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ANKHM_DROME
ID   ANKHM_DROME             Reviewed;        4001 AA.
AC   Q9VCA8; Q6NP19; Q8SX96; Q8T0H2; Q8T8Q4; Q8WRQ7;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Ankyrin repeat and KH domain-containing protein mask;
DE   AltName: Full=Multiple ankyrin repeat single KH domain-containing protein;
GN   Name=mask {ECO:0000312|EMBL:AAO41600.1, ECO:0000312|FlyBase:FBgn0043884};
GN   ORFNames=CG33106;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAL65911.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=11782402; DOI=10.1242/dev.129.1.71;
RA   Smith R.K., Carroll P.M., Allard J.D., Simon M.A.;
RT   "MASK, a large ankyrin repeat and KH domain-containing protein involved in
RT   Drosophila receptor tyrosine kinase signaling.";
RL   Development 129:71-82(2002).
RN   [2] {ECO:0000312|EMBL:AAO41600.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAO41600.1}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAR82779.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-4001.
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAR82779.1}; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAM11086.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2024-2883 AND 3301-4001.
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM11086.1};
RC   TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
RC   Head {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6] {ECO:0000305}
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501 AND SER-1389, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501; SER-1588; SER-2687;
RP   THR-2698; SER-2747; SER-2753; SER-3596; SER-3820; SER-3822 AND SER-3825,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [8]
RP   FUNCTION, INTERACTION WITH UNC-89, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=26251439; DOI=10.1242/jcs.170639;
RA   Katzemich A., West R.J., Fukuzawa A., Sweeney S.T., Gautel M., Sparrow J.,
RA   Bullard B.;
RT   "Binding partners of the kinase domains in Drosophila obscurin and their
RT   effect on the structure of the flight muscle.";
RL   J. Cell Sci. 128:3386-3397(2015).
CC   -!- FUNCTION: Mediator of receptor tyrosine kinase (RTK) signaling, and may
CC       act either downstream of MAPK or transduce signaling through a parallel
CC       branch of the RTK pathway (PubMed:11782402). Required for the
CC       development and organization of indirect flight muscle sarcomeres by
CC       regulating the formation of M line and H zone and the correct assembly
CC       of thick and thin filaments in the sarcomere (PubMed:26251439).
CC       {ECO:0000269|PubMed:11782402, ECO:0000269|PubMed:26251439}.
CC   -!- SUBUNIT: May interact with Unc-89 (via protein kinase domain 1 or 2).
CC       {ECO:0000269|PubMed:26251439}.
CC   -!- INTERACTION:
CC       Q9VCA8; P14130: RpS14b; NbExp=2; IntAct=EBI-89853, EBI-114906;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11782402}.
CC       Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:26251439}.
CC       Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:26251439}.
CC       Note=In indirect flight muscle, more strongly associated with Z lines
CC       where it colocalizes with sls isoform A (kettin).
CC       {ECO:0000269|PubMed:26251439}.
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in eye imaginal disk,
CC       slightly higher expression is seen in presumptive photoreceptors
CC       (PubMed:11782402). Expressed in indirect flight muscle (IFM) (at
CC       protein level) (PubMed:26251439). {ECO:0000269|PubMed:11782402,
CC       ECO:0000269|PubMed:26251439}.
CC   -!- DISRUPTION PHENOTYPE: Flies exhibit compromised photoreceptor
CC       differentiation, cell survival and proliferation (PubMed:11782402).
CC       RNAi-mediated knockdown in muscles causes severe lethality at the early
CC       pupal stage and the few surviving animals cannot fly (PubMed:26251439).
