ID LOK_DROME Reviewed; 476 AA.
AC O61267; O61268; P91876; Q8SZS3;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 195.
DE RecName: Full=Ovarian-specific serine/threonine-protein kinase Lok;
DE EC=2.7.11.1;
DE AltName: Full=Protein loki;
DE AltName: Full=dMNK;
GN Name=lok; ORFNames=CG10895;
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}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=9507063; DOI=10.1016/s0925-4773(97)00200-1;
RA Oishi I., Sugiyama S., Otani H., Yamamura H., Nishida Y., Minami Y.;
RT "A novel Drosophila nuclear protein serine/threonine kinase expressed in
RT the germline during its establishment.";
RL Mech. Dev. 71:49-63(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE (ISOFORM SHORT).
RC STRAIN=Oregon-R; TISSUE=Ovary;
RA Larochelle S., Suter B.;
RT "Identification of a novel ovarian specific protein kinase.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC STRAIN=Berkeley; TISSUE=Embryo;
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]
RP DISRUPTION PHENOTYPE.
RX PubMed=34644293; DOI=10.1371/journal.pgen.1009834;
RA Yang Y., Kong R., Goh F.G., Somers W.G., Hime G.R., Li Z., Cai Y.;
RT "dRTEL1 is essential for the maintenance of Drosophila male germline stem
RT cells.";
RL PLoS Genet. 17:e1009834-e1009834(2021).
CC -!- FUNCTION: May have a role in germline establishment.
CC {ECO:0000269|PubMed:9507063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
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;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9507063}.
CC Note=Speckled subnuclear compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O61267-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O61267-2; Sequence=VSP_004865;
CC -!- TISSUE SPECIFICITY: In stage 3 embryos, both isoforms are expressed in
CC both somatic and pole cell nuclei. Expression in pole cell nuclei is
CC sustained until stage 9 and weakly expressed after pole cell
CC invagination into the abdominal cavity. {ECO:0000269|PubMed:9507063}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in adult
CC females. Levels of the long isoform remain fairly constant from ovaries
CC to embryos, the levels of short isoform decrease dramatically.
CC {ECO:0000269|PubMed:9507063}.
CC -!- DISRUPTION PHENOTYPE: Does not affect male germline stem cells
CC maintenance (PubMed:34644293). In the germline, RNAi-mediated knockdown
CC of Rtel1 in lok mutant background results in partial rescue of single
CC Rtel1 knockdown phenotype which includes loss of germline stem cell and
CC reduced levels of Stat92E expression (PubMed:34644293).
CC {ECO:0000269|PubMed:34644293}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CDS1 subfamily. {ECO:0000305}.
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DR EMBL; AB007821; BAA28755.1; -; mRNA.
DR EMBL; AB007822; BAA28756.1; -; mRNA.
DR EMBL; U87984; AAB49642.1; -; mRNA.
DR EMBL; AE014134; AAF53867.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN11062.1; -; Genomic_DNA.
DR EMBL; AY070549; AAL48020.1; -; mRNA.
DR RefSeq; NP_477218.1; NM_057870.4. [O61267-2]
DR RefSeq; NP_477219.1; NM_057871.4. [O61267-1]
DR RefSeq; NP_724241.1; NM_165318.3. [O61267-2]
DR AlphaFoldDB; O61267; -.
DR SMR; O61267; -.
DR BioGRID; 61259; 56.
DR IntAct; O61267; 6.
DR STRING; 7227.FBpp0080860; -.
DR PaxDb; 7227-FBpp0080860; -.
DR DNASU; 35288; -.
DR EnsemblMetazoa; FBtr0081328; FBpp0080860; FBgn0019686. [O61267-1]
DR EnsemblMetazoa; FBtr0081329; FBpp0080861; FBgn0019686. [O61267-2]
DR EnsemblMetazoa; FBtr0081330; FBpp0080862; FBgn0019686. [O61267-2]
DR GeneID; 35288; -.
DR KEGG; dme:Dmel_CG10895; -.
DR AGR; FB:FBgn0019686; -.
DR CTD; 35288; -.
DR FlyBase; FBgn0019686; lok.
DR VEuPathDB; VectorBase:FBgn0019686; -.
DR eggNOG; KOG0615; Eukaryota.
DR GeneTree; ENSGT00800000124190; -.
DR InParanoid; O61267; -.
DR OMA; FAYGHPA; -.
DR OrthoDB; 20430at2759; -.
DR PhylomeDB; O61267; -.
DR BRENDA; 2.7.11.1; 1994.
DR Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR Reactome; R-DME-69541; Stabilization of p53.
DR Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR BioGRID-ORCS; 35288; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35288; -.
DR PRO; PR:O61267; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0019686; Expressed in cleaving embryo and 57 other cell types or tissues.
DR ExpressionAtlas; O61267; baseline and differential.
DR Genevisible; O61267; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:FlyBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0050321; F:tau-protein kinase activity; IDA:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IMP:FlyBase.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:BHF-UCL.
DR GO; GO:0071481; P:cellular response to X-ray; IMP:FlyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0006974; P:DNA damage response; IMP:FlyBase.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IEP:UniProtKB.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IGI:BHF-UCL.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:FlyBase.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IDA:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IGI:FlyBase.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; NAS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IMP:FlyBase.
DR CDD; cd22666; FHA_CHK2; 1.
DR CDD; cd14084; STKc_Chk2; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR PANTHER; PTHR44167:SF8; OVARIAN-SPECIFIC SERINE_THREONINE-PROTEIN KINASE LOK; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..476
FT /note="Ovarian-specific serine/threonine-protein kinase
FT Lok"
FT /id="PRO_0000086237"
FT DOMAIN 69..129
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086,
FT ECO:0000305"
FT DOMAIN 174..441
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 180..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 46..62
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9507063"
FT /id="VSP_004865"
SQ SEQUENCE 476 AA; 54261 MW; 58D583E015C4E626 CRC64;
MARDTQGTQG TQSQASNIWT QVESQPMEKI VWGRLYGKNI KIKSLGTSSK YRIIYTHSSF
SVDLNNDEFT AGRGEANDLI LTLNDLPEKI LTRISKVHFI IKRANCELTN PVYIQDLSRN
GTFVNNEKIG TNRMRILKND DVISLSHPTY KAFVFKDLSP NESIGLPEEI NKTYYVNRKL
GSGAYGLVRL VYDTRTCQQF AMKIVKKNML SGARPSTNFS DPDRVLNEAK IMKNLSHPCV
VRMHDIVDKP DSVYMVLEFM RGGDLLNRII SNKLLSEDIS KLYFYQMCHA VKYLHDRGIT
HRDLKPDNVL LETNDEETLL KVSDFGLSKF VQKDSVMRTL CGTPLYVAPE VLITGGREAY
TKKVDIWSLG VVLFTCLSGT LPFSDEYGTP AAQQIKKGRF AYGHPSWKSV SQRAKLLINQ
MLIVDPERRP SIDDVLQSSW LRDAPMLQKA KRLMKLDGME IEEENFLEPP TKRSRR
//
