ID ANR17_HUMAN Reviewed; 2603 AA. AC O75179; E7EUV3; G5E964; Q6PJ85; Q6PK85; Q6PKA2; Q86XI3; Q8NDR5; Q96I86; AC Q9H288; Q9H6J9; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 3. DT 09-APR-2025, entry version 192. DE RecName: Full=Ankyrin repeat domain-containing protein 17; DE AltName: Full=Gene trap ankyrin repeat protein; DE AltName: Full=Serologically defined breast cancer antigen NY-BR-16; GN Name=ANKRD17; Synonyms=GTAR, KIAA0697; 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 3). RC TISSUE=Mammary gland; RX PubMed=12747765; RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.; RT "Humoral immunity to human breast cancer: antigen definition and RT quantitative analysis of mRNA expression."; RL Cancer Immun. 1:4-4(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 181-2603 (ISOFORM 4). RC TISSUE=Lymph, Muscle, Placenta, and Uterus; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-2603 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [6] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1487 (ISOFORM 1). RC TISSUE=Brain; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1035-1492 (ISOFORM 1). 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2059, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP FUNCTION, INTERACTION WITH ENTEROVIRUS 71 PROTEIN VP1 (MICROBIAL RP INFECTION), TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=17276651; DOI=10.1016/j.micpath.2006.12.002; RA Yeo W.M., Chow V.T.K.; RT "The VP1 structural protein of enterovirus 71 interacts with human RT ornithine decarboxylase and gene trap ankyrin repeat."; RL Microb. Pathog. 42:129-137(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803; SER-1700; SER-1709; RP SER-2045; SER-2047 AND SER-2401, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP TISSUE SPECIFICITY, INTERACTION WITH CDK2; MCM3; MCM5; MCM7; CDC6 AND PCNA, RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-2042; SER-2045 AND SER-2401 BY RP CDK2, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION. RX PubMed=19150984; DOI=10.1074/jbc.m807827200; RA Deng M., Li F., Ballif B.A., Li S., Chen X., Guo L., Ye X.; RT "Identification and functional analysis of a novel cyclin e/cdk2 substrate RT ankrd17."; RL J. Biol. Chem. 284:7875-7888(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-1709; SER-2047 AND RP SER-2401, AND 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). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1457; SER-1709; SER-2047 AND RP SER-2067, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] 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., Buerckstuemmer T., RA 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1635; SER-1696; SER-1709 AND RP SER-2047, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP INTERACTION WITH MAVS; IFIH1; DDX58, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=22328336; DOI=10.1002/eji.201142125; RA Wang Y., Tong X., Li G., Li J., Deng M., Ye X.; RT "Ankrd17 positively regulates RIG-I-like receptor (RLR)-mediated immune RT signaling."; RL Eur. J. Immunol. 42:1304-1315(2012). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP INTERACTION WITH NOD2, AND FUNCTION. RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037; RA Menning M., Kufer T.A.; RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and RT Nod2-mediated inflammatory responses."; RL FEBS Lett. 587:2137-2142(2013). