IFT88_MOUSE
ID IFT88_MOUSE Reviewed; 824 AA.
AC Q61371; E9QKU0; Q3UXY9; Q921J5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Intraflagellar transport protein 88 homolog;
DE AltName: Full=Recessive polycystic kidney disease protein Tg737;
DE AltName: Full=Tetratricopeptide repeat protein 10;
DE Short=TPR repeat protein 10;
DE AltName: Full=TgN(Imorpk)737Rpw;
GN Name=Ift88; Synonyms=Tg737, Tg737Rpw, TgN737Rpw, Ttc10;
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], AND INVOLVEMENT IN PKD.
RC STRAIN=C3HF/RL;
RX PubMed=8191288; DOI=10.1126/science.8191288;
RA Moyer J.H., Lee-Tischler M.J., Kwon H.-Y., Schrick J.J., Avner E.D.,
RA Sweeney W.E., Godfrey V.L., Cacheiro N.L., Wilkinson J.E., Woychik R.P.;
RT "Candidate gene associated with a mutation causing recessive polycystic
RT kidney disease in mice.";
RL Science 264:1329-1333(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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 [5]
RP FUNCTION, AND INTERACTION WITH IFT57 AND IFT172.
RX PubMed=11062270; DOI=10.1083/jcb.151.3.709;
RA Pazour G.J., Dickert B.L., Vucica Y., Seeley E.S., Rosenbaum J.L.,
RA Witman G.B., Cole D.G.;
RT "Chlamydomonas IFT88 and its mouse homologue, polycystic kidney disease
RT gene tg737, are required for assembly of cilia and flagella.";
RL J. Cell Biol. 151:709-718(2000).
RN [6]
RP INTERACTION WITH IFT46.
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 [7]
RP IDENTIFICATION IN THE IFT COMPLEX B, INTERACTION WITH IFT20; IFT22; HSPB11;
RP IFT27; IFT46; IFT52; TRAF3IP1; IFT57; IFT74; IFT80 AND IFT81, 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 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).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=20230748; DOI=10.1016/j.devcel.2009.12.022;
RA Singla V., Romaguera-Ros M., Garcia-Verdugo J.M., Reiter J.F.;
RT "Ofd1, a human disease gene, regulates the length and distal structure of
RT centrioles.";
RL Dev. Cell 18:410-424(2010).
RN [10]
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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=23386061; DOI=10.1038/emboj.2013.3;
RA Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
RA Reiter J.F.;
RT "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole
RT subdistal appendages.";
RL EMBO J. 32:597-607(2013).
RN [12]
RP IDENTIFICATION IN THE IFT COMPLEX B, AND INTERACTION WITH IFT57 AND 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 [13]
RP INTERACTION WITH DZIP1.
RX PubMed=23955340; DOI=10.1074/jbc.m113.492066;
RA Wang C., Low W.C., Liu A., Wang B.;
RT "Centrosomal protein DZIP1 regulates Hedgehog signaling by promoting
RT cytoplasmic retention of transcription factor GLI3 and affecting
RT ciliogenesis.";
RL J. Biol. Chem. 288:29518-29529(2013).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=24089209; DOI=10.1038/nature12639;
RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I.,
RA Codogno P., Satir B.H., Satir P., Cuervo A.M.;
RT "Functional interaction between autophagy and ciliogenesis.";
RL Nature 502:194-200(2013).
RN [15]
RP INTERACTION WITH C2CD3.
RX PubMed=24469809; DOI=10.1073/pnas.1318737111;
RA Ye X., Zeng H., Ning G., Reiter J.F., Liu A.;
RT "C2cd3 is critical for centriolar distal appendage assembly and ciliary
RT vesicle docking in mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2164-2169(2014).
RN [16]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27682589; DOI=10.1091/mbc.e16-05-0318;
RA Zhang Z., Li W., Zhang Y., Zhang L., Teves M.E., Liu H., Strauss J.F. III,
RA Pazour G.J., Foster J.A., Hess R.A., Zhang Z.;
RT "Intraflagellar transport protein IFT20 is essential for male fertility and
RT spermiogenesis in mice.";
RL Mol. Biol. Cell 0:0-0(2016).
