ID ANK3_HUMAN Reviewed; 4377 AA. AC Q12955; B1AQT2; B4DIL1; E9PE32; Q13484; Q5CZH9; Q5VXD5; Q7Z3G4; AC Q9H0P5; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 3. DT 09-DEC-2015, entry version 154. 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 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 [MRNA] (ISOFORM 5), FUNCTION (ISOFORM 5), AND RP SUBCELLULAR LOCATION (ISOFORM 5). RC TISSUE=Kidney; RX PubMed=8666667; DOI=10.1083/jcb.133.4.819; RA Devarajan P., Stabach P.R., Mann A.S., Ardito T., Kashgarian M., RA Morrow J.S.; RT "Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney RT and muscle that binds beta I sigma spectrin and associates with the RT Golgi apparatus."; RL J. Cell Biol. 133:819-830(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Kidney; RX PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] 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 [5] 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 [6] 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 [7] 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 [8] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4338. 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 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 [10] RP INTERACTION WITH PLEC AND FLNC, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002; RA Maiweilidan Y., Klauza I., Kordeli E.; RT "Novel interactions of ankyrins-G at the costameres: the muscle- RT specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin RT and filamin C."; RL Exp. Cell Res. 317:724-736(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-847; SER-1445 RP AND SER-4298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4229; SER-4290 AND RP SER-4298, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1632 AND RP SER-1658 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-1625 AND SER-1651 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-765 AND SER-791 (ISOFORM 4), PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-468 (ISOFORM 5), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP INTERACTION WITH KCNA1. RX PubMed=23903368; DOI=10.1038/ki.2013.280; RA San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G., RA Bindels R.J.; RT "Ankyrin-3 is a novel binding partner of the voltage-gated potassium RT channel Kv1.1 implicated in renal magnesium handling."; RL Kidney Int. 85:94-102(2014). RN [14] RP VARIANTS ALA-1569; MET-3720 AND PRO-4255, AND POSSIBLE INVOLVEMENT IN RP SUSCEPTIBILITY TO AUTISM. 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 susceptibility."; RL Hum. Mutat. 33:1635-1638(2012). RN [15] RP INVOLVEMENT IN MRT37. RX PubMed=23390136; DOI=10.1093/hmg/ddt043; RA Iqbal Z., Vandeweyer G., van der Voet M., Waryah A.M., Zahoor M.Y., RA Besseling J.A., Roca L.T., Vulto-van Silfhout A.T., Nijhof B., RA Kramer J.M., Van der Aa N., Ansar M., Peeters H., Helsmoortel C., RA Gilissen C., Vissers L.E., Veltman J.A., de Brouwer A.P., RA Frank Kooy R., Riazuddin S., Schenck A., van Bokhoven H., Rooms L.; RT "Homozygous and heterozygous disruptions of ANK3: at the crossroads of RT neurodevelopmental and psychiatric disorders."; RL Hum. Mol. Genet. 22:1960-1970(2013). 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. Regulates KCNA1 channel activity in function of dietary CC Mg(2+) levels, and thereby contributes to the regulation of renal CC Mg(2+) reabsorption (PubMed:23903368). {ECO:0000250, CC ECO:0000269|PubMed:17974005}. CC -!- FUNCTION: Isoform 5: May be part of a Golgi-specific membrane CC cytoskeleton in association with beta-spectrin. CC {ECO:0000305|PubMed:17974005}. 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). Interacts (via N-terminal ANK repeats) CC with SCHIP1 isoform 5 (via C-terminus); this interaction is CC required for the localization at axon initial segments (AISs) and CC nodes of Ranvier (NRs) (By similarity). May be a constituent of a CC neurofascin/NRCAM/ankyrin G complex. Interacts with RHBG CC (PubMed:15611082). Interacts with PLEC and FLNC (PubMed:21223964). CC Interacts with KCNA1; this inhibits channel activity CC (PubMed:23903368). {ECO:0000250|UniProtKB:G5E8K5, CC ECO:0000269|PubMed:15611082, ECO:0000269|PubMed:21223964, CC ECO:0000269|PubMed:23903368}. CC -!