NRX1A_RAT
ID NRX1A_RAT Reviewed; 1530 AA.
AC Q63372;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Neurexin-1;
DE AltName: Full=Neurexin I-alpha;
DE AltName: Full=Neurexin-1-alpha;
DE Flags: Precursor;
GN Name=Nrxn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13A), INTERACTION WITH
RP ALPHA-LATROTOXIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Brain;
RX PubMed=1621094; DOI=10.1126/science.1621094;
RA Ushkaryov Y.A., Petrenko A.G., Geppert M., Suedhof T.C.;
RT "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin
RT receptor and laminin.";
RL Science 257:50-56(1992).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RX PubMed=7695896; DOI=10.1016/0896-6273(95)90306-2;
RA Ullrich B., Ushkaryov Y.A., Suedhof T.C.;
RT "Cartography of neurexins: more than 1000 isoforms generated by alternative
RT splicing and expressed in distinct subsets of neurons.";
RL Neuron 14:497-507(1995).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND INTERACTION WITH NXPH1 AND NXPH3.
RX PubMed=9856994; DOI=10.1074/jbc.273.52.34716;
RA Missler M., Hammer R.E., Suedhof T.C.;
RT "Neurexophilin binding to alpha-neurexins. A single LNS domain functions as
RT an independently folding ligand-binding unit.";
RL J. Biol. Chem. 273:34716-34723(1998).
RN [4]
RP INTERACTION WITH CASK.
RX PubMed=8786425; DOI=10.1523/jneurosci.16-08-02488.1996;
RA Hata Y., Butz S., Suedhof T.C.;
RT "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent
RT protein kinase domain identified by interaction with neurexins.";
RL J. Neurosci. 16:2488-2494(1996).
RN [5]
RP INTERACTION WITH ALPHA-LATROTOXIN.
RX PubMed=10197529; DOI=10.1016/s0896-6273(00)80704-7;
RA Sugita S., Khvochtev M., Suedhof T.C.;
RT "Neurexins are functional alpha-latrotoxin receptors.";
RL Neuron 22:489-496(1999).
RN [6]
RP INTERACTION WITH DAG1.
RX PubMed=11470830; DOI=10.1083/jcb.200105003;
RA Sugita S., Saito F., Tang J., Satz J., Campbell K., Suedhof T.C.;
RT "A stoichiometric complex of neurexins and dystroglycan in brain.";
RL J. Cell Biol. 154:435-445(2001).
RN [7]
RP INTERACTION WITH CASK; CASKIN1 AND APBA1.
RX PubMed=12040031; DOI=10.1523/jneurosci.22-11-04264.2002;
RA Tabuchi K., Biederer T., Butz S., Suedhof T.C.;
RT "CASK participates in alternative tripartite complexes in which Mint 1
RT competes for binding with Caskin 1, a novel CASK-binding protein.";
RL J. Neurosci. 22:4264-4273(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LRRTM1; LRRTM2; LRRTM3
RP AND LRRTM4.
RX PubMed=20064387; DOI=10.1016/j.neuron.2009.12.012;
RA Ko J., Fuccillo M.V., Malenka R.C., Sudhof T.C.;
RT "LRRTM2 functions as a neurexin ligand in promoting excitatory synapse
RT formation.";
RL Neuron 64:791-798(2009).
RN [9]
RP FUNCTION, INTERACTION WITH LRRTM2, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=20064388; DOI=10.1016/j.neuron.2009.12.019;
RA de Wit J., Sylwestrak E., O'Sullivan M.L., Otto S., Tiglio K., Savas J.N.,
RA Yates J.R. III, Comoletti D., Taylor P., Ghosh A.;
RT "LRRTM2 interacts with Neurexin1 and regulates excitatory synapse
RT formation.";
RL Neuron 64:799-806(2009).
RN [10]
RP INTERACTION WITH CASK.