CC       Severe defects in the indirect flight muscle structure characterized by
CC       narrower myofibrils and abnormal positioning of sarcomere Z line, M
CC       line and H line (PubMed:26251439). Although the spacing between Z line
CC       and M lines stays regular, M lines are not straight and sarcomere
CC       length is shorter. In the more affected myofibrils, the sarcomere
CC       structure is lost (PubMed:26251439). Localization of unc-89/obscurin to
CC       M lines and localization of kettin (sls isoform A) to Z line is not
CC       affected (PubMed:26251439). {ECO:0000269|PubMed:11782402,
CC       ECO:0000269|PubMed:26251439}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL39468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAL39468.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAL68383.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAM11086.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF425651; AAL65911.1; -; mRNA.
DR   EMBL; AE014297; AAO41600.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAO41601.1; -; Genomic_DNA.
DR   EMBL; BT011112; AAR82779.1; -; mRNA.
DR   EMBL; AY069323; AAL39468.1; ALT_SEQ; mRNA.
DR   EMBL; AY075578; AAL68383.1; ALT_INIT; mRNA.
DR   EMBL; AY094733; AAM11086.1; ALT_INIT; mRNA.
DR   RefSeq; NP_788733.1; NM_176556.2.
DR   RefSeq; NP_788734.1; NM_176557.2.
DR   SMR; Q9VCA8; -.
DR   BioGRID; 72524; 33.
DR   DIP; DIP-22630N; -.
DR   IntAct; Q9VCA8; 15.
DR   MINT; Q9VCA8; -.
DR   STRING; 7227.FBpp0293580; -.
DR   iPTMnet; Q9VCA8; -.
DR   PaxDb; Q9VCA8; -.
DR   PRIDE; Q9VCA8; -.
DR   ABCD; Q9VCA8; 4 sequenced antibodies.
DR   EnsemblMetazoa; FBtr0084562; FBpp0083947; FBgn0043884.
DR   EnsemblMetazoa; FBtr0084563; FBpp0083948; FBgn0043884.
DR   GeneID; 50070; -.
DR   KEGG; dme:Dmel_CG33106; -.
DR   CTD; 50070; -.
DR   FlyBase; FBgn0043884; mask.
DR   VEuPathDB; VectorBase:FBgn0043884; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG4369; Eukaryota.
DR   GeneTree; ENSGT00940000174194; -.
DR   InParanoid; Q9VCA8; -.
DR   SignaLink; Q9VCA8; -.
DR   BioGRID-ORCS; 50070; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; mask; fly.
DR   GenomeRNAi; 50070; -.
DR   PRO; PR:Q9VCA8; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0043884; Expressed in cleaving embryo and 37 other tissues.
DR   ExpressionAtlas; Q9VCA8; baseline and differential.
DR   Genevisible; Q9VCA8; DM.
DR   GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0031430; C:M band; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:FlyBase.
DR   GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR   GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR   GO; GO:0060361; P:flight; IMP:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR   GO; GO:1903147; P:negative regulation of autophagy of mitochondrion; IMP:FlyBase.
DR   GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; IMP:FlyBase.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IGI:FlyBase.
DR   GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IGI:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:FlyBase.
DR   GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IGI:FlyBase.
DR   Gene3D; 1.25.40.20; -; 7.