RN [17]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=31761534; DOI=10.1016/j.cell.2019.11.005;
RA Hilgendorf K.I., Johnson C.T., Mezger A., Rice S.L., Norris A.M.,
RA Demeter J., Greenleaf W.J., Reiter J.F., Kopinke D., Jackson P.K.;
RT "Omega-3 Fatty Acids Activate Ciliary FFAR4 to Control Adipogenesis.";
RL Cell 179:1289-1305(2019).
CC -!- FUNCTION: Involved in primary cilium biogenesis (PubMed:31761534,
CC PubMed:11062270, PubMed:21289087). Also involved in autophagy since it
CC is required for trafficking of ATG16L and the expansion of the
CC autophagic compartment. {ECO:0000269|PubMed:11062270,
CC ECO:0000269|PubMed:21289087, ECO:0000269|PubMed:31761534}.
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 (PubMed:19253336, PubMed:23810713). Interacts
CC with IFT20, IFT22, HSPB11, IFT27, IFT52, TRAF3IP1, IFT74, IFT80 and
CC IFT81 (PubMed:19253336). Interacts with IFT172 (PubMed:11062270).
CC Interacts with IFT57 (PubMed:11062270, PubMed:19253336,
CC PubMed:23810713). Interacts with IFT46 (PubMed:19253336,
CC PubMed:17312020). Interacts with TTC30B (PubMed:23810713). Interacts
CC with C2CD3 (PubMed:24469809). Interacts with ENTR1 (via N-terminus) (By
CC similarity). Interacts with LRRC56 (By similarity). Interacts with
CC DZIP1 (PubMed:23955340). {ECO:0000250|UniProtKB:Q13099,
CC ECO:0000269|PubMed:11062270, ECO:0000269|PubMed:17312020,
CC ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:23810713,
CC ECO:0000269|PubMed:23955340, ECO:0000269|PubMed:24469809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:20230748,
CC ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:20230748}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q13099}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q13099}. Cytoplasm
CC {ECO:0000269|PubMed:27682589}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:27682589}. Note=Colocalizes with ENTR1 and gamma-
CC tubulin at the basal body of primary cilia. Colocalizes with ENTR1 and
CC pericentrin at the centrosome. {ECO:0000250|UniProtKB:Q13099}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:27682589}.
CC -!- DISEASE: Note=Defects in Ift88 are the cause of recessive bilateral
CC polycystic kidney disease (PKD) with collecting duct and tubule
CC ectasia, and a liver lesion involving biliary dysplasia and/or portal
CC fibrosis.
CC -!- DISRUPTION PHENOTYPE: Cilia absent or reduced, virtually no cilia of
CC the normal 5 uM mean length (PubMed:21289087). Conditional knockdown in
CC preadipocytes results in loss of cilia. Mutant mice show a significant
CC reduction of gonadal white adipose tissue and total fat mass associated
CC with reduced serum LEP levels (PubMed:31761534).
CC {ECO:0000269|PubMed:21289087, ECO:0000269|PubMed:31761534}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22424.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L31959; AAB59705.1; -; mRNA.
DR EMBL; AK135110; BAE22424.1; ALT_INIT; mRNA.
DR EMBL; AC124462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012250; AAH12250.1; -; mRNA.
DR PIR; I49564; I49564.
DR RefSeq; NP_033402.2; NM_009376.2.
DR AlphaFoldDB; Q61371; -.
DR SMR; Q61371; -.
DR BioGRID; 204171; 14.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR STRING; 10090.ENSMUSP00000113768; -.
DR iPTMnet; Q61371; -.
DR PhosphoSitePlus; Q61371; -.
DR MaxQB; Q61371; -.
DR PaxDb; Q61371; -.
DR PRIDE; Q61371; -.
DR ProteomicsDB; 267289; -.
DR DNASU; 21821; -.
DR GeneID; 21821; -.
DR KEGG; mmu:21821; -.
DR CTD; 8100; -.
DR MGI; MGI:98715; Ift88.
DR eggNOG; KOG2003; Eukaryota.
DR InParanoid; Q61371; -.
DR OMA; RIKIMHN; -.
DR OrthoDB; 259837at2759; -.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR BioGRID-ORCS; 21821; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ift88; mouse.