RX PubMed=25385611; DOI=10.1073/pnas.1416515111;
RA Li Y., Wei Z., Yan Y., Wan Q., Du Q., Zhang M.;
RT "Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem
RT reveals a highly specific assembly mechanism for the apical Crumbs
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17444-17449(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1146-1361 IN COMPLEX WITH NLGN4.
RX PubMed=18093522; DOI=10.1016/j.neuron.2007.12.002;
RA Arac D., Boucard A.A., Ozkan E., Strop P., Newell E., Sudhof T.C.,
RA Brunger A.T.;
RT "Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex
RT reveal specific protein-protein and protein-Ca2+ interactions.";
RL Neuron 56:992-1003(2007).
CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions,
CC exocytosis of secretory granules and regulation of signal transmission.
CC Function is isoform-specific. Alpha-type isoforms have a long N-
CC terminus with six laminin G-like domains and play an important role in
CC synaptic signal transmission. Alpha-type isoforms play a role in the
CC regulation of calcium channel activity and Ca(2+)-triggered
CC neurotransmitter release at synapses and at neuromuscular junctions.
CC They play an important role in Ca(2+)-triggered exocytosis of secretory
CC granules in pituitary gland. They may affect their functions at
CC synapses and in endocrine cells via their interactions with proteins
CC from the exocytotic machinery. Likewise, alpha-type isoforms play a
CC role in regulating the activity of postsynaptic NMDA receptors, a
CC subtype of glutamate-gated ion channels (By similarity). Both alpha-
CC type and beta-type isoforms may play a role in the formation or
CC maintenance of synaptic junctions via their interactions (via the
CC extracellular domains) with neuroligin family members, CBLN1 or CBLN2.
CC In vitro, triggers the de novo formation of presynaptic structures. May
CC be involved in specification of excitatory synapses. Alpha-type
CC isoforms were first identified as receptors for alpha-latrotoxin from
CC spider venom. {ECO:0000250, ECO:0000269|PubMed:20064387,
CC ECO:0000269|PubMed:20064388}.
CC -!- SUBUNIT: Interacts (via laminin G-like domain 2 and/or laminin G-like
CC domain 6) with NLGN1 forming a heterotetramer, where one NLGN1 dimer
CC interacts with one NRXN1 dimer (By similarity). Interacts (via
CC cytoplasmic C-terminal region) with CASK (via the PDZ, SH3 and
CC guanylate kinase-like domains) (PubMed:8786425, PubMed:12040031).
CC Interacts (via cytoplasmic C-terminus) with CASKIN1 and APBA1
CC (PubMed:12040031). Interacts with SYT13 and SYTL1 (By similarity).
CC Interacts (via laminin G-like domain 2 and/or laminin G-like domain 6)
CC with NLGN1, NLGN2 and NLGN3; these interactions are calcium-dependent.
CC Interacts with CBLN1, CBLN2 and, less avidly, with CBLN4 (By
CC similarity). Interacts (via laminin G-like domain 2 and/or laminin G-
CC like domain 6) with NLGN4. Interacts (via laminin G-like domain 2) with
CC NXPH1 and NXPH3. Alpha-type isoforms (neurexin-1-alpha) interact (via
CC laminin G-like domain 2 and/or laminin G-like domain 6) with DAG1 (via
CC alpha-dystroglycan chain). Alpha-type isoforms interact with alpha-
CC latrotoxin from spider venom. Isoform 9a and isoform 13a bind to DAG1
CC (via alpha-dystroglycan chain). Isoform 13a binds to alpha-latrotoxin.