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-1457; SER-1639; RP SER-1696; SER-1709; SER-2045; SER-2047; SER-2067; SER-2373 AND SER-2401, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2045; SER-2047 AND SER-2059, RP AND IDENTIFICATION BY MASS 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [25] RP INVOLVEMENT IN CAGS, AND VARIANTS CAGS VAL-278; THR-377; PRO-519; ARG-716; RP 833-GLN--GLY-2603 DEL; 906-CYS--GLY-2603 DEL; ARG-1120; ARG-1186; ALA-1364; RP 1468-LEU--GLY-2603 DEL; PRO-1880 AND GLY-2434. RX PubMed=33909992; DOI=10.1016/j.ajhg.2021.04.007; RA Chopra M., McEntagart M., Clayton-Smith J., Platzer K., Shukla A., RA Girisha K.M., Kaur A., Kaur P., Pfundt R., Veenstra-Knol H., RA Mancini G.M.S., Cappuccio G., Brunetti-Pierri N., Kortuem F., Hempel M., RA Denecke J., Lehman A., Kleefstra T., Stuurman K.E., Wilke M., RA Thompson M.L., Bebin E.M., Bijlsma E.K., Hoffer M.J.V., Peeters-Scholte C., RA Slavotinek A., Weiss W.A., Yip T., Hodoglugil U., Whittle A., diMonda J., RA Neira J., Yang S., Kirby A., Pinz H., Lechner R., Sleutels F., Helbig I., RA McKeown S., Helbig K., Willaert R., Juusola J., Semotok J., Hadonou M., RA Short J., Yachelevich N., Lala S., Fernandez-Jaen A., Pelayo J.P., RA Kloeckner C., Kamphausen S.B., Abou Jamra R., Arelin M., Innes A.M., RA Niskakoski A., Amin S., Williams M., Evans J., Smithson S., Smedley D., RA de Burca A., Kini U., Delatycki M.B., Gallacher L., Yeung A., Pais L., RA Field M., Martin E., Charles P., Courtin T., Keren B., Iascone M., RA Cereda A., Poke G., Abadie V., Chalouhi C., Parthasarathy P., RA Halliday B.J., Robertson S.P., Lyonnet S., Amiel J., Gordon C.T.; RT "Heterozygous ANKRD17 loss-of-function variants cause a syndrome with RT intellectual disability, speech delay, and dysmorphism."; RL Am. J. Hum. Genet. 108:1138-1150(2021). CC -!- FUNCTION: Could play pivotal roles in cell cycle and DNA regulation CC (PubMed:19150984). Involved in innate immune defense against viruse by CC positively regulating the viral dsRNA receptors DDX58 and IFIH1 CC signaling pathways (PubMed:22328336). Involves in NOD2- and NOD1- CC mediated responses to bacteria suggesting a role in innate CC antibacterial immune pathways too (PubMed:23711367). Target of CC enterovirus 71 which is the major etiological agent of HFMD (hand, foot CC and mouth disease) (PubMed:17276651). Could play a central role for the CC formation and/or maintenance of the blood vessels of the circulation CC system (By similarity). {ECO:0000250|UniProtKB:Q99NH0, CC ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984, CC ECO:0000269|PubMed:22328336, ECO:0000269|PubMed:23711367}. CC -!- SUBUNIT: Interacts (via N-terminus) with NOD2. Interacts with CDK2, CC MCM3, MCM5, MCM7, CDC6 and PCNA. Interacts with MAVS and IFIH1. CC Interacts (via the second ankyrin repeat cluster) with DDX58. CC {ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336, CC ECO:0000269|PubMed:23711367}. CC -!