ACK_DROME
ID ACK_DROME Reviewed; 1073 AA.
AC Q9VZI2; Q9U4G3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Activated Cdc42 kinase Ack {ECO:0000303|PubMed:18816840};
DE EC=2.7.10.2 {ECO:0000269|PubMed:11773052};
DE EC=2.7.11.1 {ECO:0000269|PubMed:11773052};
GN Name=Ack {ECO:0000312|FlyBase:FBgn0028484};
GN Synonyms=DACK {ECO:0000303|PubMed:11997505},
GN p145 {ECO:0000303|PubMed:11773052};
GN ORFNames=CG14992 {ECO:0000312|FlyBase:FBgn0028484};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAD55428.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAD55428.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAD55428.1};
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 [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH DOCK AND SH3PX1,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-156.
RX PubMed=11773052; DOI=10.1074/jbc.m110172200;
RA Worby C.A., Simonson-Leff N., Clemens J.C., Huddler D. Jr., Muda M.,
RA Dixon J.E.;
RT "Drosophila Ack targets its substrate, the sorting nexin DSH3PX1, to a
RT protein complex involved in axonal guidance.";
RL J. Biol. Chem. 277:9422-9428(2002).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP LYS-156.
RX PubMed=11997505; DOI=10.1128/mcb.22.11.3685-3697.2002;
RA Sem K.P., Zahedi B., Tan I., Deak M., Lim L., Harden N.;
RT "ACK family tyrosine kinase activity is a component of Dcdc42 signaling
RT during dorsal closure in Drosophila melanogaster.";
RL Mol. Cell. Biol. 22:3685-3697(2002).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18816840; DOI=10.1002/dvdy.21722;
RA Zahedi B., Shen W., Xu X., Chen X., Mahey M., Harden N.;
RT "Leading edge-secreted Dpp cooperates with ACK-dependent signaling from the
RT amnioserosa to regulate myosin levels during dorsal closure.";
RL Dev. Dyn. 237:2936-2946(2008).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DRK, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-156.
RX PubMed=22615583; DOI=10.1371/journal.pgen.1002725;
RA Schoenherr J.A., Drennan J.M., Martinez J.S., Chikka M.R., Hall M.C.,
RA Chang H.C., Clemens J.C.;
RT "Drosophila activated Cdc42 kinase has an anti-apoptotic function.";
RL PLoS Genet. 8:E1002725-E1002725(2012).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DOCK, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-156 AND 549-LEU--ASP-551.
RC STRAIN=Canton-S {ECO:0000303|PubMed:23562806};
RX PubMed=23562806; DOI=10.1016/j.ydbio.2013.02.025;
RA Abdallah A.M., Zhou X., Kim C., Shah K.K., Hogden C., Schoenherr J.A.,
RA Clemens J.C., Chang H.C.;
RT "Activated Cdc42 kinase regulates Dock localization in male germ cells
RT during Drosophila spermatogenesis.";
RL Dev. Biol. 378:141-153(2013).
RN [9] {ECO:0000305}
RP MUTAGENESIS OF LYS-156.
RX PubMed=23579691; DOI=10.1371/journal.pone.0060180;
RA Shen W., Chen X., Cormier O., Cheng D.C., Reed B., Harden N.;
RT "Modulation of morphogenesis by Egfr during dorsal closure in Drosophila.";
RL PLoS ONE 8:E60180-E60180(2013).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF LYS-156.
RX PubMed=25223282; DOI=10.15252/embr.201438688;
RA Strochlic T.I., Stavrides K.P., Thomas S.V., Nicolas E., O'Reilly A.M.,
RA Peterson J.R.;
RT "Ack kinase regulates CTP synthase filaments during Drosophila oogenesis.";
RL EMBO Rep. 15:1184-1191(2014).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH YKI AND EX, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LYS-156.
RX PubMed=27462444; DOI=10.1038/celldisc.2015.47;
RA Hu L., Xu J., Yin M.X., Zhang L., Lu Y., Wu W., Xue Z., Ho M.S., Gao G.,
RA Zhao Y., Zhang L.;
RT "Ack promotes tissue growth via phosphorylation and suppression of the
RT Hippo pathway component Expanded.";
RL Cell Discov. 2:15047-15047(2016).
