KTU_ORYLA
ID KTU_ORYLA Reviewed; 588 AA.
AC B6F1W5;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 45.
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};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19052621; DOI=10.1038/nature07471;
RA Omran H., Kobayashi D., Olbrich H., Tsukahara T., Loges N.T., Hagiwara H.,
RA Zhang Q., Leblond G., O'Toole E., Hara C., Mizuno H., Kawano H.,
RA Fliegauf M., Yagi T., Koshida S., Miyawaki A., Zentgraf H., Seithe H.,
RA Reinhardt R., Watanabe Y., Kamiya R., Mitchell D.R., Takeda H.;
RT "Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal dyneins.";
RL Nature 456:611-616(2008).
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, ECO:0000269|PubMed:19052621}.
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 -!- DISRUPTION PHENOTYPE: Organ laterality defects due to altered ciliary
CC motility. Typical randomized left-right mutant leading to situs
CC inversus. Fishes lack directional liquid flow in Kupffer's vesicle (an
CC organ functionally equivalent to the mouse node in terms of left-right
CC specification). Although the number and length of cilia in Kupffer's
CC vesicle seem normal, their motility is completely lost. Homozygous fish
CC are viable but develop primary ciliary dyskinesia. Furthermore, male
CC mutant fish have impaired sperm motility leading to reduced fertility.
CC Ultrastructurally, affected cilia and flagella show partial or complete
CC loss of outer and inner dynein arms. This loss of dynein arms is more
CC severe in Kupffer's vesicle cilia than in sperm flagella.
CC {ECO:0000269|PubMed:19052621}.
CC -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03069}.
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DR EMBL; AB455535; BAG75150.1; -; mRNA.
DR RefSeq; NP_001131059.1; NM_001137587.1.
DR AlphaFoldDB; B6F1W5; -.
DR SMR; B6F1W5; -.
DR PRIDE; B6F1W5; -.
DR GeneID; 100192402; -.
DR KEGG; ola:100192402; -.
DR CTD; 55172; -.
DR InParanoid; B6F1W5; -.
DR OrthoDB; 943252at2759; -.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IDA: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:UniProtKB.
DR GO; GO:0060285; P:cilium-dependent cell motility; IMP:UniProtKB.
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..588
FT /note="Protein kintoun"
FT /id="PRO_0000365799"
FT REGION 199..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 66584 MW; 0A9CB6FE51C2019A CRC64;
MEVGKKLELS ITADEVEVLS KAIKNEKFQE MLSNYFQEIS SPENVKTYQE EVTLLEQKRG
NSIEFIHPSP FRALETSVDG KQRCFINICA CDKVGKPESK TVRTVQRFGE KWSLPHLLQP
GRQNCERKGN ISTIYDVCFH PETLHLADKS EKFMDMVKEV AIQGIQKAFK VLLDKSNLKE
MDIKYKGVPQ SCVIRKPIPG YEAKEPPEER DLSPSTSHLP ENSIDVPSKL LQKQPEEPIK
PIYAIKYRSV IDLQDFRVSR ESARSLRPKE IVITIDLPLL PTVHGMVLEV EEKRLLLESE
NPSYRLELHL SYPVDENNGK AKFNKHQRQL TVTLPVQPPL EAPQLPGGSP NPTSDPQNEN
QTRVEERVEE MAEKGGEQHQ RGNDNGAAQG RRQVLEDQNG EKEGKKIQKR NERPEHEVKN
ETLRKKHDEK FELQDVQQEN KGNCSNTKEV KCCRRTKDSL DSLIPTTAAS PDGQKKHILT
QETEKPKGSV EIPTSSQEYL KVPVTSAATA ANVNASDETS KRKPTEEQLE DADEDVLPAE
QRFQEPEEIN VPAAGTLRQN NAAGNEKIND PHTSAGFVLQ NKLMYELD