CC Interacts with LRRTM1, LRRTM2, LRRTM3 and LRRTM4. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q28146, ECO:0000269|PubMed:10197529,
CC ECO:0000269|PubMed:11470830, ECO:0000269|PubMed:12040031,
CC ECO:0000269|PubMed:1621094, ECO:0000269|PubMed:18093522,
CC ECO:0000269|PubMed:20064387, ECO:0000269|PubMed:20064388,
CC ECO:0000269|PubMed:8786425, ECO:0000269|PubMed:9856994}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Presynaptic cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=17;
CC Comment=Two isoform types, alpha-type and beta-type are produced by
CC alternative promoter usage. 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 five
CC sites may lead to the generation of at least 96 isoforms but for
CC simplicity only individual splice events or observed combinations are
CC explicitly described below. Beta-type isoforms share the possibility
CC of alternative splicing at sites 4 and 5. Experimental confirmation
CC may be lacking for some isoforms. {ECO:0000269|PubMed:1621094,
CC ECO:0000269|PubMed:7695896};
CC Name=1a; Synonyms=Alpha-1A2A3A4A5A;
CC IsoId=Q63372-2; Sequence=Displayed;
CC Name=2a; Synonyms=Alpha-1B;
CC IsoId=Q63372-1; Sequence=VSP_022560;
CC Name=3a; Synonyms=Alpha-1C;
CC IsoId=Q63372-3; Sequence=VSP_003486;
CC Name=4a; Synonyms=Alpha-1D;
CC IsoId=Q63372-4; Sequence=VSP_003488;
CC Name=5a; Synonyms=Alpha-1E;
CC IsoId=Q63372-5; Sequence=VSP_003486, VSP_003488;
CC Name=6a; Synonyms=Alpha-1F;
CC IsoId=Q63372-6; Sequence=VSP_022559;
CC Name=7a; Synonyms=Alpha-1G;
CC IsoId=Q63372-7; Sequence=VSP_003487;
CC Name=8a; Synonyms=Alpha-2B;
CC IsoId=Q63372-8; Sequence=VSP_003490;
CC Name=9a; Synonyms=Alpha-2C;
CC IsoId=Q63372-9; Sequence=VSP_003489;
CC Name=10a; Synonyms=Alpha-3B;
CC IsoId=Q63372-10; Sequence=VSP_003491;
CC Name=11a; Synonyms=Alpha-4B;
CC IsoId=Q63372-11; Sequence=VSP_003492;
CC Name=12a; Synonyms=Alpha-5B;
CC IsoId=Q63372-12; Sequence=VSP_003493;
CC Name=13a; Synonyms=Alpha-1B2B;
CC IsoId=Q63372-13; Sequence=VSP_022560, VSP_003490;
CC Name=1b; Synonyms=Beta-4A5A;
CC IsoId=Q63373-1; Sequence=External;
CC Name=2b; Synonyms=Beta-4A5B;
CC IsoId=Q63373-2; Sequence=External;
CC Name=3b; Synonyms=Beta-4B5A;
CC IsoId=Q63373-3; Sequence=External;
CC Name=4b; Synonyms=Beta-4B5B;
CC IsoId=Q63373-4; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain (neuronal synapse).
CC {ECO:0000269|PubMed:1621094, ECO:0000269|PubMed:7695896}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Alpha-latrotoxin competes with alpha-dystroglycan for
CC binding.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; M96374; AAA41704.1; -; mRNA.
DR PIR; A40228; A40228.
DR RefSeq; NP_068535.2; NM_021767.2. [Q63372-13]
DR PDB; 3BIW; X-ray; 3.50 A; E/F/G/H=1146-1361.
DR PDBsum; 3BIW; -.
DR AlphaFoldDB; Q63372; -.
DR SMR; Q63372; -.
DR BioGRID; 248813; 6.
DR MINT; Q63372; -.
DR STRING; 10116.ENSRNOP00000066979; -.
DR GlyGen; Q63372; 4 sites.
DR iPTMnet; Q63372; -.
DR PhosphoSitePlus; Q63372; -.
DR PRIDE; Q63372; -.
DR GeneID; 60391; -.
DR KEGG; rno:60391; -.
DR CTD; 9378; -.
DR RGD; 628659; Nrxn1.
DR InParanoid; Q63372; -.
DR OrthoDB; 35129at2759; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR EvolutionaryTrace; Q63372; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISS:BHF-UCL.
DR GO; GO:0033130; F:acetylcholine receptor binding; ISS:BHF-UCL.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR GO; GO:0097109; F:neuroligin family protein binding; ISS:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISO:RGD.
