KTU_BOVIN
ID KTU_BOVIN Reviewed; 829 AA.
AC Q0VC73;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 408-422.
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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 -!- 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=AAI20320.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AAFC03057991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03057994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120319; AAI20320.1; ALT_INIT; mRNA.
DR RefSeq; NP_001069492.2; NM_001076024.3.
DR AlphaFoldDB; Q0VC73; -.
DR SMR; Q0VC73; -.
DR STRING; 9913.ENSBTAP00000042390; -.
DR PaxDb; Q0VC73; -.
DR PRIDE; Q0VC73; -.
DR Ensembl; ENSBTAT00000044951; ENSBTAP00000042390; ENSBTAG00000004930.
DR GeneID; 534465; -.
DR KEGG; bta:534465; -.
DR CTD; 55172; -.
DR VEuPathDB; HostDB:ENSBTAG00000004930; -.
DR VGNC; VGNC:28119; DNAAF2.
DR eggNOG; KOG4356; Eukaryota.
DR GeneTree; ENSGT00510000048466; -.
DR HOGENOM; CLU_018349_0_0_1; -.
DR InParanoid; Q0VC73; -.
DR OMA; KQCMSLT; -.
DR OrthoDB; 943252at2759; -.
DR TreeFam; TF336215; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000004930; Expressed in thymus and 105 other tissues.
DR GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IBA:GO_Central.
DR GO; GO:0061966; P:establishment of left/right asymmetry; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0036159; P:inner dynein arm assembly; IEA:Ensembl.
DR GO; GO:0036158; P:outer dynein arm assembly; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..829
FT /note="Protein kintoun"
FT /id="PRO_0000283065"
FT REGION 197..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVR5"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVR5"
SQ SEQUENCE 829 AA; 90970 MW; 625CBCF2361402D0 CRC64;
MAKEAASSPL EDLDLSGEEV QRLTSAFQDP EFRRMFSEYA EELTDPENRR RYEEEITALE
RERGVEVRFV HPEPGHVLRT SLDGTRRCFV NVCSNALVGA PSSQPGSGSA VSGRQWSLPY
SLAPGREYAW GRGTRYTVYD VVFHPDAIAL ARRHERFRQM LDATALEAVE KQFGVKLDRR
NAKTLKIKYK GTPDAAVLRT PLPGGAPARP EGEPESPFPD FPYPYRYPAA GASAAVPRPQ
APSPPEAVRQ PAPTEPRYSV VQRHHVDLQD YRCSRDSAPG TVPQELVVTI ELPLLRSAEQ
AALEVTGKLL CLDSRKPDYR LRLSLPYPVD DSRGKAQFNK ARRQLVVTLP VAPTASRPEP
AASPEEAADP PGTDGAACAS ACRGEAGPAG VCAGDAISGP SRTRAADAGI TTPDAPGKER
VAKSEERDFG GQEISTTGTR EEPPSGAGNS PGDRGGGALS TSWGDLDAGL SVGSASVRPT
LGVEARETRE GTGREPAYRA MGGPGTDRGE ALCPPLQCSQ DEESLTLLVQ VPWILLQSLQ
GEVNPLWYKL SFSTQDLVYY SFFLQFTPEN KLSTKEPEVS ISSNNAVINL AKSPECHGYW
REWYYGLNNY CLEERLFVNE DNVNEFLEEV LSPPFKQTLP LTPPLIEVLQ VTDSKIEIHA
KLQECSNSEQ LHEKEERVHE GSPLTEKENT EHATISTTDS ASSVAVTVLE ADRCGSATCL
QQGALDVSQK LFAESQQPKS EKEREFIKDK SAVYANERKD NLKEPVITEE KELDGNHPSS
LLNKTAVRDT PGFDHIKETN MQDGSVQIIK DHVTHCSFSF QNNLLYDLD
