KTU_DROPS
ID KTU_DROPS Reviewed; 846 AA.
AC Q292G3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 68.
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=GA13787;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
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; CM000071; EAL24899.2; -; Genomic_DNA.
DR RefSeq; XP_001360324.2; XM_001360287.3.
DR RefSeq; XP_015039219.1; XM_015183733.1.
DR AlphaFoldDB; Q292G3; -.
DR SMR; Q292G3; -.
DR STRING; 7237.FBpp0277424; -.
DR EnsemblMetazoa; FBtr0278986; FBpp0277424; FBgn0073823.
DR EnsemblMetazoa; FBtr0368564; FBpp0331303; FBgn0073823.
DR GeneID; 4803636; -.
DR KEGG; dpo:Dpse_GA13787; -.
DR eggNOG; KOG4356; Eukaryota.
DR HOGENOM; CLU_012715_0_0_1; -.
DR InParanoid; Q292G3; -.
DR OMA; YSIKHSH; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0073823; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..846
FT /note="Protein kintoun"
FT /id="PRO_0000365810"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0E9G3"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ SEQUENCE 846 AA; 95653 MW; 1AA6598C8227B89F CRC64;
MSTAAGSRKK HSKLHNEERA DITKDEFEAI REALSKEEFR KLFFDYVEEV QDPENRKIYE
QEITQLEKER GVDIKFVHPK PGFVVKTSID GELKCFINIA SSPEVARPNS EVGMNPETGG
RGLSWSIPMA QTGGRDDCDA KNNHCKVFDV VFHPDALHLS TRDSQFRKAL IDTALDAVER
EYEVALDRAN LKYPKLDYKG IARPTVIRKL AANPTPEEQE PHPLEHMYPT KPPASNSEPK
ILPMKTKAAP VPEFAVPKYS IKQSHDVDLS EYTDELDAKL HVTVPRSLVV EIELPLLRST
AECQLDVTAK SVYLLSERLG AKYRLKLDLP FVVDDKAGNA RFDTEKRRLS ITLPVVRKSV
NQQRQMHDTL RYLSREDSGV ELHSNSESPV EDDADGYMPE TPELETAAPP DPPALTPSTF
LKDSVHYQLP KFDCNALDNA MAFVLDVAHV QPDSIVTLKT DRSVSVKFAT IGSGYYPTHY
AFYMELPSVD MEEYHKDHCI ESIEAEAWDN NVIMKLFLGA ESKAPTSYLA GLHANGLKEY
QVYGHYKAKT DKNNECEPNP PRDVQIMRTD DAVVITVRPP HTSITTEEDD EQQQQLHKKP
SKKQRKRNKK QRSYSESACE EMLDQQDGPL GRKKDATTPM VPQRKQRSYS ECNDSTIGSE
NVNRGILKRF SRYGPRPSMS DSCSSIDDCG FSSHSCSVDA SSSLFSQSFN GIPEEDRTEE
GLSESCKKTV RFNDQIMKQV FRHDSSILGQ RKKNQKRRNC KLRAQQRRLS EGDSADYEET
RDTALKQQGE PSGNKLHDSG LDLTGASASH RTDNNSKSYR TRQDHADADA KNDAMMFEMD
DEDDEI
