ADCK_DROME
ID ADCK_DROME Reviewed; 518 AA.
AC Q9W133;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=AarF domain-containing kinase 1 {ECO:0000303|PubMed:31175694};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=Adck1 {ECO:0000303|PubMed:31175694, ECO:0000312|FlyBase:FBgn0035039};
GN Synonyms=Adck {ECO:0000312|FlyBase:FBgn0035039};
GN ORFNames=CG3608 {ECO:0000312|FlyBase:FBgn0035039};
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:AAM50029.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50029.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM50029.1};
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, AND DISRUPTION PHENOTYPE.
RX PubMed=31175694; DOI=10.1002/dvdy.66;
RA Wisidagama D.R., Thomas S.M., Lam G., Thummel C.S.;
RT "Functional analysis of Aarf domain-containing kinase 1 in Drosophila
RT melanogaster.";
RL Dev. Dyn. 248:762-770(2019).
RN [5] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 343-ARG--VAL-463.
RX PubMed=31125351; DOI=10.1371/journal.pgen.1008184;
RA Yoon W., Hwang S.H., Lee S.H., Chung J.;
RT "Drosophila ADCK1 is critical for maintaining mitochondrial structures and
RT functions in the muscle.";
RL PLoS Genet. 15:E1008184-E1008184(2019).
CC -!- FUNCTION: Essential for maintaining mitochondrial cristae formation and
CC mitochondrial function by acting via YME1L to regulate the
CC mitochondrial structural proteins Opa1 and Mitofilin (PubMed:31125351).
CC This function is likely to be kinase-independent (By similarity).
CC Functions in tracheal development and larval molting probably by acting
CC in sterol modification and/or intracellular lipid trafficking
CC (PubMed:31175694). The action of this enzyme is not yet clear
CC (Probable). It is not known if it has protein kinase activity and what
CC type of substrate it would phosphorylate (Ser, Thr or Tyr) (Probable).
CC {ECO:0000250|UniProtKB:Q86TW2, ECO:0000269|PubMed:31125351,
CC ECO:0000269|PubMed:31175694, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown is larval lethal
CC (PubMed:31175694, PubMed:31125351). RNAi-mediated knockdown in adults
CC results in the thoracic muscles displaying abnormally orientated fibers
CC as well as an abnormal increase in mitochondrial fusion resulting in
CC mitochondrial dysfunction in ATP production, ROS generation and cell
CC apoptosis (PubMed:31125351). Consequently, adults display a held-up
CC wing phenotype, are unable to fly and also display defects in
CC locomotion (PubMed:31125351). RNAi-mediated knockdown in salivary
CC glands also results in an increase in mitochondrial fusion
CC (PubMed:31125351). RNAi-mediated knockdown in the trachea results in
CC arrested development at either the first or second instar larval stage
CC (PubMed:31175694). In addition the larvae display tracheal defects,
CC such as tracheal breaks and lumen separation, and prematurely wander
CC away from food (PubMed:31175694). {ECO:0000269|PubMed:31125351,
CC ECO:0000269|PubMed:31175694}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AE013599; AAF47244.2; -; Genomic_DNA.
DR EMBL; AY118660; AAM50029.1; -; mRNA.
DR EMBL; AE013599; AHN56646.1; -; Genomic_DNA.
DR RefSeq; NP_001286851.1; NM_001299922.1.
DR RefSeq; NP_611947.2; NM_138103.3.
DR AlphaFoldDB; Q9W133; -.
DR SMR; Q9W133; -.
DR IntAct; Q9W133; 1.
DR STRING; 7227.FBpp0072227; -.
DR PaxDb; Q9W133; -.
DR PRIDE; Q9W133; -.
DR DNASU; 37938; -.
DR EnsemblMetazoa; FBtr0072320; FBpp0072227; FBgn0035039.
DR EnsemblMetazoa; FBtr0343487; FBpp0310095; FBgn0035039.
DR GeneID; 37938; -.
DR KEGG; dme:Dmel_CG3608; -.
DR UCSC; CG3608-RA; d. melanogaster.
DR CTD; 57143; -.
DR FlyBase; FBgn0035039; Adck1.
DR VEuPathDB; VectorBase:FBgn0035039; -.
DR eggNOG; KOG1235; Eukaryota.
DR GeneTree; ENSGT00940000158221; -.
DR HOGENOM; CLU_006533_2_0_1; -.
DR InParanoid; Q9W133; -.
DR OMA; PYVKGNS; -.
DR OrthoDB; 790106at2759; -.
DR PhylomeDB; Q9W133; -.
DR BioGRID-ORCS; 37938; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37938; -.
DR PRO; PR:Q9W133; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0035039; Expressed in crop (Drosophila) and 29 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0055088; P:lipid homeostasis; ISS:FlyBase.
DR GO; GO:0007005; P:mitochondrion organization; ISS:FlyBase.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:1903852; P:positive regulation of cristae formation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
DR CDD; cd13969; ADCK1-like; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR045307; ADCK1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF03109; ABC1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Secreted;
KW Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..518
FT /note="AarF domain-containing kinase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448065"
FT DOMAIN 149..468
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 155..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 343..463
FT /note="Missing: Third instar larval lethal. First and
FT second instar larvae are reduced in size."
FT /evidence="ECO:0000269|PubMed:31125351"
SQ SEQUENCE 518 AA; 59859 MW; 59C731F6247BBCF8 CRC64;
MLLRRVLGYG VVGAGLASAG WSLHTNDYDP NSLGIVRLSR SAAAVVDVAL TYKRELYYKE
WDKETPEYKA EKSRVHKIAA EKLLQLICIN KGVYIKVGQH IGALEYLLPK EFVQTMKVLH
SDAPQNPIED LYKVIRQDLH CNPEEIFDSF EREPLGTASL AQVHKARLKT GELVAVKVQH
PYVKGNSRVD MKTMELAVNV LARIFPDFKI HWLVEESKKN LPIELDFLNE GRNAEKVAKQ
FKKYSWLRVP KIYWKYSSSR VLVMEYLEGG HVTDLDYIRR NKIDSFAVAN RIGQLYSEMI
FRTGFVHSDP HPGNILVRRT PENSLEIVLL DHGLYANLTD KFRYDYSNLW LSILKVDRKA
MRQHSEQLGI KGDLYGLFAC MVTGRPWETV MQGLTKVKYS KEEKNTLQNN TSLVLPHISD
VLEQVDRQML LILKTNDLIR GIESTLRTQN RMTAFWVMSK CCVQSSYAEQ RAKQSDSGSS
RILWLRVRER WELFKLNCYY LYLGLINFGF LEALKQVI
