ID   KTU_DROSE               Reviewed;         838 AA.
AC   B4HR78;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=GM20755;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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; CH480816; EDW46821.1; -; Genomic_DNA.
DR   RefSeq; XP_002032808.1; XM_002032772.1.
DR   AlphaFoldDB; B4HR78; -.
DR   SMR; B4HR78; -.
DR   STRING; 7238.B4HR78; -.
DR   PRIDE; B4HR78; -.
DR   EnsemblMetazoa; FBtr0203740; FBpp0202232; FBgn0175636.
DR   GeneID; 6608060; -.
DR   KEGG; dse:6608060; -.
DR   HOGENOM; CLU_012715_0_0_1; -.
DR   OMA; YSIKHSH; -.
DR   PhylomeDB; B4HR78; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
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..838
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365811"
FT   REGION          106..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..797
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
FT   MOD_RES         781
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ   SEQUENCE   838 AA;  95203 MW;  5D72D0CC7CB23416 CRC64;
     MSASRSRNKQ SKLCDDERLD ISKDEFNRFQ EAFGQEEFRK LFFDYVDEIQ DPENRKIYEA
     EITQLEKERG VEVRFIHPKP GFVIKTALDG ELKCFINIAS SEEIERPKNE VATDPSSGSR
     GLNWSIPMAQ TTSRDDFDAK NNHCKVFDVV FHPDALHLAM RNKQFRQCLI DTALDAVERE
     YKVSLDRANL KFPKLDYKGI PRPTVIRKMS DNPTAEEQEP HPLAHMFPTK PPAPGKPEPR
     VLPMKTKPTP VPEFTVPRYT IKHSHDVDLS EYTDELDAKL HVTVPRSLVV EIELPLLRST
     AECQLDVTSK SVYLFSERQG AKYRLKLDLP FIVDDKAGRA RFDTDMRRLS ITLPVVRKSV
     QEQAQMHETL RHFSREDSGV ELHSNSESPV EEDPDGELSD SKADISKTSS PTVVRNANSP
     FLKSSVHYQL PSKFDCNVLD NVMAFVLHVP NVQPDSIEQL REQRSLHLKF ATIGSGYYPT
     HYAFYVELSA DHEDSAIESA EAEAWDNNVV LKLYLNSQSE TPAGYLAGLD ATELKEYPVH
     GQYHVKSKEK VNAKKENAPL DVEFERNQEG HALKVTIRPG TKEEEEEEED KENQDQKPES
     DQQQQQQVQN KKSGKKQRKR NKKERSLSES ACADMVLQEP LAKSNELQPR ATFKLPPQRK
     QRSYSESNDS TGRSHRGILK RFSRYGPRPS MSDSCSSIDD SSSYSCSVDA SGASLFSQSF
     GGIPEEDRSD AGLSESCKKT VRFNDHIMKQ VFRLDSSILG QRKKNQKRRD LKLRAQQRRL
     SEGDSVDYEE TRGSALKQKE NPSRNCTDSG LDLTGAAGAH SNNNESDAKN AMMFEMDD