IFT20_MOUSE
ID IFT20_MOUSE Reviewed; 132 AA.
AC Q61025; Q5SYG9; Q99M35;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Intraflagellar transport protein 20 homolog;
DE Short=mIFT20;
GN Name=Ift20;
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), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11916979; DOI=10.1083/jcb.200107108;
RA Pazour G.J., Baker S.A., Deane J.A., Cole D.G., Dickert B.L.,
RA Rosenbaum J.L., Witman G.B., Besharse J.C.;
RT "The intraflagellar transport protein, IFT88, is essential for vertebrate
RT photoreceptor assembly and maintenance.";
RL J. Cell Biol. 157:103-113(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=CD-1; TISSUE=Uterus;
RA Das N., Dey S.K.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Kidney;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [6]
RP TISSUE SPECIFICITY, SUBUNIT, INTERACTION WITH IFT57 AND KIF3B, AND REGION.
RX PubMed=12821668; DOI=10.1074/jbc.m300156200;
RA Baker S.A., Freeman K., Luby-Phelps K., Pazour G.J., Besharse J.C.;
RT "IFT20 links kinesin II with a mammalian intraflagellar transport complex
RT that is conserved in motile flagella and sensory cilia.";
RL J. Biol. Chem. 278:34211-34218(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15337773; DOI=10.1083/jcb.200405023;
RA Jurczyk A., Gromley A., Redick S., San Agustin J., Witman G., Pazour G.J.,
RA Peters D.J.M., Doxsey S.;
RT "Pericentrin forms a complex with intraflagellar transport proteins and
RT polycystin-2 and is required for primary cilia assembly.";
RL J. Cell Biol. 166:637-643(2004).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16775004; DOI=10.1091/mbc.e06-02-0133;
RA Follit J.A., Tuft R.A., Fogarty K.E., Pazour G.J.;
RT "The intraflagellar transport protein IFT20 is associated with the Golgi
RT complex and is required for cilia assembly.";
RL Mol. Biol. Cell 17:3781-3792(2006).
RN [9]
RP INTERACTION WITH TRIP11.
RX PubMed=19112494; DOI=10.1371/journal.pgen.1000315;
RA Follit J.A., San Agustin J.T., Xu F., Jonassen J.A., Samtani R., Lo C.W.,
RA Pazour G.J.;
RT "The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex.";
RL PLoS Genet. 4:E1000315-E1000315(2008).
RN [10]
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 [11]
RP INTERACTION WITH SPEF2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19889948; DOI=10.1095/biolreprod.108.074971;
RA Sironen A., Hansen J., Thomsen B., Andersson M., Vilkki J., Toppari J.,
RA Kotaja N.;
RT "Expression of SPEF2 during mouse spermatogenesis and identification of
RT IFT20 as an interacting protein.";
RL Biol. Reprod. 82:580-590(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, 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 [13]
RP FUNCTION.
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 [14]
RP SUBCELLULAR LOCATION.
RX PubMed=25243405; DOI=10.1371/journal.pone.0108470;
RA Broekhuis J.R., Verhey K.J., Jansen G.;
RT "Regulation of cilium length and intraflagellar transport by the RCK-
RT kinases ICK and MOK in renal epithelial cells.";
RL PLoS ONE 9:E108470-E108470(2014).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [16]
RP SUBCELLULAR LOCATION.
RX PubMed=28619825; DOI=10.1242/dev.152108;
RA Lehti M.S., Zhang F.P., Kotaja N., Sironen A.;
RT "SPEF2 functions in microtubule-mediated transport in elongating spermatids
RT to ensure proper male germ cell differentiation.";
RL Development 144:2683-2693(2017).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29237719; DOI=10.1083/jcb.201611050;
RA Schmid F.M., Schou K.B., Vilhelm M.J., Holm M.S., Breslin L., Farinelli P.,
RA Larsen L.A., Andersen J.S., Pedersen L.B., Christensen S.T.;
RT "IFT20 modulates ciliary PDGFRalpha signaling by regulating the stability
RT of Cbl E3 ubiquitin ligases.";
RL J. Cell Biol. 217:151-161(2018).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=29690537; DOI=10.3390/ijms19041252;
RA Kazarian E., Son H., Sapao P., Li W., Zhang Z., Strauss J.F., Teves M.E.;
RT "SPAG17 Is Required for Male Germ Cell Differentiation and Fertility.";
RL Int. J. Mol. Sci. 19:0-0(2018).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=31637240; DOI=10.3389/fcell.2019.00216;
RA Sorusch N., Yildirim A., Knapp B., Janson J., Fleck W., Scharf C.,
RA Wolfrum U.;
RT "SANS (USH1G) Molecularly Links the Human Usher Syndrome Protein Network to
RT the Intraflagellar Transport Module by Direct Binding to IFT-B Proteins.";
RL Front. Cell Dev. Biol. 7:216-216(2019).
