NR3AA_DANRE
ID NR3AA_DANRE Reviewed; 1697 AA.
AC A1XQX8; A1XQX9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Neurexin-3a;
DE AltName: Full=Neurexin IIIa-alpha;
DE AltName: Full=Neurexin-3a-alpha;
DE Flags: Precursor;
GN Name=nrxn3a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 2A), DEVELOPMENTAL STAGE, AND
RP ALTERNATIVE SPLICING.
RX PubMed=17041151; DOI=10.1093/molbev/msl147;
RA Rissone A., Monopoli M., Beltrame M., Bussolino F., Cotelli F., Arese M.;
RT "Comparative genome analysis of the neurexin gene family in Danio rerio:
RT insights into their functions and evolution.";
RL Mol. Biol. Evol. 24:236-252(2007).
CC -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion.
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=A1XQX8-1; Sequence=Displayed;
CC Name=2a; Synonyms=Soluble form;
CC IsoId=A1XQX8-2; Sequence=VSP_041706, VSP_041707;
CC Name=1b;
CC IsoId=A1XQY0-1; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: After the very early developmental stages, the
CC expression levels decrease and remain relatively constant until around
CC 24 h, with the onset of an increase of expression that continues till
CC the larval stages. {ECO:0000269|PubMed:17041151}.
CC -!- MISCELLANEOUS: [Isoform 2a]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; DQ641432; ABG25169.1; -; mRNA.
DR EMBL; DQ641433; ABG25170.1; -; mRNA.
DR RefSeq; NP_001073478.1; NM_001080009.1. [A1XQX8-2]
DR AlphaFoldDB; A1XQX8; -.
DR SMR; A1XQX8; -.
DR STRING; 7955.ENSDARP00000082612; -.
DR PaxDb; A1XQX8; -.
DR PeptideAtlas; A1XQX8; -.
DR PRIDE; A1XQX8; -.
DR GeneID; 563598; -.
DR KEGG; dre:563598; -.
DR CTD; 563598; -.
DR ZFIN; ZDB-GENE-070206-9; nrxn3a.
DR eggNOG; KOG3514; Eukaryota.
DR InParanoid; A1XQX8; -.
DR OrthoDB; 35129at2759; -.
DR PhylomeDB; A1XQX8; -.
DR Reactome; R-DRE-6794361; Neurexins and neuroligins.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0001525; P:angiogenesis; 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; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
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; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 2: Evidence at transcript level;
KW Alternative promoter usage; Alternative splicing; Angiogenesis; Calcium;
KW Cell adhesion; Disulfide bond; EGF-like domain; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1697
FT /note="Neurexin-3a"
FT /id="PRO_0000412549"
FT TOPO_DOM 24..1622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1623..1643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1644..1697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..198
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 194..231
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 258..455
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 462..654
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 658..695
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 700..872
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 886..1061
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1073..1110
