NRX1A_CHICK
ID NRX1A_CHICK Reviewed; 1363 AA.
AC Q9DDD0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Neurexin-1;
DE AltName: Full=Neurexin I-alpha;
DE AltName: Full=Neurexin-1-alpha;
DE Flags: Fragment;
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] (ISOFORMS 1A; 2A; 3A; 4A; 5A; 6A; 7A; 8A AND
RP 9A).
RC TISSUE=Sympathetic ganglion;
RX PubMed=10860582; DOI=10.1006/mcne.2000.0853;
RA Patzke H., Ernsberger U.;
RT "Expression of neurexin I alpha splice variants in sympathetic neurons:
RT selective changes during differentiation and in response to
RT neurotrophins.";
RL Mol. Cell. Neurosci. 15:561-572(2000).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion. May mediate intracellular signaling.
CC -!- SUBUNIT: The cytoplasmic C-terminal region binds to CASK. The laminin
CC G-like domain 1 binds to NXPH1. Specific isoforms bind to alpha-
CC dystroglycan and to alpha-latrotoxin (By similarity). {ECO:0000250}.
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=1a; Synonyms=Alpha;
CC IsoId=Q9DDD0-1; Sequence=Displayed;
CC Name=2a; Synonyms=Alpha-1,2;
CC IsoId=Q9DDD0-2; Sequence=VSP_003500;
CC Name=3a; Synonyms=Alpha-1,3;
CC IsoId=Q9DDD0-3; Sequence=VSP_003499;
CC Name=4a; Synonyms=Alpha-1,4;
CC IsoId=Q9DDD0-4; Sequence=VSP_003499, VSP_003500;
CC Name=5a; Synonyms=Alpha-1,5;
CC IsoId=Q9DDD0-5; Sequence=VSP_003498;
CC Name=6a; Synonyms=Alpha-2,5;
CC IsoId=Q9DDD0-6; Sequence=VSP_003502;
CC Name=7a; Synonyms=Alpha-2,8;
CC IsoId=Q9DDD0-7; Sequence=VSP_003501;
CC Name=8a; Synonyms=Alpha-4,10;
CC IsoId=Q9DDD0-8; Sequence=VSP_003503;
CC Name=9a; Synonyms=Alpha-5,13;
CC IsoId=Q9DDD0-9; Sequence=VSP_003504;
CC Name=1b;
CC IsoId=D0PRN2-1; Sequence=External;
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; AJ300473; CAC17606.1; -; mRNA.
DR AlphaFoldDB; Q9DDD0; -.
DR SMR; Q9DDD0; -.
DR STRING; 9031.ENSGALP00000014816; -.
DR PaxDb; Q9DDD0; -.
DR VEuPathDB; HostDB:geneid_395398; -.
DR eggNOG; KOG3514; Eukaryota.
DR InParanoid; Q9DDD0; -.
DR OrthoDB; 35129at2759; -.
DR PhylomeDB; Q9DDD0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 5.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; SSF49899; 5.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 2: Evidence at transcript level;
KW Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN <1..1363
FT /note="Neurexin-1"
FT /id="PRO_0000220496"
FT TOPO_DOM <1..1287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1288..1308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1309..1363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 67..105
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 132..329
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 336..528
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 532..569
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 574..747
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 761..936
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 939..976
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 982..1180
