KTU_DROME
ID KTU_DROME Reviewed; 834 AA.
AC Q0E9G3; C7LA99; E2QC75; Q8T8Q3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein kintoun {ECO:0000255|HAMAP-Rule:MF_03069};
DE AltName: Full=Dynein assembly factor 2, axonemal homolog {ECO:0000255|HAMAP-Rule:MF_03069};
DE AltName: Full=PP1-interacting protein 20 {ECO:0000255|HAMAP-Rule:MF_03069};
GN Name=Nop17l {ECO:0000255|HAMAP-Rule:MF_03069};
GN Synonyms=Ppi20 {ECO:0000255|HAMAP-Rule:MF_03069}; ORFNames=CG1553;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PP1ALPHA-96A; PP1-87B;
RP PP1-13C AND FLW.
RX PubMed=17007873; DOI=10.1016/j.jmb.2006.08.094;
RA Bennett D., Lyulcheva E., Alphey L.;
RT "Towards a comprehensive analysis of the protein phosphatase 1 interactome
RT in Drosophila.";
RL J. Mol. Biol. 364:196-212(2006).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378 AND SER-777, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for cytoplasmic pre-assembly of axonemal dyneins,
CC thereby playing a central role in motility in cilia and flagella.
CC Involved in pre-assembly of dynein arm complexes in the cytoplasm
CC before intraflagellar transport loads them for the ciliary compartment.
CC {ECO:0000255|HAMAP-Rule:MF_03069}.
CC -!- SUBUNIT: Interacts with Pp1alpha-96A, Pp1-87B, Pp1-13C and flw.
CC {ECO:0000255|HAMAP-Rule:MF_03069, ECO:0000269|PubMed:17007873}.
CC -!- INTERACTION:
CC Q0E9G3; P48462: flw; NbExp=3; IntAct=EBI-150380, EBI-869621;
CC Q0E9G3; Q05547: Pp1-13C; NbExp=2; IntAct=EBI-150380, EBI-157144;
CC Q0E9G3; P12982: Pp1-87B; NbExp=3; IntAct=EBI-150380, EBI-152633;
CC Q0E9G3; P48461: Pp1alpha-96A; NbExp=4; IntAct=EBI-150380, EBI-91997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}.
CC -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03069}.
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DR EMBL; AM262814; CAK18654.1; -; mRNA.
DR EMBL; AE013599; AAF59190.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68861.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68862.1; -; Genomic_DNA.
DR EMBL; AY075579; AAL68384.1; -; mRNA.
DR EMBL; BT099649; ACV21069.1; -; mRNA.
DR EMBL; BT133346; AFF57511.1; -; mRNA.
DR RefSeq; NP_610324.2; NM_136480.3.
DR RefSeq; NP_724604.1; NM_165557.2.
DR RefSeq; NP_724605.1; NM_165558.2.
DR AlphaFoldDB; Q0E9G3; -.
DR SMR; Q0E9G3; -.
DR BioGRID; 61597; 6.
DR IntAct; Q0E9G3; 8.
DR STRING; 7227.FBpp0087974; -.
DR iPTMnet; Q0E9G3; -.
DR PaxDb; Q0E9G3; -.
DR PRIDE; Q0E9G3; -.
DR DNASU; 35730; -.
DR EnsemblMetazoa; FBtr0088900; FBpp0087974; FBgn0033224.
DR EnsemblMetazoa; FBtr0088901; FBpp0087975; FBgn0033224.
DR EnsemblMetazoa; FBtr0088902; FBpp0087976; FBgn0033224.
DR GeneID; 35730; -.
DR KEGG; dme:Dmel_CG1553; -.
DR UCSC; CG1553-RA; d. melanogaster.
DR UCSC; CG1553-RB; d. melanogaster.
DR CTD; 35730; -.
DR FlyBase; FBgn0033224; Nop17l.
DR VEuPathDB; VectorBase:FBgn0033224; -.
DR eggNOG; KOG4356; Eukaryota.
DR GeneTree; ENSGT00510000048466; -.
DR HOGENOM; CLU_012715_0_0_1; -.
DR InParanoid; Q0E9G3; -.
DR OMA; YSIKHSH; -.
DR OrthoDB; 943252at2759; -.
DR PhylomeDB; Q0E9G3; -.
DR BioGRID-ORCS; 35730; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35730; -.
DR PRO; PR:Q0E9G3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033224; Expressed in adult hindgut (Drosophila) and 27 other tissues.
DR Genevisible; Q0E9G3; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:FlyBase.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0060285; P:cilium-dependent cell motility; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03069; Kintoun; 1.
DR InterPro; IPR034727; Kintoun.
DR InterPro; IPR012981; PIH1_N.
DR InterPro; IPR041442; PIH1D1/2/3_CS-like.
DR Pfam; PF08190; PIH1; 1.
DR Pfam; PF18201; PIH1_CS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..834
FT /note="Protein kintoun"
FT /id="PRO_0000365807"
FT REGION 214..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 160
FT /note="M -> I (in Ref. 5; ACV21069)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="H -> R (in Ref. 4; AAL68384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 94774 MW; 5912223C12B72881 CRC64;
MSASRSRNKQ SKLCDDERLD ISRDEFNRFQ EAFGKEEFRK LFFDYVDEIQ DPENRKIYES
EITQLEKERG VEVRFIHPKP GFVIKTALDG ELKCFINIAS CEEIQRPKNE VATDPSSGSR
GLSWSIPMAQ TTSRDDFDAK NNHCKVFDVV FHPDALHLAM RNKQFRQCLI DTALDAIERE
YKVSLDRANL KFPKLDYKGI PRPTVIRKMA DNPTAEEQEP HPLAHMFPTK PPAPGKQEPR
VLPMKTKPSP VPEFTVPRYT IKHSHDVDLS EYTDELDAKL HVTVPRSLVV EIELPLLRST
AECQLDVTSK SIYLFSERQG AKYRLKLDLP FIVDDKAGRA RFDTDMRRLS ITLPVVRKSI
QEQAQMHETL RHFSREDSGV ELHSNSESPV EEDPDGELSD SKADISETSS PSVAPANSPF
LKSSVHYQLP SKFDCNVLDN VMAFVLHVPN VQPDSIEQLR EQRSLHLKFA TIGSGYYPTH
YAFYVELSAE HEDSSIESAE AEAWDNNVVL KLCLNSQSET PASYLAGLDA TELKEYPVHG
QYHVKSKGKV NAKKDNAPLD VKFERNQEGH ALKVTIRPGT KEEEEDKENQ DQEPESDQQQ
QQQVQNKKPG KKQRKKNKKE RSLSESACAD MILQEPLAKT NELQPRATFK LPPQRKQRSY
SECNDSTGRS HRGILKRFSR YGPRPSMSDS WSSIDDSSSY SCSVDASGTS LFSQSFGGIP
EEDRSDAGLS ESCKKTVRFN DHIMKQVFRL DSSILGQRKK NQKRRDLKLR AQQRRLSEGD
SVDYEETRGS ALKQEENPSR NCNDSGLDLT GAAGAHSNNN ESDAKNTMMF EMDD