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; 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; SSF48403; 3.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Cytoplasm; Developmental protein; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..4001
FT                   /note="Ankyrin repeat and KH domain-containing protein
FT                   mask"
FT                   /id="PRO_0000312681"
FT   REPEAT          546..575
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          584..614
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          618..647
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          651..680
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          684..713
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          718..747
FT                   /note="ANK 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          751..780
FT                   /note="ANK 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          784..813
FT                   /note="ANK 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          817..846
FT                   /note="ANK 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          851..880
FT                   /note="ANK 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          881..910
FT                   /note="ANK 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          914..943
FT                   /note="ANK 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          947..976
FT                   /note="ANK 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          981..1011
FT                   /note="ANK 14"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1014..1043
FT                   /note="ANK 15"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2312..2341
FT                   /note="ANK 16"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2345..2374
FT                   /note="ANK 17"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2379..2408
FT                   /note="ANK 18"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2412..2441
FT                   /note="ANK 19"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2447..2476
FT                   /note="ANK 20"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2481..2510
FT                   /note="ANK 21"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2514..2543
FT                   /note="ANK 22"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2549..2578
FT                   /note="ANK 23"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2582..2611
FT                   /note="ANK 24"
FT                   /evidence="ECO:0000255"
FT   REPEAT          2615..2644
FT                   /note="ANK 25"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3036..3100
FT                   /note="KH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1046..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1583..1612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1646..1669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1682..1779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1852..1872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2084..2108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2225..2256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2699..3033
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3156..3329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3383..3457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3520..3636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3744..3786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3876..3945
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2674..2732
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..488
