IFT46_MOUSE
ID IFT46_MOUSE Reviewed; 301 AA.
AC Q9DB07; Q91Z06; Q9JHT1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Intraflagellar transport protein 46 homolog;
GN Name=Ift46;
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].
RX PubMed=10873569; DOI=10.1006/bbrc.2000.2910;
RA O'Brien K.P., Tapia-Paez I., Staahle-Baeckdahl M., Kedra D., Dumanski J.P.;
RT "Characterization of five novel human genes in the 11q13-q22 region.";
RL Biochem. Biophys. Res. Commun. 273:90-94(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Wolffian duct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=17720815; DOI=10.1074/jbc.m705730200;
RA Gouttenoire J., Valcourt U., Bougault C., Aubert-Foucher E., Arnaud E.,
RA Giraud L., Mallein-Gerin F.;
RT "Knockdown of the intraflagellar transport protein IFT46 stimulates
RT selective gene expression in mouse chondrocytes and affects early
RT development in zebrafish.";
RL J. Biol. Chem. 282:30960-30973(2007).
RN [5]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17312020; DOI=10.1083/jcb.200608041;
RA Hou Y., Qin H., Follit J.A., Pazour G.J., Rosenbaum J.L., Witman G.B.;
RT "Functional analysis of an individual IFT protein: IFT46 is required for
RT transport of outer dynein arms into flagella.";
RL J. Cell Biol. 176:653-665(2007).
RN [6]
RP INTERACTION WITH DAW1.
RX PubMed=18852297; DOI=10.1083/jcb.200802025;
RA Ahmed N.T., Gao C., Lucker B.F., Cole D.G., Mitchell D.R.;
RT "ODA16 aids axonemal outer row dynein assembly through an interaction with
RT the intraflagellar transport machinery.";
RL J. Cell Biol. 183:313-322(2008).
RN [7]
RP IDENTIFICATION IN THE IFT COMPLEX B, INTERACTION WITH IFT88, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19253336; DOI=10.1002/cm.20346;
RA Follit J.A., Xu F., Keady B.T., Pazour G.J.;
RT "Characterization of mouse IFT complex B.";
RL Cell Motil. Cytoskeleton 66:457-468(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and 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).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21289087; DOI=10.1091/mbc.e10-07-0596;
RA Lai C.K., Gupta N., Wen X., Rangell L., Chih B., Peterson A.S., Bazan J.F.,
RA Li L., Scales S.J.;
RT "Functional characterization of putative cilia genes by high-content
RT analysis.";
RL Mol. Biol. Cell 22:1104-1119(2011).
RN [10]
RP INTERACTION WITH TTC30B.
RX PubMed=23810713; DOI=10.1016/j.yexcr.2013.06.010;
RA Howard P.W., Jue S.F., Maurer R.A.;
RT "Interaction of mouse TTC30/DYF-1 with multiple intraflagellar transport
RT complex B proteins and KIF17.";
RL Exp. Cell Res. 319:2275-2281(2013).
RN [11]
RP INTERACTION WITH TTC26.
RX PubMed=25340710; DOI=10.1371/journal.pgen.1004689;
RA Swiderski R.E., Nakano Y., Mullins R.F., Seo S., Banfi B.;
RT "A mutation in the mouse ttc26 gene leads to impaired hedgehog signaling.";
RL PLoS Genet. 10:E1004689-E1004689(2014).
RN [12]
RP INTERACTION WITH TTC25.
RX PubMed=25860617; DOI=10.1371/journal.pone.0124378;
RA Xu Y., Cao J., Huang S., Feng D., Zhang W., Zhu X., Yan X.;
RT "Characterization of tetratricopeptide repeat-containing proteins critical
RT for cilia formation and function.";
RL PLoS ONE 10:E0124378-E0124378(2015).
CC -!- FUNCTION: Forms part of a complex involved in intraflagellar transport
CC (IFT), the bi-directional movement of particles required for the
CC assembly, maintenance and functioning of primary cilia. May play a role
CC in chondrocyte maturation and skeletogenesis.
CC {ECO:0000269|PubMed:17720815, ECO:0000269|PubMed:21289087}.
CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT80, IFT81, and IFT88. Interacts with IFT57, IFT88 and DAW1.
CC Interacts with ARL13B. Interacts with TTC26/IFT56. Interacts with TTC25
CC (PubMed:25860617). Interacts with TTC30B (PubMed:23810713).
CC {ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297,
CC ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:23810713,
CC ECO:0000269|PubMed:25340710, ECO:0000269|PubMed:25860617}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Cell
CC projection, cilium. Note=Expression is concentrated at the cilium basal
CC body but is also detected along the length of the cilium.
CC -!- TISSUE SPECIFICITY: Strongly expressed in ovary and testis, moderately
CC expressed in kidney and brain, and weakly expressed in thymus, heart,
CC lung, liver, spleen and muscle. Expressed in embryonic bone and
CC cartilage, with high expression in non-hypertrophic chondrocytes and
CC weaker expression in hypertrophic chondrocytes.
