ID   KTU_DROPE               Reviewed;         846 AA.
AC   B4GDK5;
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=GL11241;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479181; EDW31662.1; -; Genomic_DNA.
DR   RefSeq; XP_002015772.1; XM_002015736.1.
DR   AlphaFoldDB; B4GDK5; -.
DR   SMR; B4GDK5; -.
DR   STRING; 7234.FBpp0175348; -.
DR   EnsemblMetazoa; FBtr0176856; FBpp0175348; FBgn0148850.
DR   GeneID; 6590840; -.
DR   KEGG; dpe:6590840; -.
DR   eggNOG; KOG4356; Eukaryota.
DR   HOGENOM; CLU_012715_0_0_1; -.
DR   OMA; YSIKHSH; -.
DR   PhylomeDB; B4GDK5; -.
DR   Proteomes; UP000008744; 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..846
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365809"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..416
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        372..390
FT                   /note="Basic and acidic residues"
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;  95589 MW;  B1D95263CE3EC8AF 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 EDDADGDMPE TPELETAAPP DPPALTPSTF
     LKDSVHYQLP KFDCNALDNA MAFVLDVAHV QPDSIVTLKT DRSVSVKFAT IGSGYYPTHY
     AFYMELPSVD MEEYHKDHCI ESIEAEAWDN NVIMKLFLGA ESKAPTSYLA GLHANGLKEY
     QVYGHYKAKT DKNNECEPNP PRVVQIMRTD 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