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1244..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..83
FT /evidence="ECO:0000250"
FT DISULFID 77..92
FT /evidence="ECO:0000250"
FT DISULFID 94..104
FT /evidence="ECO:0000250"
FT DISULFID 293..329
FT /evidence="ECO:0000250"
FT DISULFID 499..528
FT /evidence="ECO:0000250"
FT DISULFID 536..547
FT /evidence="ECO:0000250"
FT DISULFID 541..556
FT /evidence="ECO:0000250"
FT DISULFID 558..568
FT /evidence="ECO:0000250"
FT DISULFID 908..936
FT /evidence="ECO:0000250"
FT DISULFID 943..954
FT /evidence="ECO:0000250"
FT DISULFID 948..963
FT /evidence="ECO:0000250"
FT DISULFID 965..975
FT /evidence="ECO:0000250"
FT VAR_SEQ 106..126
FT /note="Missing (in isoform 5a)"
FT /evidence="ECO:0000303|PubMed:10860582"
FT /id="VSP_003498"
FT VAR_SEQ 106..111
FT /note="Missing (in isoform 3a and isoform 4a)"
FT /evidence="ECO:0000303|PubMed:10860582"
FT /id="VSP_003499"
FT VAR_SEQ 123..126
FT /note="Missing (in isoform 2a and isoform 4a)"
FT /evidence="ECO:0000303|PubMed:10860582"
FT /id="VSP_003500"
FT VAR_SEQ 228..242
FT /note="Missing (in isoform 7a)"
FT /evidence="ECO:0000303|PubMed:10860582"
FT /id="VSP_003501"
FT VAR_SEQ 236..242
FT /note="Missing (in isoform 6a)"
FT /evidence="ECO:0000303|PubMed:10860582"
FT /id="VSP_003502"
FT VAR_SEQ 1096..1125
FT /note="Missing (in isoform 8a)"
FT /evidence="ECO:0000303|PubMed:10860582"
FT /id="VSP_003503"
FT VAR_SEQ 1259..1261
FT /note="Missing (in isoform 9a)"
FT /evidence="ECO:0000303|PubMed:10860582"
FT /id="VSP_003504"
FT NON_TER 1
SQ SEQUENCE 1363 AA; 150076 MW; F16374F884D20713 CRC64;
SKRRDMTVFS GLFLGGLPPE LRSATLKLTL SSVKDREPFK GWITDVRVNY TQTSPVESQE
VRLDDEQSRL CAREDVCLNG GVCSVLNDQA VCDCSQTGFR GKDCSEEDNY VEGLAHLMMG
DQGKSKGKEE YIATFKGSEY FCYDLSQNPI QSSSDEITLS FKTLQRNGLM LHTGKSADYV
NLALKNGAVS LVINLGSGAF EALVEPVNGK FNDNAWHDVK VTRNLRQHSG IGHAMVNKLH
CSVTISVDGI LTTTGYTQED YTMLGSDDFF YVGGSPSTAD LPGSPVSNNF MGCLKEVVYK
NNDVRLELSR LAKQGDPKMK IHGVVAFKCE NVATLDPITF ETPESFISLP KWNAKKTGSI
SFDFRTTEPN GLILFSHGKP RHQKDAKHPQ MVKVDFFAIE MLDGHLYLLL DMGSGTIKIK
ALQKKVNDGE WYHVDFQRDG RSGTISVNTL RTPYTAPGES EILDLDDDLY LGGLPENKAG
LVFPTEVWTA LLNYGYVGCI RDLFIDGQSK DIRQMAEIQS TAGVKPSCSR ETAKPCLSNP
CKNNGVCRDG WNRYVCDCSG TGYLGRSCER EATILSYDGS MFMKIQLPVV MHTEAEDVSL
RFRSQRAYGI LMATTSRESA DTLRLELDAG RVKLTVNLDC IRINCNSSKG PETLFAGYNL
NDNEWHTVRV VRRGKSLKLM VDDQQAMTGQ MAGDHTRLEF HNIETGIITE RRYLSSVPSN
FIGHLQSLTF NGMAYIDLCK NGDIDYCELN ARFGFRNIIA DPVTFKTKAS YVALATLQAY
TSMHLFFQFK TTSLDGLILY NSGDGNDFIV VELVKGYLHY VFDLGNGANL IKGSSNKPLN
DNQWHNVMIS RDTNNLHTVK IDTKITTQST AGARNLDLKS DLYIGGVAKE MYKSLPKLVH
AKEGFQGCLA SVDLNGRLPD LISDALFCNG QIERGCEGPS TTCQEDSCAN QGVCLQQWDG
FSCDCSMTSF SGPLCNDPGT TYIFSKGGGQ ITYTWPPNDR PSTRADRLAI GFSTVQKEAV
LVRVDSSTGL GDYLELHIHQ GKIGVKFNVG TDDIAIEEIN AIINDGKYHV VRFTRSGGNA
TLQVDNWPVI ERYPAGNNDN ERLAIARQRI PYRLGRVVDE WLLDKGRQLT IFNSQATIKI
GGKERGHPFQ GQLSGLYYNG LKVLNMAAEN DANIVIEGNV RLVGEVPSSM TTESTATAMQ
SEMSTSVMET TTTLATSTAR RGKAPTKEPI GQTTDDILVA SAECPSDDED IDPCEPSSGG
LANPTRAGGG REYPGSSEVI RESSSTTGMV VGIVAAAALC ILILLYAMYK YRNRDEGSYH
VDESRNYISN SAQSNGAVIK EKQPNSAKSS NKNKKNKDKE YYV