CC -!- FUNCTION: Non-receptor tyrosine-protein and serine/threonine-protein
CC kinase that is implicated in diverse biological functions such as cell
CC survival, cell differentiation, cell growth and proliferation
CC (PubMed:11997505, PubMed:18816840, PubMed:22615583, PubMed:23562806,
CC PubMed:25223282, PubMed:27462444). Phosphorylates SH3PX1 and ex
CC (PubMed:22615583, PubMed:11773052, PubMed:27462444). Phosphorylates
CC SH3PX1 predominantly on 'Tyr-56', which likely promotes the recruitment
CC of SH3PX1 to an axonal guidance receptor complex that includes dock and
CC Dscam; because phosphorylation of SH3PX1 increases its interaction with
CC the complex member dock while decreasing its interaction with the actin
CC cytoskeleton modulator WASp (PubMed:11773052). In the wing and eye,
CC promotes tissue growth, and during embryogenesis coordinates cell shape
CC changes required for correct dorsal closure (PubMed:22615583,
CC PubMed:27462444, PubMed:18816840). Functions in the negative regulation
CC of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway by enhancing yki
CC activity thereby promoting cell proliferation and inhibiting apoptosis
CC (PubMed:22615583, PubMed:27462444). This is accomplished, at least in
CC part, by phosphorylating ex thereby reducing its ability to efficiently
CC activate the Hippo signaling cascade (PubMed:27462444). In the eye
CC disk, wing disk and possibly spermatids, inhibits programmed cell death
CC induced by hid and rpr through a mechanism that is independent of the
CC MAP kinase signal transduction pathway (PubMed:22615583). Essential for
CC male and female fertility (PubMed:22615583, PubMed:23562806). During
CC oogenesis required for the correct temporal assembly, and consequently
CC the catalytic activity of long CTPsyn filaments (cytoophidium) in the
CC germline nurse cells, likely by phosphorylating an unidentified
CC substrate that is essential for linking individual CTPsyn filaments
CC into large, catalytically active assemblies (PubMed:25223282).
CC {ECO:0000269|PubMed:11773052, ECO:0000269|PubMed:11997505,
CC ECO:0000269|PubMed:18816840, ECO:0000269|PubMed:22615583,
CC ECO:0000269|PubMed:23562806, ECO:0000269|PubMed:25223282,
CC ECO:0000269|PubMed:27462444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000269|PubMed:11773052};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11773052};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11773052};
CC -!- SUBUNIT: Interacts with yki and ex (PubMed:27462444). Interacts with
CC drk (PubMed:22615583). Likely to be a member of an axonal guidance
CC receptor complex that includes SH3PX1, dock and Dscam
CC (PubMed:11773052). Interacts (via N-terminus) with dock
CC (PubMed:23562806, PubMed:11773052). Interacts with SH3PX1 (via SH3
CC domain) (PubMed:11773052). {ECO:0000269|PubMed:11773052,
CC ECO:0000269|PubMed:22615583, ECO:0000269|PubMed:23562806,
CC ECO:0000269|PubMed:27462444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22615583,
CC ECO:0000269|PubMed:25223282}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:23562806}. Note=In nurse cells localizes to
CC cytoophidium, a subcellular filamentary structure where CTP synthase is
CC compartmentalized (PubMed:25223282). In third instar photoreceptor R-
CC cells, expressed in the cytoplasm and cytoplasmic puncta
CC (PubMed:22615583). In spermatocytes displays localization to peripheral
CC clathrin-positive structures and localization to some secretory
CC clathrin (PubMed:23562806). {ECO:0000269|PubMed:22615583,
CC ECO:0000269|PubMed:23562806, ECO:0000269|PubMed:25223282}.
CC -!- TISSUE SPECIFICITY: Detected in ovaries (at protein level)
CC (PubMed:25223282). In adults, relatively higher expression in the head
CC compared to the body (PubMed:11997505). {ECO:0000269|PubMed:11997505,
CC ECO:0000269|PubMed:25223282}.
CC -!- DEVELOPMENTAL STAGE: In stage 13 embryos at the beginning of dorsal
CC closure, enriched in the leading edge of the epidermis (at protein
CC level). {ECO:0000269|PubMed:11997505}.
CC -!- DOMAIN: The SAM, Protein kinase and SH3 domains are required for sperm
CC formation. {ECO:0000269|PubMed:23562806}.
CC -!- DOMAIN: The SAM and SH3 domains are required for localization to
CC clathrin-coated vesicles in spermatocytes.
