ANR17_HUMAN
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 03-AUG-2022, entry version 177.
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};
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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_001286771.2. [O75179-7]
DR RefSeq; NP_056389.1; NM_015574.1. [O75179-2]
DR RefSeq; NP_115593.3; NM_032217.4. [O75179-1]
DR RefSeq; NP_942592.1; NM_198889.2. [O75179-6]
DR AlphaFoldDB; O75179; -.
DR SMR; O75179; -.
DR BioGRID; 117519; 188.
DR DIP; DIP-47290N; -.
DR IntAct; O75179; 48.
DR MINT; O75179; -.
DR STRING; 9606.ENSP00000351416; -.
DR GlyGen; O75179; 18 sites, 2 O-linked glycans (18 sites).
DR iPTMnet; O75179; -.
DR MetOSite; O75179; -.
DR PhosphoSitePlus; O75179; -.
DR SwissPalm; O75179; -.
DR BioMuta; ANKRD17; -.
DR EPD; O75179; -.
DR jPOST; O75179; -.
DR MassIVE; O75179; -.
DR MaxQB; O75179; -.
DR PaxDb; O75179; -.
DR PeptideAtlas; O75179; -.
DR PRIDE; 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 Antibodypedia; 24452; 147 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 CTD; 26057; -.
DR DisGeNET; 26057; -.
DR GeneCards; ANKRD17; -.
DR HGNC; HGNC:23575; ANKRD17.
DR HPA; ENSG00000132466; Low tissue specificity.
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; GWLEMER; -.
DR OrthoDB; 1115202at2759; -.
DR PhylomeDB; O75179; -.
DR TreeFam; TF328552; -.
DR PathwayCommons; O75179; -.
DR SignaLink; O75179; -.
DR BioGRID-ORCS; 26057; 114 hits in 1087 CRISPR screens.
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 208 other tissues.
DR ExpressionAtlas; O75179; baseline and differential.
DR Genevisible; O75179; HS.
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: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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA: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 Gene3D; 1.25.40.20; -; 8.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 9.
DR Pfam; PF00013; KH_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 25.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR SUPFAM; SSF54791; SSF54791; 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; Reference proteome; Repeat; 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 81..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1944..1995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2011..2029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2051..2114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2156..2183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2273..2301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2381..2401
FT /note="Polar residues"
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)"
FT /evidence="ECO:0000269|PubMed:33909992"
FT /id="VAR_086095"
FT VARIANT 716
FT /note="L -> R (in CAGS)"
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)"
FT /evidence="ECO:0000269|PubMed:33909992"
FT /id="VAR_086100"
FT VARIANT 1186
FT /note="P -> R (in CAGS)"
FT /evidence="ECO:0000269|PubMed:33909992"
FT /id="VAR_086101"
FT VARIANT 1364
FT /note="G -> A (in CAGS)"
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)"
FT /evidence="ECO:0000269|PubMed:33909992"
FT /id="VAR_086104"
FT VARIANT 2434
FT /note="R -> G (in CAGS)"
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