- INTERACTION: CC Q15796:SMAD2; NbExp=2; IntAct=EBI-2691178, EBI-1040141; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:21223964}. Cell projection, axon CC {ECO:0000250}. Cell membrane, sarcolemma CC {ECO:0000269|PubMed:21223964}. Cell junction, synapse, CC postsynaptic cell membrane {ECO:0000250}. Lysosome {ECO:0000250}. CC Note=In skeletal muscle, localized at costameres and neuromuscular CC junctions. In macrophages, associated with lysosomes. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:8666667}. Golgi apparatus CC {ECO:0000269|PubMed:8666667}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; 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 Note=Contains a phosphoserine at position 1632. Contains a CC phosphoserine at position 1658. {ECO:0000244|PubMed:24275569}; CC Name=3; CC IsoId=Q12955-5; Sequence=VSP_044348, VSP_044351, VSP_044352, CC VSP_044353, VSP_044354; CC Note=Contains a phosphoserine at position 1625. Contains a CC phosphoserine at position 1651. {ECO:0000244|PubMed:24275569}; CC Name=4; CC IsoId=Q12955-6; Sequence=VSP_046885, VSP_046886, VSP_044351, CC VSP_044352, VSP_044353, VSP_044354; CC Note=Ref.3 (CAB66645) sequence(s) differ(s) from that shown due CC to (a) frameshift(s) in position(s) 810. Contains a CC phosphoserine at position 765. Contains a phosphoserine at CC position 791. {ECO:0000244|PubMed:24275569}; CC Name=5; Synonyms=AnkG119, Golgi ankyrin; CC IsoId=Q12955-7; Sequence=VSP_053753, VSP_053754, VSP_053755, CC VSP_053756, VSP_053757, VSP_044351, CC VSP_053758, VSP_053759; CC Note=Avidly binds beta spectrin. Contains a phosphoserine at CC position 468. {ECO:0000244|PubMed:24275569}; CC -!- TISSUE SPECIFICITY: Expressed in brain, neurons, muscles and other CC tissues. {ECO:0000269|PubMed:21223964, CC ECO:0000269|PubMed:7836469}. CC -!- DEVELOPMENTAL STAGE: Up-regulated during muscle cell CC differentiation. {ECO:0000269|PubMed:21223964}. 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). {ECO:0000250}. CC -!- DISEASE: Note=Genetic variations in ANK3 may be associated with CC autism spectrum disorders susceptibility. CC -!- DISEASE: Mental retardation, autosomal recessive 37 (MRT37) CC [MIM:615493]: A disorder characterized by significantly below CC average general intellectual functioning associated with CC impairments in adaptive behavior and manifested during the CC developmental period. MRT37 patients manifest delayed global CC development with speech delay, hypotonia, spasticity, and a sleep CC disorder. Severe behavioral abnormalities include aggression, CC hyperactivity, and grinding of the teeth. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC A homozygous deletion in ANK3 predicted to result in frameshift CC and premature truncation, has been shown to be the cause of CC moderate intellectual disability, an ADHD-like phenotype and CC behavioral problems in a consanguineous family (PubMed:23390136). CC {ECO:0000269|PubMed:23390136}. CC -!- SIMILARITY: Contains 23 ANK repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00023}. CC -!- SIMILARITY: Contains 1 death domain. {ECO:0000255|PROSITE- CC ProRule:PRU00064}. CC -!- SIMILARITY: Contains 2 ZU5 domains. {ECO:0000255|PROSITE- CC ProRule:PRU00485}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry; CC URL="https://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; U43965; AAB08437.1; -; mRNA. DR EMBL; AL136710; CAB66645.1; ALT_FRAME; mRNA. DR EMBL; AK295661; BAG58523.1; -; mRNA. DR EMBL; BX537917; CAD97900.2; -; mRNA. DR EMBL; BX648574; CAI56716.1; -; mRNA. DR EMBL; AC022390; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC023904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359267; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359377; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391707; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL592430; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL607065; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS55711.1; -. [Q12955-4] DR