GenomeNet

Database: UniProt
Entry: Q9UHC6
LinkDB: Q9UHC6
Original site: Q9UHC6 
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   13-FEB-2019, entry version 186.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH KCNA2, AND
RP   TISSUE 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.,
RA   Salzer J.L., 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
RT   over 2 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.,
RA   Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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.,
RA   Dobrin S.E., 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.,
RA   Collins A.L., Bijlsma E.K., Oortveld M.A., Ekici A.B., Reis A.,
RA   Schenck A., Rauch A.;
RT   "CNTNAP2 and NRXN1 are mutated in autosomal-recessive Pitt-Hopkins-
RT   like mental retardation and determine the level of a common synaptic
RT   protein in Drosophila.";
RL   Am. J. Hum. Genet. 85:655-666(2009).
RN   [9]
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;
RP   ASP-779; THR-869; HIS-906; ASN-1038; ALA-1102; GLY-1114; HIS-1119;
RP   HIS-1129; THR-1227; THR-1253 AND ILE-1278, AND CHROMOSOMAL
RP   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.,
RA   Stillman A.A., Tanriover G., Abrahams B.S., Duvall J.A., Robbins E.M.,
RA   Geschwind D.H., Biederer T., Gunel M., Lifton R.P., State M.W.;
RT   "Molecular cytogenetic analysis and resequencing of contactin
RT   associated protein-like 2 in autism spectrum disorders.";
RL   Am. J. Hum. Genet. 82:165-173(2008).
RN   [10]
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, with CNTNAP1, for radial and longitudinal
CC       organization of myelinated axons. Plays a role in the formation of
CC       functional distinct domains critical for saltatory conduction of
CC       nerve impulses in myelinated nerve fibers. Demarcates the
CC       juxtaparanodal region of the axo-glial junction.
CC       {ECO:0000250|UniProtKB:Q9CPW0}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with KCNA2.
CC       {ECO:0000269|PubMed:10624965}.
CC   -!- INTERACTION:
CC       P27824:CANX; NbExp=2; IntAct=EBI-16594440, EBI-355947;
CC       Q12860:CNTN1; NbExp=5; IntAct=EBI-310892, EBI-5564336;
CC       P50222:MEOX2; NbExp=3; IntAct=EBI-310892, EBI-748397;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9CPW0};
CC       Single-pass type I membrane protein {ECO:0000305}. Cell
CC       projection, axon {ECO:0000250|UniProtKB:Q9CPW0}. Cell junction,
CC       paranodal septate junction {ECO:0000250|UniProtKB:Q9CPW0}.
CC       Note=Expressed in the juxtaparadonal region.
CC       {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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in nervous system.
CC       {ECO:0000269|PubMed:10624965}.
CC   -!- DISEASE: Autism 15 (AUTS15) [MIM:612100]: A complex
CC       multifactorial, pervasive developmental disorder characterized by
CC       impairments in reciprocal social interaction and communication,
CC       restricted and stereotyped patterns of interests and activities,
CC       and the presence of developmental abnormalities by 3 years of age.
CC       Most individuals with autism also manifest moderate mental
CC       retardation. {ECO:0000269|PubMed:18179895}. Note=Disease
CC       susceptibility is associated with variations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Note=A chromosomal aberration involving CNTNAP2 is found
CC       in a patient with autism spectrum disorder. Paracentric inversion
CC       46,XY,inv(7)(q11.22;q35). The inversion breakpoints disrupt the
CC       genes AUTS2 and CNTNAP2.
CC   -!- DISEASE: Pitt-Hopkins-like syndrome 1 (PTHSL1) [MIM:610042]: A
CC       syndrome characterized by severe mental retardation and variable
CC       additional symptoms, such as impaired speech development,
CC       seizures, autistic behavior, breathing anomalies and a broad
CC       mouth, resembling Pitt-Hopkins syndrome. In contrast to patients
CC       with Pitt-Hopkins syndrome, PTHSL1 patients present with normal or
CC       only mildly to moderately delayed motor milestones.
