KTU_MOUSE
ID KTU_MOUSE Reviewed; 814 AA.
AC Q8BPI1; Q3T9I8; Q3U4G5; Q6P5G9; Q9CZC7;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH DNAI2 AND HSPA1A.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 387-814 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 385-814 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 DNAI2 and HSPA1A (PubMed:19052621). Interacts
CC with CFAP300. Interacts with DNAAF4. Interacts with DNAAF6/PIH1D3 (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_03069,
CC ECO:0000269|PubMed:19052621}.
CC -!- INTERACTION:
CC Q8BPI1; A2AC93: Dnai2; NbExp=2; IntAct=EBI-15744709, EBI-15744757;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BPI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BPI1-2; Sequence=VSP_036538;
CC -!- TISSUE SPECIFICITY: Expressed in nearly all organs of adult, with
CC higher expression in tissues known to have motile cilia and flagella,
CC such as brain and testis. {ECO:0000269|PubMed:19052621}.
CC -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03069}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58344.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB28455.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE32466.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE43032.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB455811; BAG75151.1; -; mRNA.
DR EMBL; BC055807; AAH55807.1; -; mRNA.
DR EMBL; BC058344; AAH58344.1; ALT_INIT; mRNA.
DR EMBL; BC062898; AAH62898.1; -; mRNA.
DR EMBL; AK012767; BAB28455.1; ALT_INIT; mRNA.
DR EMBL; AK075648; BAC35879.1; ALT_INIT; mRNA.
DR EMBL; AK154254; BAE32466.1; ALT_INIT; mRNA.
DR EMBL; AK172494; BAE43032.1; ALT_INIT; mRNA.
DR CCDS; CCDS25948.1; -. [Q8BPI1-1]
DR RefSeq; NP_081545.3; NM_027269.4. [Q8BPI1-1]
DR AlphaFoldDB; Q8BPI1; -.
DR SMR; Q8BPI1; -.
DR BioGRID; 224540; 2.
DR DIP; DIP-59777N; -.
DR IntAct; Q8BPI1; 6.
DR STRING; 10090.ENSMUSP00000021356; -.
DR iPTMnet; Q8BPI1; -.
DR PhosphoSitePlus; Q8BPI1; -.
DR EPD; Q8BPI1; -.
DR MaxQB; Q8BPI1; -.
DR PaxDb; Q8BPI1; -.
DR PRIDE; Q8BPI1; -.
DR ProteomicsDB; 263680; -. [Q8BPI1-1]
DR ProteomicsDB; 263681; -. [Q8BPI1-2]
DR Antibodypedia; 139; 36 antibodies from 13 providers.
DR Ensembl; ENSMUST00000021356; ENSMUSP00000021356; ENSMUSG00000020973. [Q8BPI1-1]
DR GeneID; 109065; -.
DR KEGG; mmu:109065; -.
DR UCSC; uc007nrt.1; mouse. [Q8BPI1-1]
DR CTD; 55172; -.
DR MGI; MGI:1923566; Dnaaf2.
DR VEuPathDB; HostDB:ENSMUSG00000020973; -.
DR eggNOG; KOG4356; Eukaryota.
DR GeneTree; ENSGT00510000048466; -.
DR HOGENOM; CLU_018349_0_0_1; -.
DR InParanoid; Q8BPI1; -.
DR OMA; KQCMSLT; -.
DR OrthoDB; 943252at2759; -.
DR PhylomeDB; Q8BPI1; -.
DR TreeFam; TF336215; -.
DR BioGRID-ORCS; 109065; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Dnaaf2; mouse.
DR PRO; PR:Q8BPI1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BPI1; protein.
DR Bgee; ENSMUSG00000020973; Expressed in cerebral cortex ventricular layer and 86 other tissues.
DR Genevisible; Q8BPI1; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0061966; P:establishment of left/right asymmetry; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0036159; P:inner dynein arm assembly; IMP:MGI.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
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 Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..814
FT /note="Protein kintoun"
FT /id="PRO_0000089912"
FT REGION 234..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVR5"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVR5"
FT VAR_SEQ 400..437
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036538"
FT CONFLICT 463
FT /note="L -> Q (in Ref. 3; BAB28455)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="S -> T (in Ref. 3; BAE32466)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="V -> E (in Ref. 3; BAB28455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 88327 MW; 62F63A64B3BE73E3 CRC64;
MAKAAASSAL EDLDLSREEV QRFTSAFQDP EFRRMFSEYA AEITDPENRR RYEEEITALE
RERGVDVRFV HPEPGHVLRT SLDGEHRCYV NVCSNSLVGV PSSRPGPGRG GTAAGSHWSL
PYSLAPGRQY AGRNGARYTV YDVVFHPEAL ALARSHERFR EMLDATALEA VEQQFGVRLD
RRNAKTLKIK YKGMPEAAVL RTPLPGGVPA QPEGEPPGLF PDPPYPYRYP AAAAANTARS
PASPAPEAVQ RPEPTEPRCS VVQRHHVDLQ DYRCSRDAAP STVPHELVVT IELPLLRSVE
RAELEVKGKL LCLDSRNPDY RLRLSLPYPV DDGRGKAQYN KARRQLVVTL PVALADARQE
PPAATPEEPA EETGTDDVAR TSAGDFAAAR EESADGTGAD HGEKSGVGAP DPGAAHAEGE
LVPEPEQDFG GDSVAPLDLG KGTSPGDRSL PYSAFPGGDT ESLCGDPGVQ TNEEQERTRH
DTAGSAMGDP GTESIAPVCP PLQCNQDEDS LTLLIQVPGI LPQTLHGHLS PVGYELCFST
QDSGYSCTLQ FAPENKLSTR EPETSVSLNN AVIVLAKSPE SHGLWREWYC GLNKESLEER
LFINEENVNG FLEEVLCSPL KQARSLAPPL IEVLQATDEQ VQIHAELQEC SDPAGLQGKG
KGVREGCPLS EAEAADQSAT SPAASDSAAA VEALKINTHG SAVDLQHGCP EVPHVLSGKP
LQPEAKMDPE FIRESSTTYS TEEKENIREP VISKGEKING DHPSSLLNKT VVQNIPDFDT
IKETNMQDGS VQIIRDHTTH CAFSFQNPLL YDLD