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1331..1345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1592..1607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1647..1661
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1685..1706
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1714..1757
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1759..1779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2708..2722
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2738..2765
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2775..2814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2824..2838
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2868..2903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2909..2962
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2975..3033
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3156..3279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3395..3416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3428..3457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3536..3584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3603..3621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3894..3930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656,
FT                   ECO:0000269|PubMed:18327897"
FT   MOD_RES         1389
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   MOD_RES         1588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2687
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2698
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2747
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2753
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3596
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3822
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        2886
FT                   /note="N -> T (in Ref. 1; AAL65911)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3307
FT                   /note="A -> G (in Ref. 5; AAL68383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3401
FT                   /note="V -> A (in Ref. 5; AAL68383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3408
FT                   /note="Q -> H (in Ref. 4; AAR82779)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3415
FT                   /note="L -> Q (in Ref. 4; AAR82779)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3430..3431
FT                   /note="PL -> QPHQQQ (in Ref. 5; AAL68383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3474
FT                   /note="S -> N (in Ref. 5; AAL68383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3578
FT                   /note="A -> V (in Ref. 5; AAL68383)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   4001 AA;  423201 MW;  22335427E9C8D447 CRC64;
     MNNDAKNHES DDLNVRSTAY FNQQTTTNQP KAPATSKNNT GSGSGSNNNN NNTNQNPNRQ
     LNHNLPRIAA ARQSIAAALL KNSGRKILTA KNEPLTTTES SGVLTNTPLP SNSRLKVNNN
     NNTNNTAKMS GTSSSQSSAT PTPPTASSST TTTTTTNIST GGGGSGSSGG GGGSTTVIAN
     PASVTNTGAG SAAKFRAAVA SAPSPALPAT NAPANATAAA AIAAIATAPA PSSSSSSSSS
     SKKTRAAVAA LKRQVALQQQ QPVTGNAPNM TSKDSAHLKF ATTTLLMGAA AAAADSNAGA
     ALGGSGAGGS GSSSSVGAVG GARMALNPAV DMANAAVLLK QKLKDAAAAA SASASNRSAT
     SSMSSTASSL SSSAGIVNAI SSALQNIITP DTDTDTEFYP QPVTTDLSES EEESVSEDDI
     PESDPDSCPH EGEVREDEDE TEEESEDSDE SEGEEEEEDE EEIDVLQDND ADDEEIDDED
     EEEDAPEVSS FLLDANNKRS SNISALLEAA ANEKAPVLRH ATHAIDETKQ ALTKMRCASS
     PRDKNSGFSR SLVAACTDND VNTVKRLLCK GNVNLNDAAA STDDGESLLS MACSAGYYEL
     AQVLLAMSAA QVEDKGQKDS TPLMEAASAG HLDIVKLLLN HNADVNAHCA TGNTPLMFAC
     AGGQVDVVKV LLKHGANVEE QNENGHTPLM EAASAGHVEV AKVLLEHGAG INTHSNEFKE
     SALTLACYKG HLDMVRFLLQ AGADQEHKTD EMHTALMEAS MDGHVEVARL LLDSGAQVNM
     PTDSFESPLT LAACGGHVEL ATLLIERGAN IEEVNDEGYT PLMEAAREGH EEMVALLLSK