- SUBUNIT: (Microbial infection) Interacts with enterovirus 71/EV71 CC capsid protein VP1. {ECO:0000269|PubMed:17276651}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17276651, CC ECO:0000269|PubMed:22328336}. Nucleus {ECO:0000269|PubMed:17276651, CC ECO:0000269|PubMed:19150984, ECO:0000269|PubMed:22328336}. CC Note=Detected around the nucleolus. Localized on chromatin in a cell CC cycle-dependent manner. {ECO:0000269|PubMed:17276651, CC ECO:0000269|PubMed:19150984}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=O75179-1; Sequence=Displayed; CC Name=2; CC IsoId=O75179-2; Sequence=VSP_028863; CC Name=3; CC IsoId=O75179-3; Sequence=VSP_028864, VSP_028865; CC Name=4; CC IsoId=O75179-4; Sequence=VSP_028861, VSP_028862; CC Name=5; CC IsoId=O75179-5; Sequence=VSP_028859, VSP_028860; CC Name=6; CC IsoId=O75179-6; Sequence=VSP_047048; CC Name=7; CC IsoId=O75179-7; Sequence=VSP_054757; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:17276651, ECO:0000269|PubMed:19150984}. CC -!- PTM: Phosphorylated by CDK2. {ECO:0000269|PubMed:19150984}. CC -!- DISEASE: Chopra-Amiel-Gordon syndrome (CAGS) [MIM:619504]: An autosomal CC dominant disorder characterized by developmental delay, intellectual CC disability, speech delay, and dysmorphic facial features. Additional CC features include growth failure, feeding difficulties, non-specific CC brain abnormalities, ophthalmological abnormalities, gait and balance CC disturbance, joint hypermobility, and predisposition to recurrent CC infections. {ECO:0000269|PubMed:33909992}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAG48253.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAH04173.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAB15260.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15260.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; 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; AF308285; AAG48253.1; ALT_FRAME; mRNA. DR EMBL; AC053527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC095053; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105757; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX05655.1; -; Genomic_DNA. DR EMBL; BC004173; AAH04173.1; ALT_SEQ; mRNA. DR EMBL; BC007747; AAH07747.2; -; mRNA. DR EMBL; BC019963; AAH19963.1; -; mRNA. DR EMBL; BC043394; AAH43394.1; -; mRNA. DR EMBL; AB014597; BAA31672.2; -; mRNA. DR EMBL; AL831903; CAD38571.2; -; mRNA. DR EMBL; AK025859; BAB15260.1; ALT_SEQ; mRNA. DR CCDS; CCDS34003.1; -. [O75179-6] DR CCDS; CCDS34004.1; -. [O75179-1] DR CCDS; CCDS68721.1; -. [O75179-7] DR PIR; T00353; T00353. DR RefSeq; NP_001273700.1; NM_001286771.3. [O75179-7] DR RefSeq; NP_056389.1; NM_015574.2. [O75179-2] DR RefSeq; NP_115593.3; NM_032217.4. [O75179-1] DR RefSeq; NP_942592.1; NM_198889.3. [O75179-6] DR AlphaFoldDB; O75179; -. DR SMR; O75179; -. DR BioGRID; 117519; 234. DR DIP; DIP-47290N; -. DR IntAct; O75179; 112. DR MINT; O75179; -. DR STRING; 9606.ENSP00000351416; -. DR GlyCosmos; O75179; 18 sites, 2 glycans. DR GlyGen; O75179; 51 sites, 3 N-linked glycans (5 sites), 2 O-linked glycans (46 sites). DR iPTMnet; O75179; -. DR MetOSite; O75179; -. DR PhosphoSitePlus; O75179; -. DR SwissPalm; O75179; -. DR BioMuta; ANKRD17; -. DR jPOST; O75179; -. DR MassIVE; O75179; -. DR PaxDb; 9606-ENSP00000351416; -. DR PeptideAtlas; O75179; -. DR ProteomicsDB; 18505; -. DR ProteomicsDB; 33844; -. DR ProteomicsDB; 49850; -. [O75179-1] DR ProteomicsDB; 49851; -. [O75179-2] DR ProteomicsDB; 49852; -. [O75179-3] DR ProteomicsDB; 49853; -. [O75179-4] DR ProteomicsDB; 49854; -. [O75179-5] DR Pumba; O75179; -. DR Antibodypedia; 24452; 159 antibodies from 18 providers. DR DNASU; 26057; -. DR Ensembl; ENST00000330838.10; ENSP00000332265.6; ENSG00000132466.20. [O75179-6] DR Ensembl; ENST00000358602.9; ENSP00000351416.4; ENSG00000132466.20. [O75179-1] DR