ID ANK3_HUMAN Reviewed; 4377 AA. AC Q12955; B4DIL1; E9PE32; Q5CZH9; Q5VXD5; Q7Z3G4; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 3. DT 28-NOV-2012, entry version 119. DE RecName: Full=Ankyrin-3; DE Short=ANK-3; DE AltName: Full=Ankyrin-G; GN Name=ANK3; 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), AND TISSUE SPECIFICITY. RC TISSUE=Brain stem; RX MEDLINE=95138209; PubMed=7836469; DOI=10.1074/jbc.270.5.2352; RA Kordeli E., Lambert S., Bennett V.; RT "AnkyrinG. A new ankyrin gene with neural-specific isoforms localized RT at the axonal initial segment and node of Ranvier."; RL J. Biol. Chem. 270:2352-2359(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Cervix, and Fetal kidney; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP INTERACTION WITH RHBG. RX PubMed=15611082; DOI=10.1074/jbc.M413351200; RA Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R., RA Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.; RT "The ammonium transporter RhBG: requirement of a tyrosine-based signal RT and ankyrin-G for basolateral targeting and membrane anchorage in RT polarized kidney epithelial cells."; RL J. Biol. Chem. 280:8221-8228(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-533, AND MASS RP SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4298, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [8] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4338, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy RT for identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP VARIANTS ALA-1569; MET-3720 AND PRO-4255, AND ASSOCIATION WITH AUTISM RP SUSCEPTIBILITY. RX PubMed=22865819; DOI=10.1002/humu.22174; RA Bi C., Wu J., Jiang T., Liu Q., Cai W., Yu P., Cai T., Zhao M., RA Jiang Y.H., Sun Z.S.; RT "Mutations of ANK3 identified by exome sequencing are associated with RT autism ausceptibility."; RL Hum. Mutat. 0:0-0(2012). CC -!- FUNCTION: In skeletal muscle, required for costamere localization CC of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. CC May participate in the maintenance/targeting of ion channels and CC cell adhesion molecules at the nodes of Ranvier and axonal initial CC segments. CC -!- SUBUNIT: Directly interacts with DMD and betaDAG1. This CC interaction does not interfere with binding between DMD and CC betaDAG1. It is also required for DMD and betaDAG1 retention at CC costameres (By similarity). May be a constituent of a CC neurofascin/NRCAM/ankyrin G complex. Interacts with RHBG. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, CC synapse, postsynaptic cell membrane (By similarity). Lysosome (By CC similarity). Note=In skeletal muscle, localized at costameres and CC neuromuscular junctions (By similarity). In macrophages, CC associated with lysosomes (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q12955-3; Sequence=Displayed; CC Name=2; CC IsoId=Q12955-4; Sequence=VSP_044349, VSP_044350, VSP_044351, CC VSP_044352, VSP_044353, VSP_044354; CC Name=3; CC IsoId=Q12955-5; Sequence=VSP_044348, VSP_044351, VSP_044352, CC VSP_044353, VSP_044354; CC -!