CC       {ECO:0000269|PubMed:16571880, ECO:0000269|PubMed:19896112}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA74891.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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   UniGene; Hs.655684; -.
DR   PDB; 5Y4M; X-ray; 1.31 A; A=35-181.
DR   PDBsum; 5Y4M; -.
DR   ProteinModelPortal; Q9UHC6; -.
DR   SMR; Q9UHC6; -.
DR   BioGrid; 117510; 8.
DR   IntAct; Q9UHC6; 12.
DR   MINT; Q9UHC6; -.
DR   STRING; 9606.ENSP00000354778; -.
DR   iPTMnet; Q9UHC6; -.
DR   PhosphoSitePlus; Q9UHC6; -.
DR   SwissPalm; Q9UHC6; -.
DR   BioMuta; CNTNAP2; -.
DR   DMDM; 17433089; -.
DR   EPD; Q9UHC6; -.
DR   jPOST; Q9UHC6; -.
DR   PaxDb; Q9UHC6; -.
DR   PeptideAtlas; Q9UHC6; -.
DR   PRIDE; Q9UHC6; -.
DR   ProteomicsDB; 84311; -.
DR   ProteomicsDB; 84312; -. [Q9UHC6-2]
DR   Ensembl; ENST00000361727; ENSP00000354778; ENSG00000174469. [Q9UHC6-1]
DR   Ensembl; ENST00000463592; ENSP00000486292; ENSG00000174469. [Q9UHC6-2]
DR   Ensembl; ENST00000613345; ENSP00000481057; ENSG00000278728. [Q9UHC6-2]
DR   Ensembl; ENST00000649351; ENSP00000496805; ENSG00000174469. [Q9UHC6-1]
DR   GeneID; 26047; -.
DR   KEGG; hsa:26047; -.
DR   UCSC; uc003weu.3; human. [Q9UHC6-1]
DR   CTD; 26047; -.
DR   DisGeNET; 26047; -.
DR   EuPathDB; HostDB:ENSG00000174469.17; -.
DR   GeneCards; CNTNAP2; -.
DR   HGNC; HGNC:13830; CNTNAP2.
DR   HPA; HPA002739; -.
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; Cortical dysplasia-focal epilepsy syndrome.
DR   Orphanet; 106; NON RARE IN EUROPE: Autism.
DR   Orphanet; 221150; Pitt-Hopkins-like syndrome.
DR   PharmGKB; PA26692; -.
DR   eggNOG; KOG3516; Eukaryota.
DR   eggNOG; ENOG410XPHG; LUCA.
DR   GeneTree; ENSGT00940000154516; -.
DR   HOGENOM; HOG000230964; -.
DR   HOVERGEN; HBG057718; -.
DR   InParanoid; Q9UHC6; -.
DR   KO; K07380; -.
DR   OMA; GGRCKQT; -.
DR   OrthoDB; 338397at2759; -.
DR   PhylomeDB; Q9UHC6; -.
DR   TreeFam; TF321823; -.
DR   SIGNOR; Q9UHC6; -.
DR   ChiTaRS; CNTNAP2; human.
DR   GeneWiki; CNTNAP2; -.
DR   GenomeRNAi; 26047; -.
DR   PRO; PR:Q9UHC6; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000174469; Expressed in 163 organ(s), highest expression level in forebrain.
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: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: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   Gene3D; 2.60.120.260; -; 1.
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; PTHR43925:SF3; PTHR43925:SF3; 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;
KW   Chromosomal rearrangement; Complete proteome; Disulfide bond;
KW   EGF-like domain; Epilepsy; Glycoprotein; Membrane; Mental retardation;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   1331       Contactin-associated protein-like 2.
FT                                /FTId=PRO_0000019506.
FT   TOPO_DOM     28   1262       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1263   1283       Helical. {ECO:0000255}.
FT   TOPO_DOM   1284   1331       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       35    181       F5/8 type C. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN      216    368       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      401    552       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      554    591       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      592    798       Fibrinogen C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   DOMAIN      799    963       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      963   1002       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1055   1214       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   MOD_RES    1303   1303       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9CPW0}.
