CNTP2_HUMAN
ID CNTP2_HUMAN Reviewed; 1331 AA.
AC Q9UHC6; D3DWG2; Q14DG2; Q52LV1; Q5H9Q7; Q9UQ12;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Contactin-associated protein-like 2;
DE AltName: Full=Cell recognition molecule Caspr2;
DE Flags: Precursor;
GN Name=CNTNAP2; Synonyms=CASPR2 {ECO:0000303|PubMed:10624965}, KIAA0868;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH KCNA2, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10624965; DOI=10.1016/s0896-6273(00)81049-1;
RA Poliak S., Gollan L., Martinez R., Custer A., Einheber S., Salzer J.L.,
RA Trimmer J.S., Shrager P., Peles E.;
RT "Caspr2, a new member of the neurexin superfamily, is localized at the
RT juxtaparanodes of myelinated axons and associates with K+ channels.";
RL Neuron 24:1037-1047(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11352571; DOI=10.1006/geno.2001.6517;
RA Nakabayashi K., Scherer S.W.;
RT "The human contactin-associated protein-like 2 gene (CNTNAP2) spans over 2
RT Mb of DNA at chromosome 7q35.";
RL Genomics 73:108-112(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INVOLVEMENT IN PTHSL1.
RX PubMed=16571880; DOI=10.1056/nejmoa052773;
RA Strauss K.A., Puffenberger E.G., Huentelman M.J., Gottlieb S., Dobrin S.E.,
RA Parod J.M., Stephan D.A., Morton D.H.;
RT "Recessive symptomatic focal epilepsy and mutant contactin-associated
RT protein-like 2.";
RL N. Engl. J. Med. 354:1370-1377(2006).
RN [8]
RP INVOLVEMENT IN PTHSL1.
RX PubMed=19896112; DOI=10.1016/j.ajhg.2009.10.004;
RA Zweier C., de Jong E.K., Zweier M., Orrico A., Ousager L.B., Collins A.L.,
RA Bijlsma E.K., Oortveld M.A., Ekici A.B., Reis A., Schenck A., Rauch A.;
RT "CNTNAP2 and NRXN1 are mutated in autosomal-recessive Pitt-Hopkins-like
RT mental retardation and determine the level of a common synaptic protein in
RT Drosophila.";
RL Am. J. Hum. Genet. 85:655-666(2009).
RN [9]
RP FUNCTION.
RX PubMed=33238150; DOI=10.1016/j.devcel.2020.10.020;
RA Meng L., Yan D.;
RT "NLR-1/CASPR Anchors F-Actin to Promote Gap Junction Formation.";
RL Dev. Cell 55:574-587(2020).
RN [10]
RP INVOLVEMENT IN AUTS15, VARIANTS GLN-114; MET-218; MET-226; CYS-283;
RP ASN-382; SER-407; ASP-418; LYS-680; GLN-699; CYS-716; SER-731; ASP-779;
RP THR-869; HIS-906; ASN-1038; ALA-1102; GLY-1114; HIS-1119; HIS-1129;
RP THR-1227; THR-1253 AND ILE-1278, AND CHROMOSOMAL REARRANGEMENT.
RX PubMed=18179895; DOI=10.1016/j.ajhg.2007.09.017;
RA Bakkaloglu B., O'Roak B.J., Louvi A., Gupta A.R., Abelson J.F.,
RA Morgan T.M., Chawarska K., Klin A., Ercan-Sencicek A.G., Stillman A.A.,
RA Tanriover G., Abrahams B.S., Duvall J.A., Robbins E.M., Geschwind D.H.,
RA Biederer T., Gunel M., Lifton R.P., State M.W.;
RT "Molecular cytogenetic analysis and resequencing of contactin associated
RT protein-like 2 in autism spectrum disorders.";
RL Am. J. Hum. Genet. 82:165-173(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Required for gap junction formation (Probable). Required,
CC with CNTNAP1, for radial and longitudinal organization of myelinated
CC axons. Plays a role in the formation of functional distinct domains
CC critical for saltatory conduction of nerve impulses in myelinated nerve
CC fibers. Demarcates the juxtaparanodal region of the axo-glial junction.