- TISSUE SPECIFICITY: Expressed in brain, neurons and other tissues. CC -!- DOMAIN: The tandem configuration of the two ZU5 and the UPA CC domains forms a structural supramodule termed ZZU. ZU5-1 mediates CC interaction with beta-spectrin, and the ZU5-1/UPA interface is CC required for ankyrin's function other than binding to spectrin (By CC similarity). CC -!- DISEASE: Note=Genetic variations in ANK3 are associated with CC autism spectrum disorders susceptibility. CC -!- SIMILARITY: Contains 23 ANK repeats. CC -!- SIMILARITY: Contains 1 death domain. CC -!- SIMILARITY: Contains 2 ZU5 domains. CC -!- SEQUENCE CAUTION: CC Sequence=CAH73232.1; Type=Erroneous gene model prediction; CC Sequence=CAI40518.1; Type=Erroneous gene model prediction; CC Sequence=CAI41373.1; Type=Erroneous gene model prediction; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry; CC URL="http://en.wikipedia.org/wiki/Ankyrin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U13616; AAA64834.1; -; mRNA. DR EMBL; AK295661; BAG58523.1; -; mRNA. DR EMBL; BX537917; CAD97900.2; -; mRNA. DR EMBL; BX648574; CAI56716.1; -; mRNA. DR EMBL; AL359267; CAH73232.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC023904; CAH73232.1; JOINED; Genomic_DNA. DR EMBL; AL359377; CAH73232.1; JOINED; Genomic_DNA. DR EMBL; AL592430; CAH73232.1; JOINED; Genomic_DNA. DR EMBL; AL592430; CAI40518.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC023904; CAI40518.1; JOINED; Genomic_DNA. DR EMBL; AL359267; CAI40518.1; JOINED; Genomic_DNA. DR EMBL; AL359377; CAI40518.1; JOINED; Genomic_DNA. DR EMBL; AL359377; CAI41373.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC023904; CAI41373.1; JOINED; Genomic_DNA. DR EMBL; AL359267; CAI41373.1; JOINED; Genomic_DNA. DR EMBL; AL592430; CAI41373.1; JOINED; Genomic_DNA. DR IPI; IPI00921566; -. DR PIR; A55575; A55575. DR RefSeq; NP_001191332.1; NM_001204403.1. DR RefSeq; NP_001191333.1; NM_001204404.1. DR RefSeq; NP_066267.2; NM_020987.3. DR UniGene; Hs.499725; -. DR ProteinModelPortal; Q12955; -. DR SMR; Q12955; 37-842, 982-1442, 4090-4167. DR DIP; DIP-49017N; -. DR IntAct; Q12955; 2. DR STRING; Q12955; -. DR PhosphoSite; Q12955; -. DR DMDM; 257051061; -. DR PaxDb; Q12955; -. DR PRIDE; Q12955; -. DR DNASU; 288; -. DR Ensembl; ENST00000280772; ENSP00000280772; ENSG00000151150. DR Ensembl; ENST00000503366; ENSP00000425236; ENSG00000151150. DR GeneID; 288; -. DR KEGG; hsa:288; -. DR UCSC; uc001jky.3; human. DR CTD; 288; -. DR GeneCards; GC10M061788; -. DR H-InvDB; HIX0008849; -. DR HGNC; HGNC:494; ANK3. DR HPA; CAB015179; -. DR MIM; 