FT   MOD_RES    1306   1306       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9CPW0}.
FT   CARBOHYD    289    289       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    346    346       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    379    379       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    436    436       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    506    506       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    507    507       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    546    546       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    630    630       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    735    735       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1116   1116       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1198   1198       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     35    181       {ECO:0000250}.
FT   DISULFID    336    368       {ECO:0000250}.
FT   DISULFID    520    552       {ECO:0000250}.
FT   DISULFID    558    569       {ECO:0000250}.
FT   DISULFID    563    578       {ECO:0000250}.
FT   DISULFID    580    590       {ECO:0000250}.
FT   DISULFID    936    963       {ECO:0000250}.
FT   DISULFID    967    980       {ECO:0000250}.
FT   DISULFID    974    989       {ECO:0000250}.
FT   DISULFID    991   1001       {ECO:0000250}.
FT   DISULFID   1178   1214       {ECO:0000250}.
FT   VAR_SEQ       1   1223       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_014976.
FT   VARIANT     114    114       R -> Q (in dbSNP:rs189731792).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046227.
FT   VARIANT     218    218       T -> M (in dbSNP:rs771028883).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046228.
FT   VARIANT     226    226       L -> M (in dbSNP:rs372345438).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046229.
FT   VARIANT     283    283       R -> C (in dbSNP:rs794727802).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046230.
FT   VARIANT     382    382       S -> N (in dbSNP:rs371839994).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046231.
FT   VARIANT     407    407       N -> S (in dbSNP:rs143877693).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046232.
FT   VARIANT     418    418       N -> D (in dbSNP:rs772179690).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046233.
FT   VARIANT     680    680       E -> K (in dbSNP:rs368905425).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046234.
FT   VARIANT     699    699       P -> Q (in dbSNP:rs764412489).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046235.
FT   VARIANT     716    716       Y -> C (in dbSNP:rs760930032).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046236.
FT   VARIANT     731    731       G -> S (in dbSNP:rs369867547).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046237.
FT   VARIANT     779    779       G -> D (in dbSNP:rs200413148).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046238.
FT   VARIANT     869    869       I -> T (rare polymorphism; may be a risk
FT                                factor for autism; dbSNP:rs121908445).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046239.
FT   VARIANT     906    906       R -> H (in dbSNP:rs759801195).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046240.
FT   VARIANT    1038   1038       D -> N (in dbSNP:rs144003410).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046241.
FT   VARIANT    1102   1102       V -> A (in dbSNP:rs111599875).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046242.
FT   VARIANT    1114   1114       S -> G (in dbSNP:rs983036503).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046243.
FT   VARIANT    1119   1119       R -> H (in dbSNP:rs774709566).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046244.
FT   VARIANT    1129   1129       D -> H (in dbSNP:rs781236853).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046245.
FT   VARIANT    1227   1227       A -> T (in dbSNP:rs761684414).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046246.
FT   VARIANT    1253   1253       I -> T (in dbSNP:rs767821521).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046247.
FT   VARIANT    1278   1278       T -> I (in dbSNP:rs760047247).
FT                                {ECO:0000269|PubMed:18179895}.
FT                                /FTId=VAR_046248.
FT   STRAND       37     40       {ECO:0000244|PDB:5Y4M}.
FT   HELIX        45     47       {ECO:0000244|PDB:5Y4M}.
FT   STRAND       48     51       {ECO:0000244|PDB:5Y4M}.
FT   HELIX        56     58       {ECO:0000244|PDB:5Y4M}.
FT   HELIX        60     62       {ECO:0000244|PDB:5Y4M}.
FT   STRAND       72     74       {ECO:0000244|PDB:5Y4M}.
FT   STRAND       85    101       {ECO:0000244|PDB:5Y4M}.
FT   STRAND      110    123       {ECO:0000244|PDB:5Y4M}.
FT   STRAND      140    143       {ECO:0000244|PDB:5Y4M}.
FT   STRAND      146    166       {ECO:0000244|PDB:5Y4M}.
FT   STRAND      174    181       {ECO:0000244|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
//
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