CC {ECO:0000250|UniProtKB:Q9CPW0, ECO:0000305|PubMed:33238150}.
CC -!- SUBUNIT: Interacts (via C-terminus) with KCNA2.
CC {ECO:0000269|PubMed:10624965}.
CC -!- INTERACTION:
CC Q9UHC6; Q12860: CNTN1; NbExp=5; IntAct=EBI-310892, EBI-5564336;
CC Q9UHC6; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-310892, EBI-739467;
CC Q9UHC6; P50222: MEOX2; NbExp=3; IntAct=EBI-310892, EBI-748397;
CC Q9UHC6; P62487: POLR2G; NbExp=3; IntAct=EBI-310892, EBI-347928;
CC Q9UHC6-1; P27824: CANX; NbExp=2; IntAct=EBI-16594440, EBI-355947;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9CPW0}; Single-
CC pass type I membrane protein {ECO:0000305}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9CPW0}. Cell junction, paranodal septate
CC junction {ECO:0000250|UniProtKB:Q9CPW0}. Note=Expressed in the
CC juxtaparadonal region. {ECO:0000250|UniProtKB:Q9CPW0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHC6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHC6-2; Sequence=VSP_014976;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in nervous system.
CC {ECO:0000269|PubMed:10624965}.
CC -!- DISEASE: Autism 15 (AUTS15) [MIM:612100]: A complex multifactorial,
CC pervasive developmental disorder characterized by impairments in
CC reciprocal social interaction and communication, restricted and
CC stereotyped patterns of interests and activities, and the presence of
CC developmental abnormalities by 3 years of age. Most individuals with
CC autism also manifest moderate intellectual disability.
CC {ECO:0000269|PubMed:18179895}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving CNTNAP2 is found in a
CC patient with autism spectrum disorder. Paracentric inversion
CC 46,XY,inv(7)(q11.22;q35). The inversion breakpoints disrupt the genes
CC AUTS2 and CNTNAP2.
CC -!- DISEASE: Pitt-Hopkins-like syndrome 1 (PTHSL1) [MIM:610042]: A syndrome
CC characterized by severe intellectual disability and variable additional
CC symptoms, such as impaired speech development, seizures, autistic
CC behavior, breathing anomalies and a broad mouth, resembling Pitt-
CC Hopkins syndrome. In contrast to patients with Pitt-Hopkins syndrome,
CC PTHSL1 patients present with normal or only mildly to moderately
CC delayed motor milestones. {ECO:0000269|PubMed:16571880,
CC ECO:0000269|PubMed:19896112}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74891.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF193613; AAF25199.1; -; mRNA.
DR EMBL; AF319045; AAK34932.1; -; mRNA.
DR EMBL; AF318292; AAK49902.1; -; Genomic_DNA.
DR EMBL; AF318298; AAK49903.1; -; Genomic_DNA.
DR EMBL; AB020675; BAA74891.1; ALT_INIT; mRNA.
DR EMBL; CR933671; CAI45967.1; -; mRNA.
DR EMBL; CH471146; EAW80084.1; -; Genomic_DNA.
DR EMBL; BC093780; AAH93780.1; -; mRNA.
DR EMBL; BC113373; AAI13374.1; -; mRNA.
DR CCDS; CCDS5889.1; -. [Q9UHC6-1]
DR RefSeq; NP_054860.1; NM_014141.5. [Q9UHC6-1]
DR PDB; 5Y4M; X-ray; 1.31 A; A=35-181.
DR PDBsum; 5Y4M; -.
DR AlphaFoldDB; Q9UHC6; -.
DR SASBDB; Q9UHC6; -.
DR SMR; Q9UHC6; -.
DR BioGRID; 117510; 16.
