NRX3A_CHICK
ID NRX3A_CHICK Reviewed; 1693 AA.
AC D0PRN3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Neurexin-3;
DE AltName: Full=Neurexin III-alpha;
DE AltName: Full=Neurexin-3-alpha;
DE Flags: Precursor;
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], 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. May mediate intracellular signaling (By
CC 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=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=1a;
CC IsoId=D0PRN3-1; Sequence=Displayed;
CC Name=1b;
CC IsoId=D0PRN4-1; Sequence=External;
CC Name=2b;
CC IsoId=D0PRN4-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain and arteries (at protein level).
CC {ECO:0000269|PubMed:19926856}.
CC -!- MISCELLANEOUS: [Isoform 1a]: Produced by alternative promoter usage.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; EU702428; ACF35429.1; -; mRNA.
DR RefSeq; NP_001258852.1; NM_001271923.1. [D0PRN3-1]
DR RefSeq; XP_015142904.1; XM_015287418.1. [D0PRN3-1]
DR AlphaFoldDB; D0PRN3; -.
DR SMR; D0PRN3; -.
DR STRING; 9031.ENSGALP00000017104; -.
DR PaxDb; D0PRN3; -.
DR GeneID; 423385; -.
DR KEGG; gga:423385; -.
DR CTD; 9369; -.
DR VEuPathDB; HostDB:geneid_423385; -.
DR eggNOG; KOG3514; Eukaryota.
DR PhylomeDB; D0PRN3; -.
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; 6.
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; 2.
DR Pfam; PF02210; Laminin_G_2; 6.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1693
FT /note="Neurexin-3"
FT /id="PRO_0000412545"
FT TOPO_DOM 28..1618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1619..1639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1640..1693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..207
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 198..235
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 260..459
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 466..658
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 662..699
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 704..876
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 890..1065
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1068..1105
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1109..1309
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1535..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 202..213
FT /evidence="ECO:0000250"
FT DISULFID 207..222
FT /evidence="ECO:0000250"
FT DISULFID 224..234
FT /evidence="ECO:0000250"
FT DISULFID 423..459
FT /evidence="ECO:0000250"
FT DISULFID 629..658
FT /evidence="ECO:0000250"
FT DISULFID 666..677
FT /evidence="ECO:0000250"
FT DISULFID 671..686
FT /evidence="ECO:0000250"
FT DISULFID 688..698
FT /evidence="ECO:0000250"
FT DISULFID 1037..1065
FT /evidence="ECO:0000250"
FT DISULFID 1072..1083
FT /evidence="ECO:0000250"
FT DISULFID 1077..1092
FT /evidence="ECO:0000250"
FT DISULFID 1094..1104
FT /evidence="ECO:0000250"
SQ SEQUENCE 1693 AA; 186627 MW; 1CD841C6D4D4966B CRC64;
MGFTLHSVYF TLKVSLLLGS LLGLSLGLEF MGIPNQWTRF LRWDASTRSE LSFQFKTNVS
AGLLLYFDDG GVCDFLCLSL VDGRIQLQFS VDCAETTVIT DKQVNDSNWH FLMVSRNHLR
TVLVLDGEAK PGEVRPQRQY MNIVSDLFVG GVPSYIRPAA LTLDGVLSEP PFQGFILNLK
YGNSEPQLLG SQGVRLEMEG LCTENPCENG GTCFLLDGEP RCDCSATGYT GKLCSEDVNH
IPGLSHLMMS EQGRSKARDE NMATFRGSEY LCYDLSQNPI QSSSDEITLS FKTWQRNGLI
LHTGKSADYV NLALKDGAVS LVINLGSGAF EAIVEPVNGK FNDNAWHDVK VTRNLRQHSG
IGHAMVNKLH CLVTISVDGI LTTTGYTQED YTMLGSDDFF YVGGSPSTAD LPGSPVSNNF
MGCLKEVVYK NNDIRLELSR LARIGDTKMK IYGEVKFVCE NVATLDPISF ETPEAYISLP
KWNTKRMGSI SFDFRTTEPN GLILFTHGKP QERKDARSQK NTKVDFFAVE LLDGNLYLLL
DMGSGTIKVK ATQKKANDGE WYHVDIQRDG RSGTISVNSR RTPFTASGES EILDLEGDMY
LGGLPENRAG LILPTELWTA MLNYGYVGCI RDLFIDGRSK NIRQLAEAQN AAGVKSSCSR
LSTKQCDSYP CKNNAVCKDG WNRFICDCTG TGYWGRTCER EASILSYDGS MYMKIIMPMV
MHTEAEDVSF RFMSQRAYGL LMATTSRDSA DTLRLELDGG RVKLMVNLDC IRINCNASKG
PETLYAGQKL NDNEWHTVRV VRRGKSLKLM VDDDVAEGTM VGDHTRLEFH NIETGIMTEK
RYISVIPSSF IGHLQSLMFN GMLYIDLCKN GDIDYCELKA RFGLRNIIAD PVTFKTKSSY
LSLATLQAYT SMHLFFQFKT TSADGFILFN SGDGNDFIAV ELVKGYIHYV FDLGNGPNVI
KGNSDRPLND NQWHNVVITR DNSNTHSLKV DTKMVTQVIN GAKNLDLKGD LYIAGLAQGM
YSNLPKLVAS RDGFQGCLAS VDLNGRLPDL INDALHRSGQ IERGCEGPST TCQEDSCANQ
GICNQQWEGF TCDCSMTSYS GSQCNDPGAT YIFGKSGGLI LYTWPANDRP STRTDRLAVG
FSTTVKDGIL VRIDSAPGLG DFLQLHIEQG KIGVVFNIGT VDISIKEEST PVNDGKYHVV
RFTRNGGNAT LQVDSWPVNE HYPTGNTDSE RFQMVKQKIP FKYNRPVEEW LQEKGRQLTI
FNTQAQIAIG GKDRGRLFQG QLSGLYYNGL KVLNMAAENN PNIKINGSVR LVGEVPSILG
TTPTTSVPPE MSTTVMETTT TMATTTTRKN RSPPSIQTTD DIVSSAECSS DDEDFIDCEP
STGKSGGELV IPLLVEDPLD IPPIATRAPF ITLPPTFRPL LTIIETTKDS LSMTSEAGLP
CLSDQGSDGC DDDGLVISGY GSGETFDSNL PPTDDEDFYT TFSLVTDKSL STSIFEGGYK
AHAPKWESKD FRPNKVSETG RTTTTSLSPE LIRSTASSST GMVPKLPAGK MNNRELKPQP
DIVLLPLPTA YELDSTKLKS PLITSPMFRN VPTANPTEPG IRRVPGASEV VRESSSTTGM
VVGIVAAAAL CILILLYAMY KYRNRDEGSY QVDETRNYIS NSAQSNGTLM KEKQQSSKSG
HKKQKNKDKE YYV