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1114..1314
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1345..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1665..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 198..209
FT /evidence="ECO:0000250"
FT DISULFID 203..218
FT /evidence="ECO:0000250"
FT DISULFID 220..230
FT /evidence="ECO:0000250"
FT DISULFID 419..455
FT /evidence="ECO:0000250"
FT DISULFID 625..654
FT /evidence="ECO:0000250"
FT DISULFID 662..673
FT /evidence="ECO:0000250"
FT DISULFID 667..682
FT /evidence="ECO:0000250"
FT DISULFID 684..694
FT /evidence="ECO:0000250"
FT DISULFID 1033..1061
FT /evidence="ECO:0000250"
FT DISULFID 1077..1088
FT /evidence="ECO:0000250"
FT DISULFID 1082..1097
FT /evidence="ECO:0000250"
FT DISULFID 1099..1109
FT /evidence="ECO:0000250"
FT VAR_SEQ 1390..1425
FT /note="GGELVFPVIVKDPLELPSVATRTPSIPFPPTLTIIE -> AKNVNAARPLRT
FT AYTWTWQLTYTITPIIVISYVVCS (in isoform 2a)"
FT /evidence="ECO:0000303|PubMed:17041151"
FT /id="VSP_041706"
FT VAR_SEQ 1426..1697
FT /note="Missing (in isoform 2a)"
FT /evidence="ECO:0000303|PubMed:17041151"
FT /id="VSP_041707"
SQ SEQUENCE 1697 AA; 187194 MW; FA961C8C4306CB26 CRC64;
MNFFRFPVQL QLLISTVLGP CLGLEFTGLQ GQWARYLRWD ASTRSDLSFQ FKTDVSTALI
LYFDDGGFCD FLQLMVVEGK LQLQFSIDCA ETTVVSDKRV NDSSWHSATL SRYNLRTVLG
LDGVSKWAEV RPLRQYMKIV SDLFLGGVPQ DIRISVLTLP TVKDLPPFKG IIRELKYNSK
EPILLSSQRV RMDIEGICME NPCENGGTCS VVDGEPLCDC SKTEYVGRFC NEEANNIPGF
AHMMMADQAK GKAREENVAT FRGSEFFCYD LSQNPIQSSS DEITLSFKTW QRNGLILHTG
KSADYVNLAL KDGAVSLVIN LGSGAFEAIV EPVNGKFNDN SWHDVKVTRN LRQHSGIGHA
MVNKLHCLVT ISVDGILTTT GYTQEDYTML GSDDFFYVGG SPSTADLPGS PVSNNFMGCL
KEVVYKNNDI RLELSRLARI VDPKMKIQGD VVFKCENVAT LDPISFETPE AYISLPKWNT
KRMGSISFDF RTTEPNGLIL FTHGKPQERK DARSQKNTKV DFFAVELLDG SLYLLLDMGS
GTIKVKATQN KVNDGAWYHV DIQRDGRSGT ISVNSRRTPF TASGENEILD LEGDMYLGGL
PDSRGSLILP TELWTAMLNY GYVGCIRDLF IDGRSKDIRQ IAEAQNGAGI KPSCNKMSGK
QCDSYPCKNK GLCKEGWNRF ICDCTGTGYW SRTCEREASI LSYDGSMYMK VVMPTVMHTE
AEDVSLRFMS QRAYGLLMAT TSRDSADTLR LELDGSRVKL TVNLDCIRIN CNSSKGPETL
YAGQKLNDNE WHTVRVIRRG KSYKLTVDDD VAEGQMVGDH TRLEFHNIET GVMTERRFVS
MIPSSFIGHL QSLKFNGLLY IDLCKNGDID FCELNARFGM RSIIADPVTF KSKNSYLSLA
TLQAYTSMHL FFQFKTTSAD GFILFNSGDG SDFIAVELVK GYIHYVFNLG NGPNVIKGNS
ERALHDNQWH NVVITRDNSN VHTLKVDAKA VSQVVNGAKN LDLKGDLFIA GLGPNMYNNL
PKLVASREGF KGCLASVDLN GRLPDLINDA LFRSGQIERG CEVGFTKADL KGPSTTCQED
SCANMGICIQ QWENYTCDCS MTSYTGTHCN DPGTTYIFGK GGGLISFNWP ANERPSTRTD
RLTVGFSTSL KDGILIRIDS APGLGDYLML HIEQGKIGVT FNIGTADITV QESSTAVNDG
KYHVVRFTRN GGNATLQVDN WAINEHFPSG NSDNERIQMA NKKIPFKYAR PVEEWLQEKG
RQLTIFNTQA TITIGGSDRK RPFQGQLSGL YYNGLKVLNM AAQGNPNIKI NGSVRLVGEV
PAAGSARTTA LPPEMSTAFI ETTTTMSTTT TRKHRTPPTI QTTDDMVSSA ECSSDDEDFA
ECEGHAGGLG GELVFPVIVK DPLELPSVAT RTPSIPFPPT LTIIETTKES LSMATEAGVP
CLSDGGSDDC GDDDDDDDDD GLMISGYGSG EAYDSNLPPT DDEDFYTTFS LVTDKTLSSS
TFEGGYKAHA PKWGSKDFRP NKVFDSGRTT TASFSPKLSR STTTSTPPKL PAGKMNHREL
KPQPDIVLLP LPTSYEVDNT KMKSPLITSP MFRNVPTAIP TEPGIRRVPG ASEVVRESSS
TTGMVVGIVA AAALCILILL YAMYKYRNRD EGSYQVDETR NYITNSAQSN GAVMKDKQQS
TKSGNKKQKN KDKEYYV