CC {ECO:0000269|PubMed:23562806}.
CC -!- PTM: Phosphorylated (PubMed:22615583). Autophosphorylated
CC (PubMed:11773052). {ECO:0000269|PubMed:11773052,
CC ECO:0000269|PubMed:22615583}.
CC -!- DISRUPTION PHENOTYPE: No visible developmental defects but males and
CC females display reduced fertility (PubMed:27462444, PubMed:22615583,
CC PubMed:23562806). Males are sterile due to disruption of spermatid
CC coiling (PubMed:27462444, PubMed:22615583, PubMed:23562806). Spermatids
CC individualization complexes are displaced from the outer region of the
CC testis coil to the inner region and display increased apoptosis
CC (PubMed:22615583). During oogenesis, defective assembly and disassembly
CC of cytoophidium in nurse cells result in a range of phenotypes
CC resulting from reduced CTP production (PubMed:25223282). These include
CC reduced egg laying, disruptions in the plasma membrane between adjacent
CC nurse cells that result in the nurse cells fusing, and reduced nurse
CC cell nuclei diameter most likely as a result of defective
CC endoreplication (PubMed:25223282). Cytoophidium are observed in the
CC germanium at an earlier developmental stage and persist inappropriately
CC into late-stage egg chambers (PubMed:25223282). The number of
CC cytoophidium in the cytoplasm of nurse cells is increased and their
CC length is reduced (PubMed:25223282). Enhances the small eye phenotype
CC in hid mutants (PubMed:22615583). Developing embryos display a very low
CC frequently of dorsal defects (PubMed:18816840). Simultaneous knockdown
CC of Ack and Ack-like results in many embryos failing to properly secrete
CC the cuticle likely due to the loss of zip expression (PubMed:18816840).
CC Mutants also display defects in the dorsal surface including holes in
CC the cuticle and germband retraction failure (PubMed:18816840).
CC {ECO:0000269|PubMed:18816840, ECO:0000269|PubMed:22615583,
CC ECO:0000269|PubMed:23562806, ECO:0000269|PubMed:25223282,
CC ECO:0000269|PubMed:27462444}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AF181642; AAD55428.1; -; mRNA.
DR EMBL; AE014296; AAF47839.2; -; Genomic_DNA.
DR RefSeq; NP_647859.1; NM_139602.3.
DR AlphaFoldDB; Q9VZI2; -.
DR SMR; Q9VZI2; -.
DR IntAct; Q9VZI2; 3.
DR STRING; 7227.FBpp0073067; -.
DR PaxDb; Q9VZI2; -.
DR PRIDE; Q9VZI2; -.
DR EnsemblMetazoa; FBtr0073211; FBpp0073067; FBgn0028484.
DR GeneID; 38489; -.
DR KEGG; dme:Dmel_CG14992; -.
DR UCSC; CG14992-RA; d. melanogaster.
DR CTD; 107482; -.
DR FlyBase; FBgn0028484; Ack.
DR VEuPathDB; VectorBase:FBgn0028484; -.
DR eggNOG; KOG0199; Eukaryota.
DR GeneTree; ENSGT00940000160853; -.
DR HOGENOM; CLU_000288_7_39_1; -.
DR InParanoid; Q9VZI2; -.
DR OMA; QMYASKD; -.
DR OrthoDB; 1008736at2759; -.
DR PhylomeDB; Q9VZI2; -.
DR SignaLink; Q9VZI2; -.
DR BioGRID-ORCS; 38489; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Ack; fly.
DR GenomeRNAi; 38489; -.
DR PRO; PR:Q9VZI2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0028484; Expressed in crop (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q9VZI2; baseline and differential.
DR GO; GO:0071944; C:cell periphery; IDA:FlyBase.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:FlyBase.
DR GO; GO:0097268; C:cytoophidium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:UniProtKB.
DR GO; GO:0006241; P:CTP biosynthetic process; IMP:UniProtKB.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IGI:UniProtKB.
