S6KL_DROME
ID S6KL_DROME Reviewed; 483 AA.
AC Q9VWQ2; B9EQU9; M9NEP2; M9NFD4; O96630;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Serine/threonine-protein kinase S6KL {ECO:0000305};
DE EC=2.7.11.- {ECO:0000305};
DE AltName: Full=Protein kinase-like 17E {ECO:0000312|EMBL:AAF48886.1};
DE AltName: Full=S6 kinase-like protein {ECO:0000303|PubMed:25748449};
GN Name=S6KL {ECO:0000312|FlyBase:FBgn0283473};
GN Synonyms=Bin4 {ECO:0000303|PubMed:10717484},
GN Pk17E {ECO:0000312|FlyBase:FBgn0283473};
GN ORFNames=CG7001 {ECO:0000312|FlyBase:FBgn0283473};
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|EMBL:AAC72971.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10717484; DOI=10.1016/s0378-1119(00)00048-2;
RA Zhu W., Hanes S.D.;
RT "Identification of Drosophila bicoid-interacting proteins using a custom
RT two-hybrid selection.";
RL Gene 245:329-339(2000).
RN [2] {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 [3] {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 [4] {ECO:0000312|EMBL:AAL39636.1, ECO:0000312|EMBL:ACM16741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39636.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39636.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, COFACTOR, INTERACTION WITH TKV, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-193.
RX PubMed=25748449; DOI=10.1371/journal.pgen.1004984;
RA Zhao G., Wu Y., Du L., Li W., Xiong Y., Yao A., Wang Q., Zhang Y.Q.;
RT "Drosophila S6 Kinase like inhibits neuromuscular junction growth by
RT downregulating the BMP receptor thickveins.";
RL PLoS Genet. 11:E1004984-E1004984(2015).
CC -!- FUNCTION: Displays kinase activity. Inhibits neuromuscular junction
CC (NMJ) growth by interacting with and promoting the proteasome-mediated
CC degradation of the receptor tkv which inhibits bone morphogenetic
CC protein (BMP) signaling. {ECO:0000269|PubMed:25748449}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25748449};
CC -!- SUBUNIT: Interacts with tkv. {ECO:0000269|PubMed:25748449}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25748449}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A {ECO:0000312|FlyBase:FBgn0283473};
CC IsoId=Q9VWQ2-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0283473};
CC IsoId=Q9VWQ2-3; Sequence=VSP_057952;
CC Name=C {ECO:0000312|FlyBase:FBgn0283473};
CC IsoId=Q9VWQ2-2; Sequence=VSP_057953;
CC -!- DISRUPTION PHENOTYPE: Mutants are viable and fertile but display NMJ
CC overgrowth with excess satellite boutons, fewer and larger synaptic
CC vesicles, defective synaptic endocytosis and increased levels of tkv.
CC {ECO:0000269|PubMed:25748449}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AF096866; AAC72971.1; -; mRNA.
DR EMBL; AE014298; AAF48886.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07455.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07456.1; -; Genomic_DNA.
DR EMBL; AY069491; AAL39636.1; -; mRNA.
DR EMBL; BT058024; ACM16741.1; -; mRNA.
DR RefSeq; NP_001245742.1; NM_001258813.1. [Q9VWQ2-3]
DR RefSeq; NP_001245743.1; NM_001258814.2. [Q9VWQ2-2]
DR RefSeq; NP_524861.2; NM_080122.4. [Q9VWQ2-1]
DR AlphaFoldDB; Q9VWQ2; -.
DR SMR; Q9VWQ2; -.
DR IntAct; Q9VWQ2; 5.
DR STRING; 7227.FBpp0074405; -.
DR PaxDb; Q9VWQ2; -.
DR DNASU; 45970; -.
DR EnsemblMetazoa; FBtr0074634; FBpp0074405; FBgn0283473. [Q9VWQ2-1]
DR EnsemblMetazoa; FBtr0307198; FBpp0298027; FBgn0283473. [Q9VWQ2-3]
DR EnsemblMetazoa; FBtr0307199; FBpp0298028; FBgn0283473. [Q9VWQ2-2]
DR GeneID; 45970; -.
DR KEGG; dme:Dmel_CG7001; -.
DR UCSC; CG7001-RA; d. melanogaster. [Q9VWQ2-1]
DR CTD; 45970; -.
DR FlyBase; FBgn0283473; S6KL.
DR VEuPathDB; VectorBase:FBgn0283473; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_184_1_1; -.
DR InParanoid; Q9VWQ2; -.
DR OMA; KTDNSLC; -.
DR PhylomeDB; Q9VWQ2; -.
DR SignaLink; Q9VWQ2; -.
DR BioGRID-ORCS; 45970; 0 hits in 2 CRISPR screens.
DR ChiTaRS; S6KL; fly.
DR GenomeRNAi; 45970; -.
DR PRO; PR:Q9VWQ2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0283473; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; Q9VWQ2; baseline and differential.
DR Genevisible; Q9VWQ2; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05123; STKc_AGC; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR045270; STKc_AGC.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..483
FT /note="Serine/threonine-protein kinase S6KL"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434556"
FT DOMAIN 159..435
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 165..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..314
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_057952"
FT VAR_SEQ 85..86
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_057953"
FT MUTAGEN 193
FT /note="K->A: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:25748449"
FT CONFLICT 42
FT /note="E -> EQQQQ (in Ref. 1; AAC72971)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="I -> N (in Ref. 1; AAC72971)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="R -> G (in Ref. 4; ACM16741)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="H -> Q (in Ref. 1; AAC72971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 55372 MW; 24629C417D601F0F CRC64;
MGNSQPRNAS RSRRTSQWPQ GAAELGASAS DHHYHQEELY QEQQQQQQQP QQEQPSSRRI
QFQAHTNQPT QSHPPGDEEQ PVQSQQQQLS TWSLGSLSGG RLNWSFSGAR NSFRHRNKAT
RKSLTSLHGS RRGKTQWHRP LTNSIFNSHF KETSKNDLYR IDHLVAKGAF GVVFKVSSKS
DISQCYALKV LKKSKLIEDN SVRQIKDEAD IQKVCGHHPF IVKQIDLWQN RHNLHILSEY
VPNGELFSKI THFSIDLVRL YIGEIALALD FLHNAGIIYR DAKPENILLT EQFHIKLTDF
GLSKWLKLGA NTRTMCGTFK YMAPEILCGE PYGHAVDWWA LGVIACQMLT QKSPNIKRHL
LRRRESVEPE DGLSNAPSIA QINGCLQDSD GDSEDFLPEE VQHLTHEGRD VLRKLLTIEP
RQRIRSVMAL QRIAIYKDYN LSSKQLLSLS PREIIARDGI RIYEDRHFDQ LTNQCAIDAF
LDF