Ensembl; ENST00000509867.6; ENSP00000427151.2; ENSG00000132466.20. [O75179-7] DR GeneID; 26057; -. DR KEGG; hsa:26057; -. DR MANE-Select; ENST00000358602.9; ENSP00000351416.4; NM_032217.5; NP_115593.3. DR UCSC; uc003hgo.5; human. [O75179-1] DR AGR; HGNC:23575; -. DR CTD; 26057; -. DR DisGeNET; 26057; -. DR GeneCards; ANKRD17; -. DR GeneReviews; ANKRD17; -. DR HGNC; HGNC:23575; ANKRD17. DR HPA; ENSG00000132466; Low tissue specificity. DR MalaCards; ANKRD17; -. DR MIM; 615929; gene. DR MIM; 619504; phenotype. DR neXtProt; NX_O75179; -. DR OpenTargets; ENSG00000132466; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA134943225; -. DR VEuPathDB; HostDB:ENSG00000132466; -. DR eggNOG; KOG0504; Eukaryota. DR eggNOG; KOG4369; Eukaryota. DR GeneTree; ENSGT00940000153768; -. DR HOGENOM; CLU_000590_0_1_1; -. DR InParanoid; O75179; -. DR OMA; NDNGHCA; -. DR OrthoDB; 9534190at2759; -. DR PhylomeDB; O75179; -. DR TreeFam; TF328552; -. DR PathwayCommons; O75179; -. DR SignaLink; O75179; -. DR BioGRID-ORCS; 26057; 132 hits in 1170 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; ANKRD17; human. DR GeneWiki; ANKRD17; -. DR GenomeRNAi; 26057; -. DR Pharos; O75179; Tbio. DR PRO; PR:O75179; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O75179; protein. DR Bgee; ENSG00000132466; Expressed in secondary oocyte and 210 other cell types or tissues. DR ExpressionAtlas; O75179; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0001955; P:blood vessel maturation; IEA:Ensembl. DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; IDA:UniProtKB. DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IDA:UniProtKB. DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB. DR CDD; cd22502; KH-I_ANKRD17; 1. DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1. DR FunFam; 1.25.40.20:FF:000046; Ankyrin repeat and KH domain-containing protein 1; 1. DR FunFam; 1.25.40.20:FF:000114; ankyrin repeat and KH domain-containing protein 1 isoform X2; 1. DR FunFam; 1.25.40.20:FF:000062; ankyrin repeat domain-containing protein 17; 1. DR FunFam; 1.25.40.20:FF:000012; ankyrin repeat domain-containing protein 17 isoform X1; 1. DR FunFam; 3.30.1370.10:FF:000031; ankyrin repeat domain-containing protein 17 isoform X1; 1. DR FunFam; 1.25.40.20:FF:000014; ankyrin repeat domain-containing protein 17 isoform X2; 1. DR FunFam; 1.25.40.20:FF:000055; ankyrin repeat domain-containing protein 17 isoform X2; 1. DR FunFam; 1.25.40.20:FF:000161; ankyrin repeat domain-containing protein 17 isoform X3; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 8. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1. DR InterPro; IPR051631; Ankyrin-KH/SAM_domain. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR047375; KH-I_ANKRD17. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR PANTHER; PTHR23206:SF1; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 17; 1. DR PANTHER; PTHR23206; MASK PROTEIN; 1. DR Pfam; PF00023; Ank; 3. DR Pfam; PF12796; Ank_2; 8. DR Pfam; PF00013; KH_1; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 25. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 3. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 20. DR PROSITE; PS50084; KH_TYPE_1; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ANK repeat; Coiled coil; Cytoplasm; KW Disease variant; Host-virus interaction; Immunity; Innate immunity; KW Intellectual disability; Isopeptide bond; Methylation; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat; KW RNA-binding; Ubl conjugation. FT CHAIN 1..2603 FT /note="Ankyrin repeat domain-containing protein 17" FT /id="PRO_0000307917" FT REPEAT 233..262 FT /note="ANK 1" FT REPEAT 266..295 FT /note="ANK 2" FT REPEAT 300..329 FT /note="ANK 3" FT REPEAT 333..362 FT /note="ANK 4" FT REPEAT 366..395 FT /note="ANK 5" FT REPEAT 400..429 FT /note="ANK 6" FT REPEAT 433..462 FT /note="ANK 7" FT REPEAT 466..495 FT /note="ANK 8" FT REPEAT 499..528 FT /note="ANK 9" FT REPEAT 533..562 FT /note="ANK 10" FT REPEAT 563..592 FT /note="ANK 11" FT REPEAT 596..625 FT /note="ANK 12" FT REPEAT 629..658 FT /note="ANK 13" FT REPEAT 663..692 FT /note="ANK 14" FT REPEAT 696..725 FT /note="ANK 15" FT REPEAT 1082..1111 FT /note="ANK 16" FT REPEAT 1115..1144 FT /note="ANK 17" FT REPEAT 1149..1178 FT /note="ANK 18" FT REPEAT 1182..1211 FT /note="ANK 19" FT REPEAT 1217..1246 FT /note="ANK 20" FT REPEAT 1251..1280 FT /note="ANK 21" FT REPEAT 1284..1313 FT /note="ANK 22" FT REPEAT 1319..1348 FT /note="ANK 23" FT REPEAT 1352..1381 FT /note="ANK 24" FT REPEAT 1385..1414 FT /note="ANK 25" FT DOMAIN 1725..1789 FT /note="KH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REGION 1..143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1479..1500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1517..1717 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1906..1995 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2011..2192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2273..2332 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2381..2423 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1442..1526 FT /evidence="ECO:0000255" FT COMPBIAS 1..34 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 42..53 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 63..79 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 84..94 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..111 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 116..131 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1481..1491 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1531..1550 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1602..1611 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1620..1632 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1642..1652 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1675..1703 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1950..1995 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2011..2028 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2066..2078 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2095..2106 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2107..2127 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2273..2303 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2308..2318 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2382..2411 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99NH0" FT MOD_RES 156 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 803 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1457 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1635 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1639 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1696 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1700 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1709 