RN [20]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPATA1.
RX PubMed=31816150; DOI=10.1002/dvdy.141;
RA Zhang L., Zhen J., Huang Q., Liu H., Li W., Zhang S., Min J., Li Y.,
RA Shi L., Woods J., Chen X., Shi Y., Liu Y., Hess R.A., Song S., Zhang Z.;
RT "Mouse spermatogenesis-associated protein 1 (SPATA1), an IFT20 binding
RT partner, is an acrosomal protein.";
RL Dev. Dyn. 249:543-555(2020).
CC -!- FUNCTION: Part of intraflagellar transport (IFT) particles involved in
CC ciliary process assembly. May play a role in the trafficking of ciliary
CC membrane proteins from the Golgi complex to the cilium
CC (PubMed:16775004). Regulates the ciliary platelet-derived growth factor
CC receptor-alpha (PDGFRA) signaling pathway. Required for protein
CC stability of E3 ubiquitin ligases CBL and CBLB that mediate
CC ubiquitination and internalization of PDGFRA for proper feedback
CC inhibition of PDGFRA signaling (PubMed:29237719). Essential for male
CC fertility. Plays an important role in spermatogenesis, particularly
CC spermiogenesis, when germ cells form flagella. May play a role in the
CC transport of flagellar proteins ODF2 and SPAG16 to build sperm flagella
CC and in the removal of redundant sperm cytoplasm (PubMed:27682589). Also
CC involved in autophagy since it is required for trafficking of ATG16L
CC and the expansion of the autophagic compartment (PubMed:24089209).
CC {ECO:0000269|PubMed:16775004, ECO:0000269|PubMed:24089209,
CC ECO:0000269|PubMed:27682589, ECO:0000269|PubMed:29237719}.
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:12821668, PubMed:16775004,
CC PubMed:19253336). Interacts directly with IFT57 and KIF3B/Kinesin II
CC subunit (PubMed:12821668). Interacts with IFT88 (PubMed:19253336).
CC Interacts with CEP83 (By similarity). Interacts with SPEF2 (via C-
CC terminus) (PubMed:19889948). Interacts with CBL and CBLB (By
CC similarity). Interacts with TRIP11 (PubMed:19112494). Interacts with
CC TTC21A (By similarity). Interacts with SPATA1 (PubMed:31816150).
CC Interacts with USH1G (By similarity). {ECO:0000250|UniProtKB:Q8IY31,
CC ECO:0000269|PubMed:12821668, ECO:0000269|PubMed:16775004,
CC ECO:0000269|PubMed:19112494, ECO:0000269|PubMed:19253336,
CC ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:31816150}.
CC -!- INTERACTION:
CC Q61025; Q8C0J2: Atg16l1; NbExp=2; IntAct=EBI-16077253, EBI-769195;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:16775004, ECO:0000269|PubMed:19253336,
CC ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:15337773}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:15337773, ECO:0000269|PubMed:16775004}. Cell
CC projection, cilium {ECO:0000269|PubMed:25243405,
CC ECO:0000269|PubMed:29237719, ECO:0000269|PubMed:31637240}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825,
CC ECO:0000269|PubMed:29690537}. Golgi apparatus
CC {ECO:0000269|PubMed:29237719}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000269|PubMed:31816150}. Cytoplasm
CC {ECO:0000269|PubMed:29690537}. Note=Present at the centrosomes during
CC the cell cycle and associated with the proximal portion of the mother
CC centriole and the lateral aspect of the daughter centriole
CC (PubMed:15337773). Associated with basal body at the base of primary
CC cilia (PubMed:15337773). Detected in the Golgi apparatus of round
CC spermatids and late spermatocytes (PubMed:19889948, PubMed:28619825).