DR GO; GO:0030534; P:adult behavior; ISS:BHF-UCL.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0046847; P:filopodium assembly; ISO:RGD.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISO:RGD.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR GO; GO:0097117; P:guanylate kinase-associated protein clustering; ISO:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0007612; P:learning; ISS:BHF-UCL.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; ISO:RGD.
DR GO; GO:0042551; P:neuron maturation; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:BHF-UCL.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL.
DR GO; GO:0090129; P:positive regulation of synapse maturation; ISS:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISS:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0060134; P:prepulse inhibition; ISS:BHF-UCL.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISO:RGD.
DR GO; GO:0035418; P:protein localization to synapse; ISO:RGD.
DR GO; GO:0090126; P:protein-containing complex assembly involved in synapse maturation; ISO:RGD.
DR GO; GO:0097120; P:receptor localization to synapse; ISO:RGD.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISO:RGD.
DR GO; GO:2000821; P:regulation of grooming behavior; ISS:BHF-UCL.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISO:RGD.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; ISO:RGD.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0099542; P:trans-synaptic signaling by endocannabinoid; ISO:RGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:MGI.
DR GO; GO:0042297; P:vocal learning; ISO:RGD.
DR GO; GO:0071625; P:vocalization behavior; ISO:RGD.
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; 1.
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 3D-structure; Alternative promoter usage; Alternative splicing; Calcium;
KW Cell adhesion; Cell membrane; Cell projection; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:9856994"
FT CHAIN 31..1530
FT /note="Neurexin-1"
FT /id="PRO_0000019491"
FT TOPO_DOM 31..1454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1455..1475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1476..1530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..217
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 213..255
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 299..496
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 503..695
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 699..736
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 741..914
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 928..1103
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1106..1143
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1149..1347
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 196..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1523
FT /note="Interaction with CASK"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT COMPBIAS 1497..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 788
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 805
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 864
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 228..243
FT /evidence="ECO:0000250"
FT DISULFID 245..255
FT /evidence="ECO:0000250"
FT DISULFID 460..496
FT /evidence="ECO:0000250"
FT DISULFID 666..695
FT /evidence="ECO:0000250"
FT DISULFID 703..714
FT /evidence="ECO:0000250"
FT DISULFID 708..723
FT /evidence="ECO:0000250"
FT DISULFID 725..735
FT /evidence="ECO:0000250"
FT DISULFID 1075..1103
FT /evidence="ECO:0000250"
FT DISULFID 1110..1121
FT /evidence="ECO:0000250"
FT DISULFID 1115..1130
FT /evidence="ECO:0000250"
FT DISULFID 1132..1142
FT /evidence="ECO:0000250"
FT VAR_SEQ 258..277
FT /note="Missing (in isoform 7a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003487"
