ID   KTU_DROER               Reviewed;         845 AA.
AC   B3N9E4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 52.
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=GG10709;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
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; CH954177; EDV59631.1; -; Genomic_DNA.
DR   RefSeq; XP_001970572.1; XM_001970536.2.
DR   AlphaFoldDB; B3N9E4; -.
DR   SMR; B3N9E4; -.
DR   STRING; 7220.FBpp0129255; -.
DR   EnsemblMetazoa; FBtr0130763; FBpp0129255; FBgn0103014.
DR   GeneID; 6541773; -.
DR   KEGG; der:6541773; -.
DR   eggNOG; KOG4356; Eukaryota.
DR   HOGENOM; CLU_012715_0_0_1; -.
DR   OMA; YSIKHSH; -.
DR   OrthoDB; 943252at2759; -.
DR   PhylomeDB; B3N9E4; -.
DR   Proteomes; UP000008711; 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.
FT   CHAIN           1..845
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365805"
FT   REGION          362..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
FT   MOD_RES         779
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ   SEQUENCE   845 AA;  95766 MW;  6813835D0F7C7C88 CRC64;
     MSASATRSRN KQSKLRDDER LDISKDEFNR IQEAFGQEEF RKLFFDYVEE IQDPENRKIY
     EEEITQLEKE RGVEVRFIHP KPGFVIKTAL DGELKCFINI AGSEEIERPK NEVATDPSSG
     NRGLSWSIPM AQTSSRDDCD AKNNHCKVFD VVFHPDALHL AKRNKQFRQC LIDTALDAVE
     REYKVSLDRA NLKFPKLDYK GIPRPTVIRK LADNPTAEEQ EPHPLAHMFP TQPPAPGKPE
     PRVLPLKTKP TPVPEFTVPR YSIKHSHDVD LSEYTDELDA KLHVTVPRAL VVEIELPLLR
     STAECQLDVT SKSVYLFSER QGAKYRLKLD LPFTVDDKAG QARFDTDLRR LSITLPVVRK
     SSKEQAQMHE TLRHFSREDS GVELHSNSES PVEEDPDGEL SDSKADISDI SSPTAAPVRH
     SNSPFLKSSV HYQLPSKFDC NVLDNVMAFV LHVPNVQPDS IEQLREQRSL HLQFATIGSG
     YYPTHYAFYV ELPAEHEDSA IESVEAEAWD NNVVLKLCLT SQSETPASYL AGLDATELKE
     YPVHGQYNVK SKEKVIARKE NAPFEIKFEH NQEGQALKVS IRPGTKEEEK ENQDQEPEID
     QQHQQQVQNK KPGKKQRKRN KKERSLSESA CADMILQEPL TKNSELQPKS TFNLPQRKQR
     SYSECNDSTG GSHRGILKRF SRYGPRPSMS DSCSSIDDCS SYSCSVDASG TSLFSHSFGG
     IPEEDRSDAG LSESCKKTVR FNDHIMKQVF RLDSSILGQR KKNQKRRDLK LRAQHRRLSE
     GDSVDYEESR GSALKQQENQ SRNCNKPKGV SVLHDSGLDL TGAPGAHSNN NESEAKNAMM
     FEMDD