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28143-2; Sequence=VSP_003533;
CC Name=3;
CC IsoId=Q28143-3; Sequence=VSP_003534;
CC Name=4;
CC IsoId=Q28143-4; Sequence=VSP_003533, VSP_003534;
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|UniProtKB:Q9HDB5}.
CC -!- PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate
CC attachment is required for synapse development by mediating
CC interactions with neuroligins. {ECO:0000250|UniProtKB:Q8C985}.
CC -!- MISCELLANEOUS: [Isoform 3]: Lacks the transmembrane domain.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Lacks the transmembrane domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19908.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L27869; AAA19907.1; -; mRNA.
DR EMBL; L27869; AAA19908.1; ALT_INIT; mRNA.
DR PIR; A53580; A53580.
DR PIR; B53580; B53580.
DR AlphaFoldDB; Q28143; -.
DR SMR; Q28143; -.
DR STRING; 9913.ENSBTAP00000052163; -.
DR GlyCosmos; Q28143; 3 sites, No reported glycans.
DR Ensembl; ENSBTAT00000022474.6; ENSBTAP00000022474.6; ENSBTAG00000025324.5. [Q28143-3]
DR Ensembl; ENSBTAT00000022475.6; ENSBTAP00000022475.6; ENSBTAG00000025324.5. [Q28143-2]
DR VEuPathDB; HostDB:ENSBTAG00000025324; -.
DR GeneTree; ENSGT00940000163749; -.
DR InParanoid; Q28143; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000025324; Expressed in prefrontal cortex and 23 other cell types or tissues.
DR ExpressionAtlas; Q28143; baseline.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 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 PANTHER; PTHR15036:SF57; NEUREXIN-3; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
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; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Calcium; Cell adhesion; Cell membrane;
KW Cell projection; Direct protein sequencing; Glycoprotein; Heparan sulfate;
KW Membrane; Metal-binding; Proteoglycan; Reference proteome; Repeat;
KW Secreted; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:8163501"
FT CHAIN 36..456
FT /note="Neurexin-3-beta"
FT /id="PRO_0000019501"
FT CHAIN 36..369
FT /note="Neurexin-3-beta, soluble form"
FT /evidence="ECO:0000250|UniProtKB:Q9HDB5"
FT /id="PRO_0000412541"
FT CHAIN 370..456
FT /note="Neurexin-3-beta, C-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:Q9HDB5"
FT /id="PRO_0000412542"
FT TOPO_DOM 36..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 82..282
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 41..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q63373"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q63373"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q63373"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q63373"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:Q8C985"
FT VAR_SEQ 198..227
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8163501"
FT /id="VSP_003533"
FT VAR_SEQ 357..456
FT /note="ANPTEPGVRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT DEGSYQVDETRNYISNSAQSNGTLLKEKPPSSKGGHKKQKNKDKEYYV -> ARSSNAA
FT RSLRAALTWTWRLTYTFTPIIFISCVVHS (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8163501"
FT /id="VSP_003534"
SQ SEQUENCE 456 AA; 50244 MW; E1B5467089A8CF2C CRC64;
MHLRIHARRN PPRRPAWTLG IWSLFWGCIV SSVWSSSNVA SSSSSPGSHS QHEHHFHGSK
HHSVPISIYR SPVSLRGGHA GATYIFGKSG GLILYTWPAN DRPSTRSDRL AVGFSTTVKD
GILVRIDSAP GLGDFLQLHI EQGKIGVVFN IGTVDISIKE ERTPVNDGKY HVVRFTRNGG
NATLQVDNWP VNEHYPTGNT DNERFQMVKQ KIPFKYNRPV EEWLQEKGRQ LTIFNTQAQI
AIGGKDKGRL FQGQLSGLYY DGLKVLNMAA ENNPNIKING SVRLVGEVPS ILGTTQTTSM
PPEMSTTVME TTTTMATTTT RKNRSTASIQ PTSDDLVSSA ECSSDDEDFV ECEPSTANPT
EPGVRRVPGA SEVIRESSST TGMVVGIVAA AALCILILLY AMYKYRNRDE GSYQVDETRN
YISNSAQSNG TLLKEKPPSS KGGHKKQKNK DKEYYV
//