DR IntAct; Q9UHC6; 13.
DR MINT; Q9UHC6; -.
DR STRING; 9606.ENSP00000354778; -.
DR GlyGen; Q9UHC6; 12 sites.
DR iPTMnet; Q9UHC6; -.
DR PhosphoSitePlus; Q9UHC6; -.
DR SwissPalm; Q9UHC6; -.
DR BioMuta; CNTNAP2; -.
DR DMDM; 17433089; -.
DR EPD; Q9UHC6; -.
DR jPOST; Q9UHC6; -.
DR MassIVE; Q9UHC6; -.
DR MaxQB; Q9UHC6; -.
DR PaxDb; Q9UHC6; -.
DR PeptideAtlas; Q9UHC6; -.
DR PRIDE; Q9UHC6; -.
DR ProteomicsDB; 84311; -. [Q9UHC6-1]
DR ProteomicsDB; 84312; -. [Q9UHC6-2]
DR ABCD; Q9UHC6; 1 sequenced antibody.
DR Antibodypedia; 682; 294 antibodies from 32 providers.
DR DNASU; 26047; -.
DR Ensembl; ENST00000361727.8; ENSP00000354778.3; ENSG00000174469.23. [Q9UHC6-1]
DR Ensembl; ENST00000463592.3; ENSP00000486292.1; ENSG00000174469.23. [Q9UHC6-2]
DR Ensembl; ENST00000613345.2; ENSP00000481057.1; ENSG00000278728.2. [Q9UHC6-2]
DR GeneID; 26047; -.
DR KEGG; hsa:26047; -.
DR MANE-Select; ENST00000361727.8; ENSP00000354778.3; NM_014141.6; NP_054860.1.
DR UCSC; uc003weu.3; human. [Q9UHC6-1]
DR CTD; 26047; -.
DR DisGeNET; 26047; -.
DR GeneCards; CNTNAP2; -.
DR HGNC; HGNC:13830; CNTNAP2.
DR HPA; ENSG00000174469; Group enriched (brain, retina).
DR MalaCards; CNTNAP2; -.
DR MIM; 604569; gene.
DR MIM; 610042; phenotype.
DR MIM; 612100; phenotype.
DR neXtProt; NX_Q9UHC6; -.
DR OpenTargets; ENSG00000174469; -.
DR Orphanet; 163681; CNTNAP2-related developmental and epileptic encephalopathy.
DR Orphanet; 106; NON RARE IN EUROPE: Autism.
DR PharmGKB; PA26692; -.
DR VEuPathDB; HostDB:ENSG00000174469; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000154516; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; Q9UHC6; -.
DR OMA; GNIWXAD; -.
DR PhylomeDB; Q9UHC6; -.
DR TreeFam; TF321823; -.
DR PathwayCommons; Q9UHC6; -.
DR SignaLink; Q9UHC6; -.
DR SIGNOR; Q9UHC6; -.
DR BioGRID-ORCS; 26047; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; CNTNAP2; human.
DR GeneWiki; CNTNAP2; -.
DR GenomeRNAi; 26047; -.
DR Pharos; Q9UHC6; Tbio.
DR PRO; PR:Q9UHC6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UHC6; protein.
DR Bgee; ENSG00000174469; Expressed in corpus callosum and 98 other tissues.
DR ExpressionAtlas; Q9UHC6; baseline and differential.
DR Genevisible; Q9UHC6; HS.
DR GO; GO:0030673; C:axolemma; IDA:BHF-UCL.
DR GO; GO:0030424; C:axon; NAS:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; NAS:BHF-UCL.
DR GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; NAS:BHF-UCL.
DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; NAS:BHF-UCL.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR GO; GO:0007420; P:brain development; TAS:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IEP:BHF-UCL.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISS:BHF-UCL.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0021761; P:limbic system development; IEP:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; ISS:BHF-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0008038; P:neuron recognition; NAS:UniProtKB.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; IMP:UniProtKB.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0021756; P:striatum development; IEP:BHF-UCL.
