ID   KTU_DANRE               Reviewed;         566 AA.
AC   Q499A3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Protein kintoun {ECO:0000255|HAMAP-Rule:MF_03069};
DE   AltName: Full=Dynein assembly factor 2, axonemal {ECO:0000255|HAMAP-Rule:MF_03069};
GN   Name=dnaaf2 {ECO:0000255|HAMAP-Rule:MF_03069};
GN   Synonyms=ktu {ECO:0000255|HAMAP-Rule:MF_03069}; ORFNames=zgc:110294;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069}.
CC       Dynein axonemal particle {ECO:0000250|UniProtKB:B1H1W9}. Note=Localizes
CC       in the apical cytoplasm around the gamma-tubulin-positive
CC       pericentriolar region, not in the cilia. {ECO:0000255|HAMAP-
CC       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; BC100006; AAI00007.1; -; mRNA.
DR   RefSeq; NP_001028272.1; NM_001033100.1.
DR   AlphaFoldDB; Q499A3; -.
DR   SMR; Q499A3; -.
DR   STRING; 7955.ENSDARP00000060295; -.
DR   PaxDb; Q499A3; -.
DR   PRIDE; Q499A3; -.
DR   GeneID; 606664; -.
DR   KEGG; dre:606664; -.
DR   CTD; 55172; -.
DR   ZFIN; ZDB-GENE-050809-128; dnaaf2.
DR   eggNOG; KOG4356; Eukaryota.
DR   InParanoid; Q499A3; -.
DR   OrthoDB; 943252at2759; -.
DR   PhylomeDB; Q499A3; -.
DR   PRO; PR:Q499A3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; IMP:ZFIN.
DR   GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central.
DR   GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..566
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365798"
FT   REGION          183..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..293
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  62676 MW;  AA50CF1A27A262FB CRC64;
     MDADRLAELQ LTRAEMRRIG EALQDRRFRE LLTEYVEEIS SPENRRRYEE EIRRLEEERG
     AAVQFIHPTP HHVLKGRGPS GKCFINICSD QLIEKPRSEA ATDDRGRSGH SWRIPYSLTP
     GRAGRDAAGA PCVLFDAVFH PDALLMAENN ARFMTLIHRT ATGGIQDNFR IRLEHVTRLK
     MMKYKGEPQP TMIRRPNPGQ TEAADRGPQQ TTGPQQPTGP QQPTDPQQPT DTQQPTDPQQ
     TTGPQQTTGP QQTTGPHQPT DPQQTTGPQQ PTDPQQPTGP HQPTDPQQTT DPPPTAPQYR
     LKYRSVLDLQ DYRCCRDSGS AGRPTAIIIE VEVPRLRSAQ EAELRVEERR LLLEAPTAEY
     RLELPLAYPV EEERAEAQFN HTHRLLTVTL PVLKRRRVEE EERRAEEEES RKGGDEDGEL
     HPDCGPDPPM MELQTEDTHT PAADTHTPAA DTHTPAADTH TPAAETGAGL GSGVALLSSS
     NVISVCGADV HQQLEEPGDP SAHTDPADTH PADTDPADTD PAHTDPADTD PADTDPAHTD
     PAHTDPEMES RIAGLHLQNT LCFQLD