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1874 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q99NH0" FT MOD_RES 2042 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19150984" FT MOD_RES 2044 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99NH0" FT MOD_RES 2045 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19150984, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2047 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2059 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2067 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2373 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2401 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT CROSSLNK 318 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..130 FT /note="MEKATVPVAAATAAEGEGSPPAVAAVAGPPAAAEVGGGVGGSSRARSASSPR FT GMVRVCDLLLKKKPPQQQHHKAKRNRTCRPPSSSESSSDSDNSGGGGGGGGGGGGGGGT FT SSNNSEEEEDDDDEEEEVS -> MVETAAEMEAYVLEDIL (in isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_054757" FT VAR_SEQ 742..751 FT /note="NRAPRVPVQA -> TDNIFPRLVC (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_028859" FT VAR_SEQ 752..2603 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_028860" FT VAR_SEQ 778..1028 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_047048" FT VAR_SEQ 982..1010 FT /note="GVIVGQPVLGQAQLAGLGQGILTETQQGL -> VLSSLLQPCFLSTLPLILM FT HRLRVIMTRR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_028861" FT VAR_SEQ 1011..1603 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_028862" FT VAR_SEQ 1028 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9734811" FT /id="VSP_028863" FT VAR_SEQ 1176..1187 FT /note="KEHRNVSDYTPL -> YRSTGMVLITHL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12747765" FT /id="VSP_028864" FT VAR_SEQ 1188..2603 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12747765" FT /id="VSP_028865" FT VARIANT 278 FT /note="G -> V (in CAGS; dbSNP:rs963581326)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086093" FT VARIANT 377 FT /note="A -> T (in CAGS)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086094" FT VARIANT 519 FT /note="L -> P (in CAGS; dbSNP:rs2148854716)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086095" FT VARIANT 716 FT /note="L -> R (in CAGS; dbSNP:rs2148821952)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086096" FT VARIANT 833..2603 FT /note="Missing (in CAGS; dbSNP:rs554386947)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086097" FT VARIANT 906..2603 FT /note="Missing (in CAGS)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086099" FT VARIANT 1120 FT /note="L -> R (in CAGS; dbSNP:rs2148719956)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086100" FT VARIANT 1186 FT /note="P -> R (in CAGS; dbSNP:rs2148701869)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086101" FT VARIANT 1364 FT /note="G -> A (in CAGS; dbSNP:rs2148684587)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086102" FT VARIANT 1468..2603 FT /note="Missing (in CAGS)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086103" FT VARIANT 1880 FT /note="S -> P (in CAGS; dbSNP:rs2110165980)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086104" FT VARIANT 2434 FT /note="R -> G (in CAGS; dbSNP:rs143161842)" FT /evidence="ECO:0000269|PubMed:33909992" FT /id="VAR_086105" FT VARIANT 2560 FT /note="H -> Y (in dbSNP:rs2306059)" FT /id="VAR_036711" FT CONFLICT 304 FT /note="P -> S (in Ref. 5; BAA31672)" FT /evidence="ECO:0000305" FT CONFLICT 705 FT /note="A -> P (in Ref. 1; AAG48253)" FT /evidence="ECO:0000305" FT CONFLICT 713 FT /note="V -> G (in Ref. 1; AAG48253)" FT /evidence="ECO:0000305" FT CONFLICT 1137 FT /note="D -> G (in Ref. 8; BAB15260)" FT /evidence="ECO:0000305" FT CONFLICT 1163 FT /note="Q -> P (in Ref. 1; AAG48253)" FT /evidence="ECO:0000305" FT CONFLICT 1391 FT /note="Missing (in Ref. 7; CAD38571)" FT /evidence="ECO:0000305" SQ SEQUENCE 2603 AA; 274258 MW; BD2BF51889283483 CRC64; MEKATVPVAA ATAAEGEGSP PAVAAVAGPP AAAEVGGGVG GSSRARSASS PRGMVRVCDL LLKKKPPQQQ HHKAKRNRTC RPPSSSESSS DSDNSGGGGG GGGGGGGGGG TSSNNSEEEE DDDDEEEEVS EVESFILDQD DLENPMLETA SKLLLSGTAD GADLRTVDPE TQARLEALLE AAGIGKLSTA DGKAFADPEV LRRLTSSVSC ALDEAAAALT RMRAESTANA GQSDNRSLAE ACSEGDVNAV RKLLIEGRSV NEHTEEGESL LCLACSAGYY ELAQVLLAMH ANVEDRGIKG DITPLMAAAN GGHVKIVKLL LAHKADVNAQ SSTGNTALTY ACAGGYVDVV KVLLESGASI EDHNENGHTP LMEAGSAGHV EVARLLLENG AGINTHSNEF KESALTLACY KGHLEMVRFL LEAGADQEHK TDEMHTALME ACMDGHVEVA RLLLDSGAQV NMPADSFESP LTLAACGGHV ELAALLIERG ASLEEVNDEG YTPLMEAARE GHEEMVALLL GQGANINAQT EETQETALTL ACCGGFLEVA DFLIKAGADI ELGCSTPLME AAQEGHLELV KYLLAAGANV HATTATGDTA LTYACENGHT DVADVLLQAG ADLEHESEGG RTPLMKAARA GHVCTVQFLI SKGANVNRTT ANNDHTVLSL ACAGGHLAVV ELLLAHGADP THRLKDGSTM LIEAAKGGHT SVVCYLLDYP NNLLSAPPPD VTQLTPPSHD LNRAPRVPVQ ALPMVVPPQE PDKPPANVAT TLPIRNKAAS KQKSSSHLPA NSQDVQGYIT NQSPESIVEE AQGKLTELEQ RIKEAIEKNA QLQSLELAHA DQLTKEKIEE LNKTREEQIQ KKQKILEELQ KVERELQLKT QQQLKKQYLE VKAQRIQLQQ QQQQSCQHLG LLTPVGVGEQ LSEGDYARLQ QVDPVLLKDE PQQTAAQMGF APIQPLAMPQ ALPLAAGPLP PGSIANLTEL QGVIVGQPVL GQAQLAGLGQ GILTETQQGL MVASPAQTLN DTLDDIMAAV SGRASAMSNT PTHSIAASIS QPQTPTPSPI ISPSAMLPIY PAIDIDAQTE SNHDTALTLA CAGGHEELVQ TLLERGASIE HRDKKGFTPL ILAATAGHVG VVEILLDNGA DIEAQSERTK DTPLSLACSG GRQEVVELLL ARGANKEHRN VSDYTPLSLA ASGGYVNIIK ILLNAGAEIN SRTGSKLGIS PLMLAAMNGH TAAVKLLLDM GSDINAQIET NRNTALTLAC FQGRTEVVSL LLDRKANVEH RAKTGLTPLM EAASGGYAEV GRVLLDKGAD VNAPPVPSSR DTALTIAADK GHYKFCELLI GRGAHIDVRN KKGNTPLWLA ANGGHLDVVQ LLVQAGADVD AADNRKITPL MAAFRKGHVK VVRYLVKEVN QFPSDSECMR YIATITDKEM LKKCHLCMES IVQAKDRQAA EANKNASILL EELDLEKLRE ESRRLALAAK REKRKEKRRK KKEEQRRKLE EIEAKNKENF ELQAAQEKEK LKVEDEPEVL TEPPSATTTT TIGISATWTT LAGSHGKRNN TITTTSSKRK NRKNKITPEN VQIIFDDPLP ISYSQPEKVN GESKSSSTSE SGDSDNMRIS SCSDESSNSN SSRKSDNHSP AVVTTTVSSK KQPSVLVTFP KEERKSVSGK ASIKLSETIS EGTSNSLSTC TKSGPSPLSS PNGKLTVASP KRGQKREEGW KEVVRRSKKV SVPSTVISRV IGRGGCNINA IREFTGAHID IDKQKDKTGD RIITIRGGTE STRQATQLIN ALIKDPDKEI DELIPKNRLK SSSANSKIGS SAPTTTAANT SLMGIKMTTV ALSSTSQTAT ALTVPAISSA STHKTIKNPV NNVRPGFPVS LPLAYPPPQF AHALLAAQTF QQIRPPRLPM THFGGTFPPA QSTWGPFPVR PLSPARATNS PKPHMVPRHS NQNSSGSQVN SAGSLTSSPT TTTSSSASTV PGTSTNGSPS SPSVRRQLFV TVVKTSNATT TTVTTTASNN NTAPTNATYP MPTAKEHYPV SSPSSPSPPA QPGGVSRNSP LDCGSASPNK VASSSEQEAG SPPVVETTNT RPPNSSSSSG SSSAHSNQQQ PPGSVSQEPR PPLQQSQVPP PEVRMTVPPL ATSSAPVAVP STAPVTYPMP QTPMGCPQPT PKMETPAIRP PPHGTTAPHK NSASVQNSSV AVLSVNHIKR PHSVPSSVQL PSTLSTQSAC QNSVHPANKP IAPNFSAPLP FGPFSTLFEN SPTSAHAFWG GSVVSSQSTP ESMLSGKSSY LPNSDPLHQS DTSKAPGFRP PLQRPAPSPS GIVNMDSPYG SVTPSSTHLG NFASNISGGQ MYGPGAPLGG APAAANFNRQ HFSPLSLLTP CSSASNDSSA QSVSSGVRAP SPAPSSVPLG SEKPSNVSQD RKVPVPIGTE RSARIRQTGT SAPSVIGSNL STSVGHSGIW SFEGIGGNQD KVDWCNPGMG NPMIHRPMSD PGVFSQHQAM ERDSTGIVTP SGTFHQHVPA GYMDFPKVGG MPFSVYGNAM IPPVAPIPDG AGGPIFNGPH AADPSWNSLI KMVSSSTENN GPQTVWTGPW APHMNSVHMN QLG //