KTU_DROGR
ID KTU_DROGR Reviewed; 893 AA.
AC B4J4Y2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 56.
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=GH21580;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916367; EDW01688.1; -; Genomic_DNA.
DR RefSeq; XP_001986821.1; XM_001986785.1.
DR AlphaFoldDB; B4J4Y2; -.
DR SMR; B4J4Y2; -.
DR STRING; 7222.FBpp0155486; -.
DR EnsemblMetazoa; FBtr0156994; FBpp0155486; FBgn0129041.
DR EnsemblMetazoa; FBtr0463518; FBpp0413840; FBgn0129041.
DR GeneID; 6559093; -.
DR KEGG; dgr:6559093; -.
DR eggNOG; KOG4356; Eukaryota.
DR HOGENOM; CLU_012715_0_0_1; -.
DR InParanoid; B4J4Y2; -.
DR OMA; YSIKHSH; -.
DR OrthoDB; 943252at2759; -.
DR PhylomeDB; B4J4Y2; -.
DR Proteomes; UP000001070; 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..893
FT /note="Protein kintoun"
FT /id="PRO_0000365806"
FT REGION 211..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0E9G3"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0E9G3"
SQ SEQUENCE 893 AA; 101747 MW; 803287D7960C8D7C CRC64;
MSATSTRNKH SKIHGNEKVD ITKDEFARMR LALQDEEFRK LFFDYVDEIQ DPENRKIYEQ
EITQLEKERG VDVTFIHPKP GFVVKTAIDG ELKCFINICG SQIVERPNNE VAINSETGER
GLTWSIPMAQ APARDDIDAN KKLCKVFDVV FHPDALHLGT RNSQFRKCLI DTALDGVERE
FNVNLDRANL KYPKLDYKGE PHATVIRKLS KNATAEEREP HPLEHTYPKK PEANAGKPKV
LPMKKNVTST PTFAVPKYSI KHSHDIDMAQ YTDELDAKLQ VTIPRALIVE IELPLLSSTA
DCQLDVTEKS VYLLSERSGA KYRLKLDLPY TVDDKSGNAR FDTEHRRLCI TLPVVRSSAR
EQRQMHDNVR ILSREDSGVE LNSNSESPAE DEEAGSEAIV ELTTMQQTQT DNFDAFPPRQ
SFLKRDLHYQ MVANFDCNIV ENVMAFLLHV PNVQPDSMRT VIREGRSVHL QFASMGSGYY
PTNYAFLVQL PDAADPQLHI DHVEPDASDD NVVLRLFMSE SCMTLPSYLA GPDATDLTEY
ACFPPCKTNI EDENCDLELD KPLRISTYHN ELNKSIEVTI IPQDISEQVH QEQQQEEEEE
EEQHEQQQHQ HKKGNKKQRK RNKKQRSLSE SAFEDLKAEQ QQQHQKQQQQ QEKLPENSSP
ESLNAGSSEP VATLKLPQRK QRSFSECNDS SSVQRGILKR FSRYGPRPSI SESSSSIDDC
SSSYSCSVDA AGIGFSHSFG GIPEERVIAD AELSESCKKT VRFNDHIMKK MFRLDSSILG
QRKKNQKRRD CKLRAQQRRV SEGDSVDYEE VEHASNGQQT ANKTAANAQY FKQPQNNNNR
SYSKNNKNQS LHDSGLDLTN NNNHNNEEDT KRNEADAKNA MIFEMDDDDD EDM
