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 27-MAR-2024, entry version 176.
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 GlyGen; Q9VCA8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9VCA8; -.
DR PaxDb; 7227-FBpp0293580; -.
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 AGR; FB:FBgn0043884; -.
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 cell types or 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:0045087; P:innate immune response; IBA:GO_Central.
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:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0044319; P:wound healing, spreading of cells; IGI:FlyBase.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IGI:FlyBase.
DR CDD; cd22404; KH-I_MASK; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 7.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047373; KH-I_MASK.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR23206:SF7; ANKYRIN REPEAT AND KH DOMAIN-CONTAINING PROTEIN 1 ISOFORM X1; 1.
DR PANTHER; PTHR23206; MASK PROTEIN; 1.
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; Ankyrin repeat; 3.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 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
//