DR GO; GO:0071109; P:superior temporal gyrus development; IEP:BHF-UCL.
DR GO; GO:0021794; P:thalamus development; IEP:BHF-UCL.
DR GO; GO:0019226; P:transmission of nerve impulse; NAS:UniProtKB.
DR GO; GO:0042297; P:vocal learning; IMP:BHF-UCL.
DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR029831; Caspr2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF33; PTHR15036:SF33; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 4.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autism; Autism spectrum disorder;
KW Cell adhesion; Cell junction; Cell projection; Chromosomal rearrangement;
KW Disulfide bond; EGF-like domain; Epilepsy; Glycoprotein;
KW Intellectual disability; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1331
FT /note="Contactin-associated protein-like 2"
FT /id="PRO_0000019506"
FT TOPO_DOM 28..1262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1263..1283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1284..1331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..181
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 216..368
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 401..552
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 554..591
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 592..798
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 799..963
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 963..1002
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1055..1214
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1026..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPW0"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPW0"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..181
FT /evidence="ECO:0000250"
FT DISULFID 336..368
FT /evidence="ECO:0000250"
FT DISULFID 520..552
FT /evidence="ECO:0000250"
FT DISULFID 558..569
FT /evidence="ECO:0000250"
FT DISULFID 563..578
FT /evidence="ECO:0000250"
FT DISULFID 580..590
FT /evidence="ECO:0000250"
FT DISULFID 936..963
FT /evidence="ECO:0000250"
FT DISULFID 967..980
FT /evidence="ECO:0000250"
FT DISULFID 974..989
FT /evidence="ECO:0000250"
FT DISULFID 991..1001
FT /evidence="ECO:0000250"
FT DISULFID 1178..1214
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_014976"
FT VARIANT 114
FT /note="R -> Q (in dbSNP:rs189731792)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046227"
FT VARIANT 218
FT /note="T -> M (in dbSNP:rs771028883)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046228"
FT VARIANT 226
FT /note="L -> M (in dbSNP:rs372345438)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046229"
FT VARIANT 283
FT /note="R -> C (in dbSNP:rs794727802)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046230"
FT VARIANT 382
FT /note="S -> N (in dbSNP:rs371839994)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046231"
FT VARIANT 407
FT /note="N -> S (in dbSNP:rs143877693)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046232"
FT VARIANT 418
FT /note="N -> D (in dbSNP:rs772179690)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046233"
FT VARIANT 680
FT /note="E -> K (in dbSNP:rs368905425)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046234"
FT VARIANT 699
FT /note="P -> Q (in dbSNP:rs764412489)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046235"
FT VARIANT 716
FT /note="Y -> C (in dbSNP:rs760930032)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046236"
FT VARIANT 731
FT /note="G -> S (in dbSNP:rs369867547)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046237"