600465; gene. DR neXtProt; NX_Q12955; -. DR PharmGKB; PA24800; -. DR eggNOG; COG0666; -. DR HOGENOM; HOG000012873; -. DR HOVERGEN; HBG024337; -. DR InParanoid; Q12955; -. DR KO; K10380; -. DR OMA; SYEFTSK; -. DR PhylomeDB; Q12955; -. DR Reactome; REACT_111045; Developmental Biology. DR GenomeRNAi; 288; -. DR NextBio; 1175; -. DR ArrayExpress; Q12955; -. DR Bgee; Q12955; -. DR CleanEx; HS_ANK3; -. DR Genevestigator; Q12955; -. DR GermOnline; ENSG00000151150; Homo sapiens. DR GO; GO:0043194; C:axon initial segment; ISS:BHF-UCL. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL. DR GO; GO:0043034; C:costamere; TAS:BHF-UCL. DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL. DR GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL. DR GO; GO:0033268; C:node of Ranvier; ISS:BHF-UCL. DR GO; GO:0014731; C:spectrin-associated cytoskeleton; ISS:BHF-UCL. DR GO; GO:0030315; C:T-tubule; ISS:BHF-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:BHF-UCL. DR GO; GO:0007409; P:axonogenesis; ISS:BHF-UCL. DR GO; GO:0000281; P:cytokinesis after mitosis; IMP:BHF-UCL. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:BHF-UCL. DR GO; GO:0072660; P:maintenance of protein location in plasma membrane; IGI:BHF-UCL. DR GO; GO:0071709; P:membrane assembly; IMP:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL. DR GO; GO:1900827; P:positive regulation of membrane depolarization involved in regulation of cardiac muscle cell action potential; ISS:BHF-UCL. DR GO; GO:0045838; P:positive regulation of membrane potential; ISS:BHF-UCL. DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL. DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISS:BHF-UCL. DR GO; GO:0072661; P:protein targeting to plasma membrane; IMP:BHF-UCL. DR GO; GO:0019228; P:regulation of action potential in neuron; ISS:BHF-UCL. DR GO; GO:0043266; P:regulation of potassium ion transport; ISS:BHF-UCL. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR Gene3D; 1.25.40.20; ANK; 3. DR Gene3D; 1.10.533.10; DEATH_like; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR000488; Death. DR InterPro; IPR011029; DEATH-like. DR InterPro; IPR000906; ZU5. DR Pfam; PF00023; Ank; 1. DR Pfam; PF12796; Ank_2; 7. DR Pfam; PF00531; Death; 1. DR Pfam; PF00791; ZU5; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 22. DR SMART; SM00005; DEATH; 1. DR SMART; SM00218; ZU5; 1. DR SUPFAM; SSF48403; ANK; 2. DR SUPFAM; SSF47986; DEATH_like; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 21. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS51145; ZU5; 1. PE 1: Evidence at protein level; KW Alternative splicing; ANK repeat; Cell junction; Cell membrane; KW Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond; Lysosome; KW Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; KW Reference proteome; Repeat; Synapse; Ubl conjugation. FT CHAIN 1 4377 Ankyrin-3. FT /FTId=PRO_0000066886. FT REPEAT 73 102 ANK 1. FT REPEAT 106 135 ANK 2. FT REPEAT 139 168 ANK 3. FT REPEAT 172 201 ANK 4. FT REPEAT 203 230 ANK 5. FT REPEAT 234 263 ANK 6. FT REPEAT 267 296 ANK 7. FT REPEAT 300 329 ANK 8. FT REPEAT 333 362 ANK 9. FT REPEAT 366 395 ANK 10. FT REPEAT 399 428 ANK 11. FT REPEAT 432 461 ANK 12. FT REPEAT 465 494 ANK 13. FT REPEAT 498 527 ANK 14. FT REPEAT 531 560 ANK 15. FT REPEAT 564 593 ANK 16. FT REPEAT 597 626 ANK 17. FT REPEAT 630 659 ANK 18. FT REPEAT 663 692 ANK 19. FT REPEAT 696 725 ANK 20. FT REPEAT 729 758 ANK 21. FT REPEAT 762 791 ANK 22. FT REPEAT 795 825 ANK 23. FT DOMAIN 982 1107 ZU5 1. FT DOMAIN 1108 1272 ZU5 2. FT DOMAIN 4090 4174 Death. FT REGION 1273 1407 UPA domain (By similarity). FT COMPBIAS 1519 1898 Ser-rich. FT COMPBIAS 2247 2250 Poly-Thr. FT COMPBIAS 2393 2396 Poly-Glu. FT COMPBIAS 3205 3211 Poly-Glu. FT COMPBIAS 3255 3259 Poly-Pro. FT COMPBIAS 3482 3487 Poly-Ser. FT COMPBIAS 3785 3791 Poly-Asn. FT COMPBIAS 3957 3981 Thr-rich. FT MOD_RES 533 533 Phosphotyrosine. FT MOD_RES 1459 1459 Phosphoserine. FT MOD_RES 4298 4298 Phosphoserine. FT CROSSLNK 4338 4338 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VAR_SEQ 1 37 MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKK -> FT MASSASSSPAGTEDSAPAQGGFGSDYSRSSR (in FT isoform 3). FT /FTId=VSP_044348. FT VAR_SEQ 1 36 MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRK -> M FT SEEPKEKNAKPAHRKRKG (in isoform 2). FT /FTId=VSP_044349. FT VAR_SEQ 872 872 G -> GNRCTWYKIPKVQEFTVKS (in isoform 2). FT /FTId=VSP_044350. FT VAR_SEQ 1442 1450 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_044351. FT VAR_SEQ 1478 4081 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_044352. FT VAR_SEQ 4082 4082 G -> S (in isoform 2 and isoform 3). FT /FTId=VSP_044353. FT VAR_SEQ 4199 4199 G -> GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIE FT SPLRTPSRLSDGLVPSQGNIEHSADGPPVVTAEDASLEDSK FT LEDSVPLTEMPEAVDVDESQLENVCLS (in isoform 2 FT and isoform 3). FT /FTId=VSP_044354. FT VARIANT 1569 1569 S -> A (associated with autism FT susceptibility). FT /FTId=VAR_068702. FT VARIANT 2318 2318 K -> R (in dbSNP:rs59021407). FT /FTId=VAR_061013. FT VARIANT 2885 2885 H -> Q (in dbSNP:rs11599164). FT /FTId=VAR_059115. FT VARIANT 2996 2996 Q -> H (in dbSNP:rs41274672). FT /FTId=VAR_061014. FT VARIANT 3117 3117 I -> V (in dbSNP:rs28932171). FT /FTId=VAR_059116. FT VARIANT 3123 3123 K -> R (in dbSNP:rs10821668). FT /FTId=VAR_059117. FT VARIANT 3720 3720 T -> M (associated with autism FT susceptibility). FT /FTId=VAR_068703. FT VARIANT 4255 4255 T -> P (associated with autism FT susceptibility). FT /FTId=VAR_068704. FT VARIANT 4257 4257 I -> V (in dbSNP:rs12261793). FT /FTId=VAR_054333. FT CONFLICT 197 197 T -> A (in Ref. 3; CAI56716). FT CONFLICT 222 222 