FT VAR_SEQ 258
FT /note="Missing (in isoform 3a and isoform 5a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003486"
FT VAR_SEQ 264..273
FT /note="Missing (in isoform 6a)"
FT /evidence="ECO:0000305"
FT /id="VSP_022559"
FT VAR_SEQ 274..277
FT /note="Missing (in isoform 4a and isoform 5a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003488"
FT VAR_SEQ 278..293
FT /note="Missing (in isoform 2a and isoform 13a)"
FT /evidence="ECO:0000303|PubMed:1621094"
FT /id="VSP_022560"
FT VAR_SEQ 395..409
FT /note="Missing (in isoform 9a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003489"
FT VAR_SEQ 403..409
FT /note="Missing (in isoform 8a and isoform 13a)"
FT /evidence="ECO:0000303|PubMed:1621094"
FT /id="VSP_003490"
FT VAR_SEQ 806..815
FT /note="DCIRINCNSS -> G (in isoform 10a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003491"
FT VAR_SEQ 1263..1292
FT /note="Missing (in isoform 11a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003492"
FT VAR_SEQ 1426..1427
FT /note="Missing (in isoform 12a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003493"
FT STRAND 1146..1161
FT /evidence="ECO:0007829|PDB:3BIW"
FT HELIX 1164..1166
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1170..1180
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1184..1194
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1200..1206
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1209..1219
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1221..1224
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1232..1234
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1236..1243
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1246..1251
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1257..1259
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1301..1309
FT /evidence="ECO:0007829|PDB:3BIW"
FT TURN 1310..1313
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1318..1325
FT /evidence="ECO:0007829|PDB:3BIW"
FT HELIX 1330..1335
FT /evidence="ECO:0007829|PDB:3BIW"
FT STRAND 1341..1350
FT /evidence="ECO:0007829|PDB:3BIW"
SQ SEQUENCE 1530 AA; 167923 MW; 548109BAF05119FC CRC64;
MGTALVQHGG CCLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR
RQFRNTTLYI DRAEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
KGWIRDVRVN SSQALPVDGS EVKLDEEPPN SGGGSPCEAG DEGDGGVCLN GGVCSVVDDQ
AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKEDN NVEGLAHLMM GDQGKEEYIA
TFKGSEYFCY DLSQNPIQSS SDEITLSFKT LQRNGLMLHT GKSADYVNLA LKNGAVSLVI
NLGSGAFEAL VEPVNGKFND NAWHDVKVTR NLRQHSGIGH AMVNKLHCSV TISVDGILTT
TGYTQEDYTM LGSDDFFYVG GSPSTADLPG SPVSNNFMGC LKEVVYKNND VRLELSRLAK
QGDPKMKIHG VVAFKCENVA TLDPITFETP ESFISLPKWN AKKTGSISFD FRTTEPNGLI
LFSHGKPRHQ KDAKHPQMIK VDFFAIEMLD GHLYLLLDMG SGTIKIKALQ KKVNDGEWYH
VDFQRDGRSG TISVNTLRTP YTAPGESEIL DLDDELYLGG LPENKAGLVF PTEVWTALLN
YGYVGCIRDL FIDGQSKDIR QMAEIQSTAG VKPSCSRETA KPCLSNPCKN NGMCRDGWNR
YVCDCSGTGY LGRSCEREAT VLSYDGSMFM KIQLPVVMHT EAEDVSLRFR SQRAYGILMA
TTSRDSADTL RLELDAGRVK LTVNLDCIRI NCNSSKGPET LFAGYNLNDN EWHTVRVVRR
GKSLKLTVDD QQAMTGQMAG DHTRLEFHNI ETGIITERRY LSSVPSNFIG HLQSLTFNGM
AYIDLCKNGD IDYCELNARF GFRNIIADPV TFKTKSSYVA LATLQAYTSM HLFFQFKTTS
LDGLILYNSG DGNDFIVVEL VKGYLHYVFD LGNGANLIKG SSNKPLNDNQ WHNVMISRDT
SNLHTVKIDT KITTQITAGA RNLDLKSDLY IGGVAKETYK SLPKLVHAKE GFQGCLASVD
LNGRLPDLIS DALFCNGQIE RGCEGPSTTC QEDSCSNQGV CLQQWDGFSC DCSMTSFSGP
LCNDPGTTYI FSKGGGQITH KWPPNDRPST RADRLAIGFS TVQKEAVLVR VDSSSGLGDY
LELHIHQGKI GVKFNVGTDD IAIEESNAII NDGKYHVVRF TRSGGNATLQ VDSWPVIERY
PAGNNDNERL AIARQRIPYR LGRVVDEWLL DKGRQLTIFN SQATIIIGGK EQGQPFQGQL
SGLYYNGLKV LNMAAENDAN IAIVGNVRLV GEVPSSMTTE STATAMQSEM STSIMETTTT
LATSTARRGK PPTKEPISQT TDDILVASAE CPSDDEDIDP CEPSSGGLAN PTRVGGREPY
PGSAEVIRES SSTTGMVVGI VAAAALCILI LLYAMYKYRN RDEGSYHVDE SRNYISNSAQ
SNGAVVKEKQ PSSAKSANKN KKNKDKEYYV
