ID   KTU_XENLA               Reviewed;         788 AA.
AC   B1H1W9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 48.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30561330; DOI=10.7554/elife.38497;
RA   Huizar R.L., Lee C., Boulgakov A.A., Horani A., Tu F., Marcotte E.M.,
RA   Brody S.L., Wallingford J.B.;
RT   "A liquid-like organelle at the root of motile ciliopathy.";
RL   Elife 7:0-0(2018).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=33263282; DOI=10.7554/elife.58662;
RA   Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L.,
RA   Marcotte E.M., Wallingford J.B.;
RT   "Functional partitioning of a liquid-like organelle during assembly of
RT   axonemal dyneins.";
RL   Elife 9:0-0(2020).
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:0000269|PubMed:30561330,
CC       ECO:0000269|PubMed:33263282}. Note=Localizes in the apical cytoplasm
CC       around the gamma-tubulin-positive pericentriolar region, not in the
CC       cilia. {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; BC160766; AAI60766.1; -; mRNA.
DR   RefSeq; NP_001121243.1; NM_001127771.1.
DR   AlphaFoldDB; B1H1W9; -.
DR   SMR; B1H1W9; -.
DR   MaxQB; B1H1W9; -.
DR   GeneID; 100158322; -.
DR   KEGG; xla:100158322; -.
DR   CTD; 100158322; -.
DR   Xenbase; XB-GENE-5887592; dnaaf2.L.
DR   OrthoDB; 943252at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 100158322; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0120293; C:dynein axonemal particle; IDA:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..788
FT                   /note="Protein kintoun"
FT                   /id="PRO_0000365800"
FT   REGION          194..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  88590 MW;  84F731E1D3636E65 CRC64;
     MAEKLQNLEL SSEELDRFTK AFQDPKFREM FVQYAEEIRD PENRRKYEQE ISQMESERGM
     DIKFIHPKPG YVLLTSVNGV QKCYLNICSN DLLQKPECKP GKDGEGKAGL HWSLPYSLSA
     GREDLGKDGS KHVIYDVVFH PDTLHIASKN EKFKMIVDST SLEAVASQFD VKLDKANVRT
     LSMKYKGVPN PSVLRKPLLG TTPKHGDPED PLSFPYPYDV PTAVGKEKKD QKRVIKEEHK
     QHVTTSEQDP DIQIATTPNY TVRHRSYVDL QDFRDSRDST PSPVPKELVI TVDLPLLNSA
     ESVNLHIAGK NLSLESEKPA YKLNVKLPYV VEDNQGKAQF NKARRQLIIT VPVIQHNILT
     LMQDHFEEAR GEKDLRGAES SVLHEEYTDN GSRTSACGTE NKLEPLISCL NEEENNSEGL
     TSESNLDTGA PYLPEISPNQ NTLDREEVVY GLTEDVPSMP SDTLVCPTFS CSQDPTSLTL
     IAHVRDIDEN SISTDVGSNH YHIRCSVKQS TSSYDLLVTF LPHDIINPNE VYVNISENNA
     LIGLTKSPES VGFWKMLYFG VSGQPLQERR FVSEDNINEV LACSIPLSQV SPSTQEHQPL
     IEVLEMTDER THIRINKPKT ECVVSAEHKE HCTDHSEHER DVGVERSNIA VGDTTEHYSN
     QVSPCRENTE LDRDHTSERY EEPESTSCTG ESTSDQQQKD SNLVFPGDSS AENKMACLKS
     SEQTTQESDL AEDDMPDRSD HTQNFDSRPA SSSVLKEIGK KDGSVQVISD HTTQCPFQFQ
     NSLLFDLD