L -> P (in Ref. 3; CAD97900). FT CONFLICT 327 327 I -> V (in Ref. 3; CAD97900). FT CONFLICT 338 338 L -> W (in Ref. 2; BAG58523). FT CONFLICT 523 523 A -> T (in Ref. 3; CAD97900). FT CONFLICT 578 578 L -> P (in Ref. 3; CAI56716). FT CONFLICT 1036 1043 MVEGEGLA -> HGERRGIS (in Ref. 1; FT AAA64834). FT CONFLICT 1237 1237 D -> G (in Ref. 3; CAI56716). FT CONFLICT 1418 1418 P -> R (in Ref. 1; AAA64834). FT CONFLICT 1455 1455 D -> E (in Ref. 2; BAG58523). FT CONFLICT 1574 1574 F -> L (in Ref. 1; AAA64834). FT CONFLICT 1685 1685 A -> R (in Ref. 1; AAA64834). FT CONFLICT 1726 1726 P -> A (in Ref. 1; AAA64834). FT CONFLICT 2062 2063 ER -> GG (in Ref. 1; AAA64834). FT CONFLICT 2146 2146 S -> T (in Ref. 1; AAA64834). FT CONFLICT 3919 3919 H -> P (in Ref. 1; AAA64834). SQ SEQUENCE 4377 AA; 480410 MW; F6F9FABD09F15C13 CRC64; MAHAASQLKK NRDLEINAEE EPEKKRKHRK RSRDRKKKSD ANASYLRAAR AGHLEKALDY IKNGVDINIC NQNGLNALHL ASKEGHVEVV SELLQREANV DAATKKGNTA LHIASLAGQA EVVKVLVTNG ANVNAQSQNG FTPLYMAAQE NHLEVVKFLL DNGASQSLAT EDGFTPLAVA LQQGHDQVVS LLLENDTKGK VRLPALHIAA RKDDTKAAAL LLQNDNNADV ESKSGFTPLH IAAHYGNINV ATLLLNRAAA VDFTARNDIT PLHVASKRGN ANMVKLLLDR GAKIDAKTRD GLTPLHCGAR SGHEQVVEML LDRAAPILSK TKNGLSPLHM ATQGDHLNCV QLLLQHNVPV DDVTNDYLTA LHVAAHCGHY KVAKVLLDKK ANPNAKALNG FTPLHIACKK NRIKVMELLL KHGASIQAVT ESGLTPIHVA AFMGHVNIVS QLMHHGASPN TTNVRGETAL HMAARSGQAE VVRYLVQDGA QVEAKAKDDQ TPLHISARLG KADIVQQLLQ QGASPNAATT SGYTPLHLSA REGHEDVAAF LLDHGASLSI TTKKGFTPLH VAAKYGKLEV ANLLLQKSAS PDAAGKSGLT PLHVAAHYDN QKVALLLLDQ GASPHAAAKN GYTPLHIAAK KNQMDIATTL LEYGADANAV TRQGIASVHL AAQEGHVDMV SLLLGRNANV NLSNKSGLTP LHLAAQEDRV NVAEVLVNQG AHVDAQTKMG YTPLHVGCHY GNIKIVNFLL QHSAKVNAKT KNGYTPLHQA AQQGHTHIIN VLLQNNASPN ELTVNGNTAL GIARRLGYIS VVDTLKIVTE ETMTTTTVTE KHKMNVPETM NEVLDMSDDE VRKANAPEML SDGEYISDVE EGEDAMTGDT DKYLGPQDLK ELGDDSLPAE GYMGFSLGAR SASLRSFSSD RSYTLNRSSY ARDSMMIEEL LVPSKEQHLT FTREFDSDSL RHYSWAADTL DNVNLVSSPI HSGFLVSFMV DARGGSMRGS RHHGMRIIIP PRKCTAPTRI TCRLVKRHKL ANPPPMVEGE GLASRLVEMG PAGAQFLGPV IVEIPHFGSM RGKERELIVL RSENGETWKE HQFDSKNEDL TELLNGMDEE LDSPEELGKK RICRIITKDF PQYFAVVSRI KQESNQIGPE GGILSSTTVP LVQASFPEGA LTKRIRVGLQ AQPVPDEIVK KILGNKATFS PIVTVEPRRR KFHKPITMTI PVPPPSGEGV SNGYKGDTTP NLRLLCSITG GTSPAQWEDI TGTTPLTFIK DCVSFTTNVS ARFWLADCHQ VLETVGLATQ LYRELICVPY MAKFVVFAKM NDPVESSLRC FCMTDDKVDK TLEQQENFEE VARSKDIEVL EGKPIYVDCY GNLAPLTKGG QQLVFNFYSF KENRLPFSIK IRDTSQEPCG RLSFLKEPKT TKGLPQTAVC NLNITLPAHK KETESDQDDE IEKTDRRQSF ASLALRKRYS YLTEPGMIER STGATRSLPT TYSYKPFFST RPYQSWTTAP ITVPGPAKSG FTSLSSSSSN TPSASPLKSI WSVSTPSPIK STLGASTTSS VKSISDVASP IRSFRTMSSP IKTVVSQSPY NIQVSSGTLA RAPAVTEATP LKGLASNSTF SSRTSPVTTA GSLLERSSIT MTPPASPKSN INMYSSSLPF KSIITSAAPL ISSPLKSVVS PVKSAVDVIS SAKITMASSL SSPVKQMPGH AEVALVNGSI SPLKYPSSST LINGCKATAT LQEKISSATN SVSSVVSAAT DTVEKVFSTT TAMPFSPLRS YVSAAPSAFQ SLRTPSASAL YTSLGSSISA