DR GO; GO:0008258; P:head involution; IGI:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0031034; P:myosin filament assembly; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:UniProtKB.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:FlyBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR015940; UBA.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoplasmic vesicle; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..1073
FT /note="Activated Cdc42 kinase Ack"
FT /id="PRO_0000449972"
FT DOMAIN 123..383
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 386..446
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1029..1072
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 88..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 129..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:27462444"
FT MUTAGEN 156
FT /note="K->A: Loss of enzyme activity. Increase in apoptotic
FT cells in the eye and wing. Increase in bristle number in
FT the interommatidial lattice and decrease in pigment cell
FT number. Disrupts vesicular localization of dock in
FT spermatocytes. Fails to rescue the nurse cell plasma
FT membrane defects and male sterility observed in null
FT mutants. Fails to rescue the small eye phenotype induced by
FT hid but able to rescue the small eye phenotype induced by
FT rpr."
FT /evidence="ECO:0000269|PubMed:11773052,
FT ECO:0000269|PubMed:22615583, ECO:0000269|PubMed:23562806,
FT ECO:0000269|PubMed:25223282"
FT MUTAGEN 156
FT /note="K->R: Loss of enzyme activity. Many embryos die
FT before hatching. Fails to promote yki-dependent tissue
FT growth in the eye and wing. Overexpression in wing imaginal
FT disks frequently results in wings with blisters and ectopic
FT veins. Eyes are disorganized and ommatidia are almost
FT completely absent, eye bristles are not present in
FT posterior two-thirds of the eye and bristle clusters occur
FT at the anterior end. Increased Egfr endocytosis in embryos.
FT No effect on Dpp expression in the leading edge cells."
FT /evidence="ECO:0000269|PubMed:11997505,
FT ECO:0000269|PubMed:23579691, ECO:0000269|PubMed:27462444"
FT MUTAGEN 549..551
FT /note="LID->AAA: Able to rescue male sterility."
FT /evidence="ECO:0000269|PubMed:23562806"
SQ SEQUENCE 1073 AA; 118418 MW; D9BF4BD87235D691 CRC64;
MTSTSAVDGG LGSETAWLED LLREVQLEQF LDRIRDDLQV TRLAHFDYVL PDDLERCGLG
KPAIRRLMEA VRKKKAHQWR KNILSKLIGG GKQPSSKKQS SAARESSQGN GTQLTCLIHE
KDITMGLKLG DGSFGVVRRG EWSASPAGKV IPVAVKVLKS DNLTQPGIID DFFREVQAMH
ALDHANLVRL YGVVLSQPMM MITELAERGS LLDTLRKQCR HTSLTIIWNW SVQIVTGMAY
LEQKRFLHRD LACRNVLLAA GNKIKIGDFG LMRALPQEDD CYVMSEHKKV PFPWCAPESL
RFRQFSHASD TWMFGVTLWE MFSFGEDPWV GLNGSQILRK IDREGERLHQ PDACPPDVYA
MMLQCWDKTP AERPTFAALK EYLASMSPPV MRASRSHHES KGLQIEPGDT IAIIDGRHEL
KLIKGQNQRT FDIGIFPRNL LEQRKVGAAG DVVMRSSVGN GSSSSPFGFC WGGAAAMANG
DDRQRKCASM TNQPHAKERK STSSKQFAYN KLVNDSATGL QRRNAVKHKG VVVGPQRPPP
PQFQQEGILI DISPDMRPIA EAGTGGAKGA GDSSSLQADS SFCILDAPID VPTYAGSSGS
GDLNVSPTYY NEQPQFDFDP AKMTASPGRL QPPPYQMPPT YSNTMEFVQK RDLHQQQLAT
PVRERDPFDT TNVETTVALY SNFNQSLEAA SPPAPIYNSP SVRKSLFGGS KSNKENIPAL
ESAAMQLNLS NLTLERHDAT CIQPVEPVPA PPGDGVLLDK SFIAELEKDM YSNGQNRAQE
EYQRNSTQMY ASKDMVYKQN LTPLKNGAAP GSVHSNHSSP SSTASPKQNN VEAAAAAAAT
TQSVVNRIWY EQVASTQSEY YAQPPTEQAE EQIYQNHRHQ QQQQQELNHS FVAISNRVVA
PKNNAYSSTA SLYDAVAAST AGSTYYGQVP NGSGAVLYDE VTQDDYLRPT RPAPLAPPPL
SAQQIQRRME KMRLQQQQQL DGAHQLYAPV PSDYGREQEK LQQLMQELGS SAVEQDVRNA
LRAASGDVGL ATRHYKIDQL ARLGVAGRPQ CEQALQQTNW SLEVAAELLL NAG