CCDS; CCDS55712.1; -. [Q12955-5] DR CCDS; CCDS7258.1; -. [Q12955-3] DR CCDS; CCDS7259.1; -. [Q12955-6] DR PIR; A55575; A55575. DR RefSeq; NP_001140.2; NM_001149.3. [Q12955-6] DR RefSeq; NP_001191332.1; NM_001204403.1. [Q12955-5] DR RefSeq; NP_001191333.1; NM_001204404.1. [Q12955-4] DR RefSeq; NP_066267.2; NM_020987.3. [Q12955-3] DR UniGene; Hs.499725; -. DR UniGene; Hs.690023; -. DR UniGene; Hs.731403; -. DR UniGene; Hs.740100; -. DR PDB; 4O6X; X-ray; 2.10 A; A/B=4088-4199. DR PDBsum; 4O6X; -. DR ProteinModelPortal; Q12955; -. DR SMR; Q12955; 35-818, 982-1442, 4088-4187. DR BioGrid; 106785; 24. DR DIP; DIP-49017N; -. DR IntAct; Q12955; 10. DR STRING; 9606.ENSP00000280772; -. DR PhosphoSite; Q12955; -. DR BioMuta; ANK3; -. DR DMDM; 257051061; -. DR MaxQB; Q12955; -. DR PaxDb; Q12955; -. DR PRIDE; Q12955; -. DR DNASU; 288; -. DR Ensembl; ENST00000280772; ENSP00000280772; ENSG00000151150. [Q12955-3] DR Ensembl; ENST00000355288; ENSP00000347436; ENSG00000151150. [Q12955-6] DR Ensembl; ENST00000373827; ENSP00000362933; ENSG00000151150. [Q12955-5] DR Ensembl; ENST00000503366; ENSP00000425236; ENSG00000151150. [Q12955-4] DR GeneID; 288; -. DR KEGG; hsa:288; -. DR UCSC; uc001jky.3; human. [Q12955-3] DR UCSC; uc001jkz.4; human. [Q12955-5] DR UCSC; uc010qih.2; human. [Q12955-4] DR CTD; 288; -. DR GeneCards; ANK3; -. DR H-InvDB; HIX0008849; -. DR HGNC; HGNC:494; ANK3. DR HPA; CAB013249; -. DR HPA; CAB015179; -. DR HPA; HPA055643; -. DR MalaCards; ANK3; -. DR MIM; 600465; gene. DR MIM; 615493; phenotype. DR neXtProt; NX_Q12955; -. DR Orphanet; 356996; Intellectual disability - hypotonia - spasticity - sleep disorder. DR Orphanet; 3140; Schizophrenia. DR PharmGKB; PA24800; -. DR eggNOG; KOG4177; Eukaryota. DR eggNOG; COG0666; LUCA. DR GeneTree; ENSGT00760000118950; -. DR HOGENOM; HOG000008707; -. DR HOVERGEN; HBG024337; -. DR InParanoid; Q12955; -. DR KO; K10380; -. DR OMA; DQSITEC; -. DR OrthoDB; EOG7P02H2; -. DR PhylomeDB; Q12955; -. DR TreeFam; TF351263; -. DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins. DR ChiTaRS; ANK3; human. DR GeneWiki; ANK3; -. DR GenomeRNAi; 288; -. DR NextBio; 1175; -. DR PRO; PR:Q12955; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; Q12955; -. DR CleanEx; HS_ANK3; -. DR ExpressionAtlas; Q12955; baseline and differential. DR Genevisible; Q12955; HS. 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:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL. DR GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0033268; C:node of Ranvier; ISS:BHF-UCL. DR GO; GO:0033270; C:paranode region of axon; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042383; C:sarcolemma; IDA: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:0045296; F:cadherin binding; ISS:BHF-UCL. DR GO; GO:0008092; F:cytoskeletal protein binding; ISS:BHF-UCL. DR GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL. DR GO; GO:0030674; F:protein binding, bridging; ISS:BHF-UCL. DR GO; GO:0030507; F:spectrin binding; ISS:BHF-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:BHF-UCL. DR GO; GO:0007411; P:axon guidance; IEA:Ensembl. DR GO; GO:0007409; P:axonogenesis; ISS:BHF-UCL. DR GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB. DR GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; TAS:ProtInc. DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:BHF-UCL. DR GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB. 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:0000281; P:mitotic cytokinesis; IMP:BHF-UCL. DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB. DR GO; GO:0019228; P:neuronal action potential; ISS:BHF-UCL. DR GO; GO:0007009; P:plasma membrane organization; 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 during 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:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL. DR GO; GO:0072661; P:protein targeting to plasma membrane; IMP: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 GO; GO:0050808; P:synapse organization; IEA:Ensembl. DR Gene3D; 1.10.533.10; -; 1. DR Gene3D; 1.25.40.20; -; 3. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR011029; DEATH-like_dom. DR InterPro; IPR000488; Death_domain. DR InterPro; IPR000906; ZU5_dom. DR Pfam; PF00023; Ank; 1. DR Pfam; PF12796; Ank_2; 6. DR Pfam; PF13606; Ank_3; 1. 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; SSF47986; SSF47986; 1. DR SUPFAM; SSF48403; SSF48403; 3. 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 3D-structure; Alternative splicing; ANK repeat; KW Autism spectrum disorder; Cell junction; Cell membrane; KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; KW Golgi apparatus; Isopeptide bond; Lysosome; Membrane; KW Mental retardation; Phosphoprotein; Polymorphism; KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; KW 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. {ECO:0000255|PROSITE- FT ProRule:PRU00485}. FT DOMAIN 1108 1272 ZU5 2. {ECO:0000255|PROSITE- FT ProRule:PRU00485}. FT DOMAIN 4090 4174 Death. {ECO:0000255|PROSITE- FT ProRule:PRU00064}. FT REGION 1273 1407 UPA domain. {ECO:0000250}. 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 39 39 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 623 623 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 847 847 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 861 861 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 867 867 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 913 913 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 916 916 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 922 922 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 957 957 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 959 959 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 1113 1113 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 1445 1445 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 1459 1459 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 1470 1470 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 1622 1622 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 1625 1625 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 1984 1984 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 2111 2111 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 2123 2123 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 2126 2126 Phosphoserine. FT {ECO:0000250|UniProtKB:O70511}. FT MOD_RES 4211 4211 Phosphoserine. FT {ECO:0000250|UniProtKB:G5E8K5}. FT MOD_RES 4229 4229 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 4290 4290 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 4298 4298 Phosphoserine. FT {ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT CROSSLNK 4338 4338 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000269|PubMed:17370265}. FT VAR_SEQ 1 866 Missing (in isoform 4). FT {ECO:0000303|PubMed:11230166}. FT /FTId=VSP_046885. FT VAR_SEQ 1 37 MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKK -> FT MASSASSSPAGTEDSAPAQGGFGSDYSRSSR (in FT isoform 3). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_044348. FT VAR_SEQ 1 36 MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRK -> M FT SEEPKEKNAKPAHRKRKG (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_044349. FT VAR_SEQ 1 6 MAHAAS -> MNLRCD (in isoform 5). FT {ECO:0000303|PubMed:8666667}. FT /FTId=VSP_053753. FT VAR_SEQ 7 385 Missing (in isoform 5). FT {ECO:0000303|PubMed:8666667}. FT /FTId=VSP_053754. FT VAR_SEQ 850 870 Missing (in isoform 5). FT {ECO:0000303|PubMed:8666667}. FT /FTId=VSP_053755. FT VAR_SEQ 867 872 SDVEEG -> MALPQS (in isoform 4). FT {ECO:0000303|PubMed:11230166}. FT /FTId=VSP_046886. FT VAR_SEQ 872 872 G -> GNRCTWYKIPKVQEFTVKS (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_044350. FT VAR_SEQ 913 918 Missing (in isoform 5). FT {ECO:0000303|PubMed:8666667}. FT /FTId=VSP_053756. FT VAR_SEQ 1036 1043 MVEGEGLA -> HGERRGIS (in isoform 5). FT {ECO:0000303|PubMed:8666667}. FT /FTId=VSP_053757. FT VAR_SEQ 1442 1450 Missing (in isoform 2, isoform 3, isoform FT 4 and isoform 5). FT {ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:8666667}. FT /FTId=VSP_044351. FT VAR_SEQ 1478 4081 Missing (in isoform 2, isoform 3 and FT isoform 4). {ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005}. FT /FTId=VSP_044352. FT VAR_SEQ 1478 1880 IERSTGATRSLPTTYSYKPFFSTRPYQSWTTAPITVPGPAK FT SGFTSLSSSSSNTPSASPLKSIWSVSTPSPIKSTLGASTTS FT SVKSISDVASPIRSFRTMSSPIKTVVSQSPYNIQVSSGTLA FT RAPAVTEATPLKGLASNSTFSSRTSPVTTAGSLLERSSITM FT TPPASPKSNINMYSSSLPFKSIITSAAPLISSPLKSVVSPV FT KSAVDVISSAKITMASSLSSPVKQMPGHAEVALVNGSISPL FT KYPSSSTLINGCKATATLQEKISSATNSVSSVVSAATDTVE FT KVFSTTTAMPFSPLRSYVSAAPSAFQSLRTPSASALYTSLG FT SSISATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFT FT KSAAALLSPIKTLTTETHPQPHFSRTSSPVKSSL -> TSC FT TVKVRKSQLKEVCKHSIEYFKGISGETLKLVDRLSEEEKKM FT QSELSDEEESTSRNTSLSETSRGGQPSVTTKSARDKKTEAA FT PLKSKSEKAGSEKRSSRRTGPQSPCERTDIRMAIVADHLGL FT SWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTR FT DGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRS FT FADENNVFHDPVDGWQNETSSGNLESCAQARRVTGGLLDRL FT DDSPDQCRDSITSYLKGEAGKFEANGSHTEITPEAKTKSYF FT PESQNDVGKQSTKETLKPKIHGSGHVEEPASPLAAYQKSLE FT ETSKLSKLIIEETKPCVPVSMKKMSRTSPADGKPRLSLHEE FT EGSSGSEQKQGEGFKVKTKKEIRHVEKKSHS (in FT isoform 5). {ECO:0000303|PubMed:8666667}. FT /FTId=VSP_053758. FT VAR_SEQ 1881 4377 Missing (in isoform 5). FT {ECO:0000303|PubMed:8666667}. FT /FTId=VSP_053759. FT VAR_SEQ 4082 4082 G -> S (in isoform 2, isoform 3 and FT isoform 4). {ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005}. FT /FTId=VSP_044353. FT VAR_SEQ 4199 4199 G -> GYPSLQVELETPTGLHYTPPTPFQQDDYFSDISSIE FT SPLRTPSRLSDGLVPSQGNIEHSADGPPVVTAEDASLEDSK FT LEDSVPLTEMPEAVDVDESQLENVCLS (in isoform FT 2, isoform 3 and isoform 4). FT {ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005}. FT /FTId=VSP_044354. FT VARIANT 1569 1569 S -> A (found in a patient with autism; FT unknown pathological significance). FT {ECO:0000269|PubMed:22865819}. 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 (found in a patient with autism; FT unknown pathological significance). FT {ECO:0000269|PubMed:22865819}. FT /FTId=VAR_068703. FT VARIANT 4255 4255 T -> P (found in a patient with autism; FT unknown pathological significance). FT {ECO:0000269|PubMed:22865819}. 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. 5; CAI56716). FT {ECO:0000305}. FT CONFLICT 222 222 L -> P (in Ref. 5; CAD97900). FT {ECO:0000305}. FT CONFLICT 327 327 I -> V (in Ref. 5; CAD97900). FT {ECO:0000305}. FT CONFLICT 338 338 L -> W (in Ref. 4; BAG58523). FT {ECO:0000305}. FT CONFLICT 523 523 A -> T (in Ref. 5; CAD97900). FT {ECO:0000305}. FT CONFLICT 578 578 L -> P (in Ref. 5; CAI56716). FT {ECO:0000305}. FT CONFLICT 921 921 R -> G (in Ref. 3; CAB66645). FT {ECO:0000305}. FT CONFLICT 977 977 S -> P (in Ref. 3; CAB66645). FT {ECO:0000305}. FT CONFLICT 1237 1237 D -> G (in Ref. 5; CAI56716). FT {ECO:0000305}. FT CONFLICT 1418 1418 P -> R (in Ref. 1; AAA64834). FT {ECO:0000305}. FT CONFLICT 1455 1455 D -> E (in Ref. 4; BAG58523). FT {ECO:0000305}. FT CONFLICT 1574 1574 F -> L (in Ref. 1; AAA64834). FT {ECO:0000305}. FT CONFLICT 1685 1685 A -> R (in Ref. 1; AAA64834). FT {ECO:0000305}. FT CONFLICT 1726 1726 P -> A (in Ref. 1; AAA64834). FT {ECO:0000305}. FT CONFLICT 2062 2063 ER -> GG (in Ref. 1; AAA64834). FT {ECO:0000305}. FT CONFLICT 2146 2146 S -> T (in Ref. 1; AAA64834). FT {ECO:0000305}. FT CONFLICT 3919 3919 H -> P (in Ref. 1; AAA64834). FT {ECO:0000305}. FT CONFLICT 4137 4137 L -> F (in Ref. 3; CAB66645). FT {ECO:0000305}. FT HELIX 4089 4101 {ECO:0000244|PDB:4O6X}. FT HELIX 4102 4104 {ECO:0000244|PDB:4O6X}. FT HELIX 4105 4111 {ECO:0000244|PDB:4O6X}. FT HELIX 4116 4125 {ECO:0000244|PDB:4O6X}. FT HELIX 4130 4145 {ECO:0000244|PDB:4O6X}. FT HELIX 4146 4148 {ECO:0000244|PDB:4O6X}. FT HELIX 4151 4160 {ECO:0000244|PDB:4O6X}. FT HELIX 4164 4171 {ECO:0000244|PDB:4O6X}. FT HELIX 4173 4178 {ECO:0000244|PDB:4O6X}. 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 //