     GANINATTEE TQETALTLAC CGGFMEVAAF LIKEGANLEL GASTPLMEAS QEGHTDLVSF
     LLKKKANVHA ETQTGDTALT HACENGHTDA AGVLLSYGAE LEHESEGGRT PLMKACRAGH
     LCTVKFLIQK GANVNKQTTS NDHTALSLAC AGGHQSVVEL LLKNNADPFH KLKDNSTMLI
     EASKGGHTRV VELLFRYPNI SPTENAASAN VTQAAPTSNQ PGPNQMRQKI MKQQLQHQLQ
     QLNAPPGLHE LSEAARASNQ QHFHQQQFSS AGNGSSNIVA MGTGDFLDAG ELQLTATAGM
     SAGAGTSTTG SETGMEEYGE VGGIDLTTLG AQQQEGLIAK SRLFHLQQQQ QQQQQQQQQQ
     QQQQQQQQQQ QQQQQQPPAA GQHQLVPCKH FDLDMEHINS LQPPQKAPPA PPVLFHTVCQ
     QPVMQQQQQQ LQPGQLKLKA MLPNRNRALK TAEVVEFIDC PVDQQQPGEQ VRTQPLGEDG
     KTPQFACAGE DPRLQRRRGF MPELKKGELP PESSSSDPNE LALKGADNNQ PVPTALDNSA
     CAQIPARNSG GAITHSSEVL QSTAISDRPK VKATNKNNRK QAAAAAAAAA AAAAAAAAAA
     QHAQQVLPNP MVSIYNNLHL QHLQHPHLQF QQQLQLHHQR VAGLDNAAAA AAAAASSANM
     AYSISPASPL PSPTGSGNYV DQQLQQQSMD VALQRKTAMD DFRGMLETAV NGPRGRKDLA
     LNTPQLNFFK DGWHMVGVHN FFGDQPKSPT ETPPEMEETT MSSPTEADRL GSEPRAEMKN
     LATLCSAAAA AAAVAAVNKD QVEISSDLES ECEDDAEGGA GADCEENTLP PEPIELAAAL
     REDGIIVEEE EDDEEEDDDD EEQDTNSGEV DKLNYDDEDA EVDNDGEVDY IDEDEGGGEG
     EEEEDDADDD EFFLDEPDSD QGTGNNNNNS KSGASSLPLK QRKMATRLEN LILNSQTVCD
     FPPELSNSEL VHVLPQISNL KAAANSNAAL NSVLQQQLAA ASAAAAHAKA SVVHQKQQHG
     EGDQQCEDDG SASASELYSG LEHFANDGEM EDIFQELASS LNYPELAEFS LNQMCKGRFA
     GNWAQSSGKW TGQEQLVGVV RSPGLINPGD VPQDAQRQAN LVLLDYPMQQ NIQLEQRLLD
     AEEMHLQQHQ QTPLSLLPFT DEQQQQLHHQ ALSNASDFQQ HQQLALENDP ELKQQLQQNS
     NARIIKAVAA QHQQQPPTNF VYNVESGDKN APPVQLLFQL PPHMAQHQAQ QQQGVGEPLT
     EQQQQQLHAE QAHLFQHRTG GQRPPTQSEL EQVAQELLLQ RSGQVPAGAP VVGVQAIPLK
     QKHFNLHPPP CPPTCVQHQV ATQTHPASVV VPQPAVGYTQ FALQASQQQQ MQQNELSIWP
     MATPTPAPSS GVSSTKSMPG GIAKKAIDKQ SRKERRCVVR QTPAGIQENT KLHLQPQVAT
     AQQQFLVQNQ LAVATTVSLD KTIEIDSETE SNHDTALTLA CAGGHEELVE LLINRGANIE
     HRDKKGFTPL ILAATAGHDK VVDILLKHSA ELEAQSERTK DTPLSLACSG GRYEVVELLL
     SVGANKEHRN VSDYTPLSLA ASGGYVNIIK LLLSHGAEIN SRTGSKLGIS PLMLAAMNGH
     TPAVKLLLDQ GSDINAQIET NRNTALTLAC FQGRHEVVSL LLDRRANVEH RAKTGLTPLM
     EAASGGYIEV GRVLLDKGAD VNAAPVPTSR DTALTIAADK GHQKFVELLL SRNASVEVKN
     KKGNSPLWLA AHGGHLSVVE LLYDHNADID SQDNRRVSCL MAAFRKGHTK IVKWMVQYVS
     QFPSDQEMIR FIGTISDKEL IDKCFDCMKI LRSAKEAQAV KANKNASILL EELDLERTRE
     ESRKAAAARR RERKKKKKME KKEEKRRQQQ GNGPGGDDMQ GDDDDASDKD DDSDKDDEDE
     EAAPAAAREE GDSGIDQGSC SSGDTKGARF GGSQSAQAAE AAANSVSTNS QGKKNKKQAK
     NKVLISVEPT QPVITSNSVL KGVCAKKHPA VEVVKQPPAT QQAAPLKRQL DVKKEEPALK
     KKEEKNSSSS SSSKREKENL APKEVALPAK QQPSSSSKLQ SSESASNINS STATNTSSAN
     TTRKEVAKPA SQTASATTLN PAKRTEVDGW KEVVRKSSAQ QTTAVGASGA PLPVTATSSA
     TSVQHHPHHH LANSSSNSSS SLTTSTTTAA SSVPEMTCKK VQVPVNAISR VIGRGGSNIN
     AIRATTGAHI EVEKQGKNQS ERCITIKGLT DATKQAHMLI LALIKDPDVD ILQMLPRINS
     SIKQASSGGA STPMSVGTWD NRTAAGVNAY TFSSAASTTS TSSSSSASST TPAGASYSNA
     HKQHQQQPQS VKGPSGRSST SVKSNGSSTK VSASSGSGSR SGRAGSSYLA QQQPGRSSGG
     GSSNGVIKSK SESSSKSLPA AQKSSTTLGK SSTVSPGAQN FAKAAAIGQS SPKKAEGGAT
     SAVVTSAGGR SSGVVAPFGR GKPVAGQGGP AATAASNVAQ LGSVSGNSNI LAGPIGTFNV
     ADVAAVNAAA AAGAAAATNS NVKPIAPIAP PSKRVGSPTQ VQQQHQTQQQ QQQQLPQPAP
     VPGPQPQQQP LQQQQQQQAP QQQPQQPNQQ QQPQTSQQNL VINTNLLNDL MAASAANTTS
     DSFSAQLAAK LSSAYSLFSD YQQSQWGKLG DPGIGGGAGA VGDGLPQADA SKAPGYNRNI
     LSSPVGSSKA SSNHSTSPPV GNVIQQQQQQ QPQSSQQALN IITSGPGGPA TAPARSPMVS
     ANEGNPAVGQ PSMNGTQGLG ETAPAHSPGV IKPPTATVPI QRHVPMPISA PEAGAPPTFG
     AIGSNPASGN NSAAAQAAAA AAASAMIDRQ QQNLQNLQTL QNLQRMVGAS QQQQPQQQLN
     YPMDPTSSFI VDANNVLRLN PRVIFPQGNT KPPQPPPQGG TQSNVFGGNP GRQPPGTGAR
     QPGGAAAQRW YGGTLEYPSY TGRDMLHLEN GAGGMAGMGS PSAMSPNHDD IRKMPRPIGT
     ERAASWKYNN FNVGGPSLNM EDALASVLPP WAHELKAQPP GLQQPPPPPQ SQQQQQQPLN
     WLKQQPQQQQ YRAYNNGPYP QQQQQHEPMN MPMDYHNMQA PPNMSQQQQQ HVNLMPSYGY
     QHFVGAPGAV DISAHMPDKM EVWDHHDKHM PWTNYTTNWS N
 
 
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