TTSSVTSSII TVPVYSVVNV LPEPALKKLP DSNSFTKSAA ALLSPIKTLT TETHPQPHFS RTSSPVKSSL FLAPSALKLS TPSSLSSSQE ILKDVAEMKE DLMRMTAILQ TDVPEEKPFQ PELPKEGRID DEEPFKIVEK VKEDLVKVSE ILKKDVCVDN KGSPKSPKSD KGHSPEDDWI EFSSEEIREA RQQAAASQSP SLPERVQVKA KAASEKDYNL TKVIDYLTND IGSSSLTNLK YKFEDAKKDG EERQKRVLKP AIALQEHKLK MPPASMRTST SEKELCKMAD SFFGTDTILE SPDDFSQHDQ DKSPLSDSGF ETRSEKTPSA PQSAESTGPK PLFHEVPIPP VITETRTEVV HVIRSYDPSA GDVPQTQPEE PVSPKPSPTF MELEPKPTTS SIKEKVKAFQ MKASSEEDDH NRVLSKGMRV KEETHITTTT RMVYHSPPGG EGASERIEET MSVHDIMKAF QSGRDPSKEL AGLFEHKSAV SPDVHKSAAE TSAQHAEKDN QMKPKLERII EVHIEKGNQA EPTEVIIRET KKHPEKEMYV YQKDLSRGDI NLKDFLPEKH DAFPCSEEQG QQEEEELTAE ESLPSYLESS RVNTPVSQEE DSRPSSAQLI SDDSYKTLKL LSQHSIEYHD DELSELRGES YRFAEKMLLS EKLDVSHSDT EESVTDHAGP PSSELQGSDK RSREKIATAP KKEILSKIYK DVSENGVGKV SKDEHFDKVT VLHYSGNVSS PKHAMWMRFT EDRLDRGREK LIYEDRVDRT VKEAEEKLTE VSQFFRDKTE KLNDELQSPE KKARPKNGKE YSSQSPTSSS PEKVLLTELL ASNDEWVKAR QHGPDGQGFP KAEEKAPSLP SSPEKMVLSQ QTEDSKSTVE AKGSISQSKA PDGPQSGFQL KQSKLSSIRL KFEQGTHAKS KDMSQEDRKS DGQSRIPVKK IQESKLPVYQ VFAREKQQKA IDLPDESVSV QKDFMVLKTK DEHAQSNEIV VNDSGSDNVK KQRTEMSSKA MPDSFSEQQA KDLACHITSD LATRGPWDKK VFRTWESSGA TNNKSQKEKL SHVLVHDVRE NHIGHPESKS VDQKNEFMSV TERERKLLTN GSLSEIKEMT VKSPSKKVLY REYVVKEGDH PGGLLDQPSR RSESSAVSHI PVRVADERRM LSSNIPDGFC EQSAFPKHEL SQKLSQSSMS KETVETQHFN SIEDEKVTYS EISKVSKHQS YVGLCPPLEE TETSPTKSPD SLEFSPGKES PSSDVFDHSP IDGLEKLAPL AQTEGGKEIK TLPVYVSFVQ VGKQYEKEIQ QGGVKKIISQ ECKTVQETRG TFYTTRQQKQ PPSPQGSPED DTLEQVSFLD SSGKSPLTPE TPSSEEVSYE FTSKTPDSLI AYIPGKPSPI PEVSEESEEE EQAKSTSLKQ TTVEETAVER EMPNDVSKDS NQRPKNNRVA YIEFPPPPPL DADQIESDKK HHYLPEKEVD MIEVNLQDEH DKYQLAEPVI RVQPPSPVPP GADVSDSSDD ESIYQPVPVK KYTFKLKEVD DEQKEKPKAS AEKASNQKEL ESNGSGKDNE FGLGLDSPQN EIAQNGNNDQ SITECSIATT AEFSHDTDAT EIDSLDGYDL QDEDDGLTES DSKLPIQAME IKKDIWNTEG ILKPADRSFS QSKLEVIEEE GKVGPDEDKP PSKSSSSEKT PDKTDQKSGA QFFTLEGRHP DRSVFPDTYF SYKVDEEFAT PFKTVATKGL DFDPWSNNRG DDEVFDSKSR EDETKPFGLA VEDRSPATTP DTTPARTPTD ESTPTSEPNP FPFHEGKMFE MTRSGAIDMS KRDFVEERLQ FFQIGEHTSE GKSGDQGEGD KSMVTATPQP QSGDTTVETN LERNVETPTV EPNPSIPTSG ECQEGTSSSG SLEKSAAATN TSKVDPKLRT PIKMGISAST MTMKKEGPGE ITDKIEAVMT SCQGLENETI TMISNTANSQ MGVRPHEKHD FQKDNFNNNN NLDSSTIQTD NIMSNIVLTE HSAPTCTTEK DNPVKVSSGK KTGVLQGHCV RDKQKVLGEQ QKTKELIGIR QKSKLPIKAT SPKDTFPPNH MSNTKASKMK QVSQSEKTKA LTTSSCVDVK SRIPVKNTHR DNIIAVRKAC ATQKQGQPEK GKAKQLPSKL PVKVRSTCVT TTTTTATTTT TTTTTTTTSC TVKVRKSQLK EVCKHSIEYF KGISGETLKL VDRLSEEEKK MQSELSDEEE STSRNTSLSE TSRGGQPSVT TKSARDKKTE AAPLKSKSEK AGSEKRSSRR TGPQSPCERT DIRMAIVADH LGLSWTELAR ELNFSVDEIN QIRVENPNSL ISQSFMLLKK WVTRDGKNAT TDALTSVLTK INRIDIVTLL EGPIFDYGNI SGTRSFADEN NVFHDPVDGW QNETSSGNLE SCAQARRVTG GLLDRLDDSP DQCRDSITSY LKGEAGKFEA NGSHTEITPE AKTKSYFPES QNDVGKQSTK ETLKPKIHGS GHVEEPASPL AAYQKSLEET SKLIIEETKP CVPVSMKKMS RTSPADGKPR LSLHEEEGSS GSEQKQGEGF KVKTKKEIRH VEKKSHS //