KTU_RAT
ID KTU_RAT Reviewed; 817 AA.
AC Q5FVL7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 101.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-817.
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 CFAP300. Interacts with DNAI2 and HSPA1A.
CC Interacts with DNAAF4. Interacts with DNAAF6/PIH1D3.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH89901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDM03505.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH473947; EDM03505.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC089901; AAH89901.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014219.3; NM_001014197.3.
DR AlphaFoldDB; Q5FVL7; -.
DR SMR; Q5FVL7; -.
DR STRING; 10116.ENSRNOP00000055960; -.
DR iPTMnet; Q5FVL7; -.
DR PhosphoSitePlus; Q5FVL7; -.
DR PaxDb; Q5FVL7; -.
DR PRIDE; Q5FVL7; -.
DR GeneID; 362746; -.
DR KEGG; rno:362746; -.
DR UCSC; RGD:1310311; rat.
DR CTD; 55172; -.
DR RGD; 1310311; Dnaaf2.
DR eggNOG; KOG4356; Eukaryota.
DR InParanoid; Q5FVL7; -.
DR OrthoDB; 943252at2759; -.
DR PhylomeDB; Q5FVL7; -.
DR PRO; PR:Q5FVL7; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 6.
DR GO; GO:0101031; C:chaperone complex; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0060285; P:cilium-dependent cell motility; ISO:RGD.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISO:RGD.
DR GO; GO:0061966; P:establishment of left/right asymmetry; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0036159; P:inner dynein arm assembly; ISO:RGD.
DR GO; GO:0036158; P:outer dynein arm assembly; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; ISO:RGD.
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 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..817
FT /note="Protein kintoun"
FT /id="PRO_0000365797"
FT REGION 233..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVR5"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 817 AA; 89349 MW; 77CE3AA53295437A CRC64;
MAKTAASSAL EDLDLSGEEV QRLTSAFQDP EFRRMFSDYA AEITDPENRR RYEEEITALE
RERGVEVRFV HPEPGHVLRT SLDGEHRCFV NVCSNSLVGA PSSRPGPGRG GTAAGSHWSL
PYSLAPGRQY AGRNGNRYTV YDVVFHPEAL ALARSHERFR EMLDATALEA VEQQFGVRLD
RRNAKTLKIK YKGTPEAAVL RTPLPEGVRA QPEGELPGLL PYPPYPYHYP AAAESTARSP
ASPAPKAVQR PEPTEPRCSV VQRHHVDLQD YRCSRDAAPS TVPHELVVTI ELPLLRSAER
AELEVKGKLL CLDSRNPDYR LRLSLPYPVD DGRGRAQYNK ARRQLVVTLP VALAVARQDF
STTPEGPTAE TGTDNIACTS AGDLAGAREE SADSSGADHG RKSCVVAPDA GTAKAEGELV
PEPEQDFGGD SVTPLGPGEG TTPENRSLLY SAFQSGDAES LAERSGVYGD LSVQTSEEQE
GTCHDTSGSD MGGPGTESIK PLCPPLQCNQ DEDSLTLLIQ VPGIQPQSLH GDLSPFSYEL
CFSTQDSGYS FTLQFAPENK LSTKEPAISI SLNNAVIVLA KSPESHGLWR EWYWGLNKDS
LEERLFIDEE NVNEFLEEVV RSPLKPARSL SPPLIEVLQV TEEQIQIHAK LQECSDPDGL
QGKEKGVKEE CPLSEKENTE HSTTSTADSN SSVAVEGLKI NTCGAVGLQQ GCPDVPHVLS
GKRLQSEAKM DPEFIRESST AYSAEEKENI KEPVITKEKK IGGDHLSSLP NKTAVQNTHD
FDTIKETNMQ DGSVQIIKDH TTHCAFDFQN SLLYDLD
