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LOK_DROME
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   03-AUG-2022, entry version 189.
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; O61267; -.
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   CTD; 35288; -.
DR   FlyBase; FBgn0019686; lok.
DR   VEuPathDB; VectorBase:FBgn0019686; -.
DR   eggNOG; KOG0615; Eukaryota.
DR   GeneTree; ENSGT00800000124190; -.
DR   InParanoid; O61267; -.
DR   OMA; FVHDNSF; -.
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 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: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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:FlyBase.
DR   GO; GO:0006915; P:apoptotic process; IMP:FlyBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; 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: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; cd00060; FHA; 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   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   SUPFAM; SSF56112; SSF56112; 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
 
 
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