NRX1B_BOVIN
ID NRX1B_BOVIN Reviewed; 467 AA.
AC Q28142;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Neurexin-1-beta {ECO:0000250|UniProtKB:P58400};
DE AltName: Full=Neurexin I-beta;
DE Flags: Precursor;
GN Name=NRXN1 {ECO:0000250|UniProtKB:P58400};
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 1B; 2B; 3B AND 4B).
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 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 May play a role in angiogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The cytoplasmic C-terminal region binds to CASK. Binds NLGN1,
CC NLGN2 and NLGN3, DAG1 (alpha-dystroglycan) and alpha-latrotoxin.
CC Binding to neuroligins is calcium-dependent, and the binding preference
CC ranks as follow: NLGN1 > NLGN4 >> NLGN3 > NLGN2 (By similarity).
CC Interacts CBLN2 and more weakly with CBLN4 (By similarity). Interacts
CC with CBLN1; interaction is CBLN1 hexamer form-dependent; CBLN1-binding
CC is calcium-independent; isoform 1b does not interact with CBLN1 (By
CC similarity). {ECO:0000250|UniProtKB:P0DI97,
CC ECO:0000250|UniProtKB:P58400, ECO:0000250|UniProtKB:Q63373}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q63373}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q63373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=16;
CC Comment=A number of isoforms alpha-type and beta-type are produced by
CC alternative promoter usage. Beta-type isoforms differ from alpha-type
CC isoforms in their N-terminus. In addition, there are at least five
CC alternatively spliced sites, each of which may be spliced in up to
CC seven different ways. Combinatorial splicing at each of these sites
CC may lead to the generation of at least 96 isoforms. Experimental
CC confirmation may be lacking for some isoforms.;
CC Name=1b; Synonyms=Beta-4A5A;
CC IsoId=Q28142-1; Sequence=Displayed;
CC Name=2b; Synonyms=Beta-4A5B;
CC IsoId=Q28142-2; Sequence=VSP_003495;
CC Name=3b; Synonyms=Beta-4B5A;
CC IsoId=Q28142-3; Sequence=VSP_003494;
CC Name=4b; Synonyms=Beta-4B5B;
CC IsoId=Q28142-4; Sequence=VSP_003494, VSP_003495;
CC Name=1a; Synonyms=Alpha-1A2A3A4A5A;
CC IsoId=Q28146-1; Sequence=External;
CC Name=2a; Synonyms=Alpha-1B;
CC IsoId=Q28146-2; Sequence=External;
CC Name=3a; Synonyms=Alpha-1C;
CC IsoId=Q28146-3; Sequence=External;
CC Name=4a; Synonyms=Alpha-1D;
CC IsoId=Q28146-4; Sequence=External;
CC Name=5a; Synonyms=Alpha-1E;
CC IsoId=Q28146-5; Sequence=External;
CC Name=6a; Synonyms=Alpha-1F;
CC IsoId=Q28146-6; Sequence=External;
CC Name=7a; Synonyms=Alpha-1G;
CC IsoId=Q28146-7; Sequence=External;
CC Name=8a; Synonyms=Alpha-2B;
CC IsoId=Q28146-8; Sequence=External;
CC Name=9a; Synonyms=Alpha-2C;
CC IsoId=Q28146-9; Sequence=External;
CC Name=10a; Synonyms=Alpha-3B;
CC IsoId=Q28146-10; Sequence=External;
CC Name=11a; Synonyms=Alpha-4B;
CC IsoId=Q28146-11; Sequence=External;
CC Name=12a; Synonyms=Alpha-5B;
CC IsoId=Q28146-12; Sequence=External;
CC -!- PTM: Highly O-glycosylated and minor N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; L27870; AAA19906.1; -; mRNA.
DR RefSeq; NP_001103275.1; NM_001109805.2. [Q28142-3]
DR PDB; 3VKF; X-ray; 3.30 A; C/D=83-290.
DR PDBsum; 3VKF; -.
DR AlphaFoldDB; Q28142; -.
DR SMR; Q28142; -.
DR STRING; 9913.ENSBTAP00000053932; -.
DR GeneID; 281950; -.
DR CTD; 9378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 Angiogenesis; Calcium; Cell adhesion; Cell membrane; Cell projection;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..45
FT /evidence="ECO:0000250"
FT CHAIN 46..467
FT /note="Neurexin-1-beta"
FT /id="PRO_0000019492"
FT TOPO_DOM 46..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 86..284
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 200..229
FT /note="Essential for interaction with CBLN1; modulates
FT interaction affinity with NLGN1, NLGN2 and NLGN3; prevents
FT interaction with DAG1/alpha-dystroglycan; modulates
FT interaction with alpha-latrotoxin"
FT /evidence="ECO:0000250|UniProtKB:P58400,
FT ECO:0000250|UniProtKB:Q63373"
FT REGION 318..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58400"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 201..230
FT /note="Missing (in isoform 3b and isoform 4b)"
FT /evidence="ECO:0000303|PubMed:8163501"
FT /id="VSP_003494"
FT VAR_SEQ 363..365
FT /note="Missing (in isoform 2b and isoform 4b)"
FT /evidence="ECO:0000303|PubMed:8163501"
FT /id="VSP_003495"
FT STRAND 86..98
FT /evidence="ECO:0007829|PDB:3VKF"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 107..118
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:3VKF"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:3VKF"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:3VKF"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:3VKF"
SQ SEQUENCE 467 AA; 50084 MW; 70D281E2510AB21E CRC64;
MYQRMLRCGA ELGSPGGGGG GAGGRLALLW IVPLTLSGLL GVAWGASSLG AHHIHHFHGS
SKHHSVPIAI YRSPASLRGG HAGTTYIFSK GGGQITYKWP PNDRPSTRAD RLAIGFSTVQ
KEAVLVRVDS SSGLGDYLEL HIHQGKIGVK FNVGTDDIAI EESNAIINDG KYHVVRFTRS
GGNATLQVDS WPVIERYPAG NNDNERLAIA RQRIPYRLGR VVDEWLLDKG RQLTIFNSQA
TIIIGGKEQG QPFQGQLSGL YYNGLKVLNM AAENDANIAI VGNVRLVGEV PSSMTTESTA
TAMQSEMSTS IMETTTTLAT STARRGNSPT KEPVSQTTDD ILVASAECPS DDEDIDPCEP
SSGGLANPTR AGGREPYPGS AEVIRESSST TGMVVGIVAA AALCILILLY AMYKYRNRDE
GSYHVDESRN YISNSAQSNG AVVKEKQPSS AKSANKNKKN KDKEYYV