DR PRO; PR:Q61371; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61371; protein.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR GO; GO:0097541; C:axonemal basal plate; IDA:MGI.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0097542; C:ciliary tip; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0060091; C:kinocilium; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR GO; GO:0002081; C:outer acrosomal membrane; ISO:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; IPI:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IGI:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR GO; GO:0036334; P:epidermal stem cell homeostasis; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0001654; P:eye development; IGI:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0048853; P:forebrain morphogenesis; IMP:MGI.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0060914; P:heart formation; IMP:MGI.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0060173; P:limb development; IGI:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0060426; P:lung vasculature development; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR GO; GO:0031016; P:pancreas development; IMP:MGI.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:1903929; P:primary palate development; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0060259; P:regulation of feeding behavior; IMP:MGI.
DR GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0070613; P:regulation of protein processing; IMP:MGI.
DR GO; GO:0034405; P:response to fluid shear stress; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR GO; GO:0007290; P:spermatid nucleus elongation; IMP:MGI.
DR GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IMP:MGI.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Flagellum; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..824
FT /note="Intraflagellar transport protein 88 homolog"
FT /id="PRO_0000106392"
FT REPEAT 196..229
FT /note="TPR 1"
FT REPEAT 232..265
FT /note="TPR 2"
FT REPEAT 271..304
FT /note="TPR 3"
FT REPEAT 415..448
FT /note="TPR 4"
FT REPEAT 450..483
FT /note="TPR 5"
FT REPEAT 484..517
FT /note="TPR 6"
FT REPEAT 518..551
FT /note="TPR 7"
FT REPEAT 552..585
FT /note="TPR 8"
FT REPEAT 586..619
FT /note="TPR 9"
FT REPEAT 620..653
FT /note="TPR 10"
FT REPEAT 654..687
FT /note="TPR 11"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 64
FT /note="I -> T (in Ref. 4; AAH12250)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="Y -> H (in Ref. 4; AAH12250)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="L -> M (in Ref. 2; BAE22424)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="D -> E (in Ref. 4; AAH12250)"
FT /evidence="ECO:0000305"
FT CONFLICT 823
FT /note="P -> S (in Ref. 1; AAB59705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 824 AA; 92994 MW; BC239BA4B8FE3B5D CRC64;
MENVHLAPET DEDDLYSGFN DYNPAYDTEE LENDTGFQQA VRTSHGRRPP VTAKIPSTAV
SRPIATGYGS KTSLTSSMGR PMTGTIQDGV ARPMTAVRAA GFSKAALRGS AFDPLGQSRG
PAPPLEAKNE DSPEEKIRQL EKKVNELVEE SCIANSCGDL KLALEKAKDA GRKERVLVRQ
REQVTSPENI NLDLTYSVLF NLASQYSANE MYAEALNTYQ VIVKNKMFSN AGRLKVNMGN
IYLKQRNYSK AIKFYRMALD QIPSVHKEMR IKIMQNIGIT FIKTGQYSDA INSFEHIMSM
APSLKAGFNL ILSCFAIGDR EKMKKAFQKL IAVPLEIDED DKYISPSDDP HTNLLIEAIK
NDHLRQMERE RKAMAEKYIM TAAKLIAPVI EASFAVGYNW CVEVVKASQY VELANDLEIN
KAITYLRQKD FNQAVDTLKM FEKKDSRVKS AAATNLSFLY YLENEFAQAS SYADLAVNSD
RYNPSALTNK GNTVFANGDY EKAAEFYKEA LRNDSSCTEA LYNIGLTYKK LNRLDEALDS
FLKLHAILRN SAQVLCQIAN IYELMEDPNQ AIEWLMQLIS VVPTDSQALS KLGELYDSEG
DKSQAFQYYY ESYRYFPSNI EVIEWLGAYY IDTQFCEKAI QYFERASLIQ PTQVKWQLMV
ASCFRRSGNY QKALDTYKEI HRKFPENVEC LRFLVRLCTD IGLKEVQEYA TKLKRLEKMK
EMREQRIKSG RDSSGGSRSK REGSAGSDSG QNNSASSKSE RLSAKLRALP GTDEPYESSG
NKEIDASYVD PLGPQIERPK TAAKKRIDED DFADEELGDD LLPE