CC {ECO:0000269|PubMed:17720815}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 8 dpc throughout embryonic
CC development, with levels increasing at 12.5 dpc and remaining constant
CC thereafter. Up-regulated during chondrocyte maturation and
CC skeletogenesis. {ECO:0000269|PubMed:17720815}.
CC -!- INDUCTION: By BMP2. {ECO:0000269|PubMed:17720815}.
CC -!- DISRUPTION PHENOTYPE: Short cilia. {ECO:0000269|PubMed:21289087}.
CC -!- SIMILARITY: Belongs to the IFT46 family. {ECO:0000305}.
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DR EMBL; AJ249981; CAB96545.1; -; mRNA.
DR EMBL; AK005360; BAB23974.1; -; mRNA.
DR EMBL; AK032880; BAC28067.1; -; mRNA.
DR EMBL; BC010326; AAH10326.1; -; mRNA.
DR EMBL; BC080764; AAH80764.1; -; mRNA.
DR CCDS; CCDS23119.1; -.
DR RefSeq; NP_076320.2; NM_023831.3.
DR RefSeq; XP_006510734.1; XM_006510671.3.
DR AlphaFoldDB; Q9DB07; -.
DR SMR; Q9DB07; -.
DR BioGRID; 218181; 3.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR IntAct; Q9DB07; 1.
DR STRING; 10090.ENSMUSP00000002099; -.
DR iPTMnet; Q9DB07; -.
DR PhosphoSitePlus; Q9DB07; -.
DR CPTAC; non-CPTAC-4041; -.
DR MaxQB; Q9DB07; -.
DR PaxDb; Q9DB07; -.
DR PeptideAtlas; Q9DB07; -.
DR PRIDE; Q9DB07; -.
DR ProteomicsDB; 266957; -.
DR Antibodypedia; 52642; 51 antibodies from 11 providers.
DR DNASU; 76568; -.
DR Ensembl; ENSMUST00000002099; ENSMUSP00000002099; ENSMUSG00000002031.
DR Ensembl; ENSMUST00000118186; ENSMUSP00000113845; ENSMUSG00000002031.
DR Ensembl; ENSMUST00000239014; ENSMUSP00000159011; ENSMUSG00000002031.
DR GeneID; 76568; -.
DR KEGG; mmu:76568; -.
DR UCSC; uc009pek.1; mouse.
DR CTD; 56912; -.
DR MGI; MGI:1923818; Ift46.
DR VEuPathDB; HostDB:ENSMUSG00000002031; -.
DR eggNOG; ENOG502QPNA; Eukaryota.
DR GeneTree; ENSGT00390000005544; -.
DR HOGENOM; CLU_039364_1_0_1; -.
DR InParanoid; Q9DB07; -.
DR OrthoDB; 878878at2759; -.
DR PhylomeDB; Q9DB07; -.
DR TreeFam; TF314221; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 76568; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ift46; mouse.
DR PRO; PR:Q9DB07; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DB07; protein.
DR Bgee; ENSMUSG00000002031; Expressed in spermatocyte and 262 other tissues.
DR ExpressionAtlas; Q9DB07; baseline and differential.
DR Genevisible; Q9DB07; MM.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0097546; C:ciliary base; ISO:MGI.
DR GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0035082; P:axoneme assembly; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0044782; P:cilium organization; ISO:MGI.
DR GO; GO:0060285; P:cilium-dependent cell motility; ISO:MGI.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR InterPro; IPR022088; Intraflagellar_transp_cmplxB.
DR PANTHER; PTHR13376; PTHR13376; 1.
DR Pfam; PF12317; IFT46_B_C; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..301
FT /note="Intraflagellar transport protein 46 homolog"
FT /id="PRO_0000085517"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 213..225
FT /note="PEFEELLGKVSLP -> RNLKSSGKGESA (in Ref. 1; CAB96545)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="L -> R (in Ref. 3; AAH10326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 34054 MW; 3E4CB2B2858A7384 CRC64;
MADNSSDEYE EDNKEKKKPS QLTPQQGFSE NDDDDDDDSS ETDSDDDDDD EEHGAPLEGA
YDPADYEHLP VSAEIKELFE YISRYTPQLI DLDHKLKPFI PDFIPAVGDI DAFLKVPRPD
GKPDHLGLLV LDEPSTKQSD PTVLSLWLTE NSKQHNITQH MKVKSLEDAE KNPKAIDTWI
ESISELHRSK PPATVHYTRP MPDIDTLMQE WSPEFEELLG KVSLPTVEID CSLAEYIDMI
CAILDIPFYK SRIQSLHLLF SLYSEFKNSQ HFKALAEGKK VFTPPPNSAS QAGDAETLTF
I