FT VARIANT 779
FT /note="G -> D (in dbSNP:rs200413148)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046238"
FT VARIANT 869
FT /note="I -> T (may be a risk factor for autism;
FT dbSNP:rs121908445)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046239"
FT VARIANT 906
FT /note="R -> H (in dbSNP:rs759801195)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046240"
FT VARIANT 1038
FT /note="D -> N (in dbSNP:rs144003410)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046241"
FT VARIANT 1102
FT /note="V -> A (in dbSNP:rs111599875)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046242"
FT VARIANT 1114
FT /note="S -> G (in dbSNP:rs983036503)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046243"
FT VARIANT 1119
FT /note="R -> H (in dbSNP:rs774709566)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046244"
FT VARIANT 1129
FT /note="D -> H (in dbSNP:rs781236853)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046245"
FT VARIANT 1227
FT /note="A -> T (in dbSNP:rs761684414)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046246"
FT VARIANT 1253
FT /note="I -> T (in dbSNP:rs767821521)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046247"
FT VARIANT 1278
FT /note="T -> I (in dbSNP:rs760047247)"
FT /evidence="ECO:0000269|PubMed:18179895"
FT /id="VAR_046248"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5Y4M"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5Y4M"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5Y4M"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5Y4M"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5Y4M"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5Y4M"
FT STRAND 85..101
FT /evidence="ECO:0007829|PDB:5Y4M"
FT STRAND 110..123
FT /evidence="ECO:0007829|PDB:5Y4M"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:5Y4M"
FT STRAND 146..166
FT /evidence="ECO:0007829|PDB:5Y4M"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:5Y4M"
SQ SEQUENCE 1331 AA; 148167 MW; CFB2CB55BEFB99C2 CRC64;
MQAAPRAGCG AALLLWIVSS CLCRAWTAPS TSQKCDEPLV SGLPHVAFSS SSSISGSYSP
GYAKINKRGG AGGWSPSDSD HYQWLQVDFG NRKQISAIAT QGRYSSSDWV TQYRMLYSDT
GRNWKPYHQD GNIWAFPGNI NSDGVVRHEL QHPIIARYVR IVPLDWNGEG RIGLRIEVYG
CSYWADVINF DGHVVLPYRF RNKKMKTLKD VIALNFKTSE SEGVILHGEG QQGDYITLEL
KKAKLVLSLN LGSNQLGPIY GHTSVMTGSL LDDHHWHSVV IERQGRSINL TLDRSMQHFR
TNGEFDYLDL DYEITFGGIP FSGKPSSSSR KNFKGCMESI NYNGVNITDL ARRKKLEPSN
VGNLSFSCVE PYTVPVFFNA TSYLEVPGRL NQDLFSVSFQ FRTWNPNGLL VFSHFADNLG
NVEIDLTESK VGVHINITQT KMSQIDISSG SGLNDGQWHE VRFLAKENFA ILTIDGDEAS
AVRTNSPLQV KTGEKYFFGG FLNQMNNSSH SVLQPSFQGC MQLIQVDDQL VNLYEVAQRK
PGSFANVSID MCAIIDRCVP NHCEHGGKCS QTWDSFKCTC DETGYSGATC HNSIYEPSCE
AYKHLGQTSN YYWIDPDGSG PLGPLKVYCN MTEDKVWTIV SHDLQMQTPV VGYNPEKYSV
TQLVYSASMD QISAITDSAE YCEQYVSYFC KMSRLLNTPD GSPYTWWVGK ANEKHYYWGG
SGPGIQKCAC GIERNCTDPK YYCNCDADYK QWRKDAGFLS YKDHLPVSQV VVGDTDRQGS
EAKLSVGPLR CQGDRNYWNA ASFPNPSSYL HFSTFQGETS ADISFYFKTL TPWGVFLENM
GKEDFIKLEL KSATEVSFSF DVGNGPVEIV VRSPTPLNDD QWHRVTAERN VKQASLQVDR
LPQQIRKAPT EGHTRLELYS QLFVGGAGGQ QGFLGCIRSL RMNGVTLDLE ERAKVTSGFI
SGCSGHCTSY GTNCENGGKC LERYHGYSCD CSNTAYDGTF CNKDVGAFFE EGMWLRYNFQ
APATNARDSS SRVDNAPDQQ NSHPDLAQEE IRFSFSTTKA PCILLYISSF TTDFLAVLVK
PTGSLQIRYN LGGTREPYNI DVDHRNMANG QPHSVNITRH EKTIFLKLDH YPSVSYHLPS
SSDTLFNSPK SLFLGKVIET GKIDQEIHKY NTPGFTGCLS RVQFNQIAPL KAALRQTNAS
AHVHIQGELV ESNCGASPLT LSPMSSATDP WHLDHLDSAS ADFPYNPGQG QAIRNGVNRN
SAIIGGVIAV VIFTILCTLV FLIRYMFRHK GTYHTNEAKG AESAESADAA IMNNDPNFTE
TIDESKKEWL I