CC Also detected in the manchette of step 10-12 spermatids
CC (PubMed:19889948, PubMed:28619825). In step 14 spermatids, found in the
CC basal body of the sperm tail (PubMed:19889948). Localization in the
CC manchette of elongating spermatids is dependent on SPAG17
CC (PubMed:29690537). {ECO:0000269|PubMed:15337773,
CC ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825,
CC ECO:0000269|PubMed:29690537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61025-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61025-2; Sequence=VSP_020392;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the testis (at protein
CC level). Expressed in kidney and retina. Expression is up-regulated
CC during spermiogenesis. {ECO:0000269|PubMed:11916979,
CC ECO:0000269|PubMed:12821668, ECO:0000269|PubMed:27682589}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at postnatal day 16
CC (P16) and increases significantly at days P30 and P42.
CC {ECO:0000269|PubMed:27682589}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in male germ cells results
CC in infertility, abnormal sperm morphology, significantly reduced sperm
CC count and sperm mobility. {ECO:0000269|PubMed:27682589}.
CC -!- MISCELLANEOUS: Cells that stably express short interference RNAs
CC targeting IFT20 show reduced centriolar IFT20 and lack primary cilia.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI25553.1; 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; AY082613; AAL99202.1; -; mRNA.
DR EMBL; U38981; AAA81518.1; -; mRNA.
DR EMBL; AK002397; BAB22069.1; -; mRNA.
DR EMBL; AK139942; BAE24189.1; -; mRNA.
DR EMBL; AL591177; CAI25553.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL591177; CAI25554.1; -; Genomic_DNA.
DR EMBL; BC002040; AAH02040.1; -; mRNA.
DR CCDS; CCDS25111.1; -. [Q61025-1]
DR RefSeq; NP_061342.1; NM_018854.4. [Q61025-1]
DR AlphaFoldDB; Q61025; -.
DR SMR; Q61025; -.
DR BioGRID; 207750; 5.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR DIP; DIP-60602N; -.
DR IntAct; Q61025; 1.
DR STRING; 10090.ENSMUSP00000118015; -.
DR PhosphoSitePlus; Q61025; -.
DR EPD; Q61025; -.
DR MaxQB; Q61025; -.
DR PaxDb; Q61025; -.
DR PeptideAtlas; Q61025; -.
DR PRIDE; Q61025; -.
DR ProteomicsDB; 267109; -. [Q61025-1]
DR ProteomicsDB; 267110; -. [Q61025-2]
DR Antibodypedia; 13983; 127 antibodies from 22 providers.
DR Ensembl; ENSMUST00000108275; ENSMUSP00000103910; ENSMUSG00000001105. [Q61025-1]
DR Ensembl; ENSMUST00000128788; ENSMUSP00000118015; ENSMUSG00000001105. [Q61025-1]
DR GeneID; 55978; -.
DR KEGG; mmu:55978; -.
DR UCSC; uc007kjs.1; mouse. [Q61025-1]
DR CTD; 90410; -.
DR MGI; MGI:1915585; Ift20.
DR VEuPathDB; HostDB:ENSMUSG00000001105; -.
DR eggNOG; ENOG502RYYR; Eukaryota.
DR GeneTree; ENSGT00390000003413; -.
DR InParanoid; Q61025; -.
DR OMA; TMAKQRQ; -.
DR OrthoDB; 1589590at2759; -.
DR PhylomeDB; Q61025; -.
DR TreeFam; TF319434; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 55978; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ift20; mouse.
DR PRO; PR:Q61025; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61025; protein.
DR Bgee; ENSMUSG00000001105; Expressed in humerus cartilage element and 255 other tissues.
DR ExpressionAtlas; Q61025; baseline and differential.
DR Genevisible; Q61025; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0044292; C:dendrite terminus; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:1902636; C:kinociliary basal body; IDA:MGI.
DR GO; GO:0002177; C:manchette; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0002046; F:opsin binding; IPI:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:MGI.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; 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; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0036372; P:opsin transport; IMP:MGI.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:MGI.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:2000583; P:regulation of platelet-derived growth factor receptor-alpha signaling pathway; IMP:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR InterPro; IPR028172; FT20.
DR PANTHER; PTHR31978; PTHR31978; 1.
DR Pfam; PF14931; IFT20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Differentiation; Golgi apparatus; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..132
FT /note="Intraflagellar transport protein 20 homolog"
FT /id="PRO_0000249304"
FT REGION 70..132
FT /note="IFT57-binding"
FT COILED 74..116
FT /evidence="ECO:0000255"
FT VAR_SEQ 107..132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020392"
SQ SEQUENCE 132 AA; 15237 MW; A0E797D01CFD001D CRC64;
MAKDILGEAG LHFDELNKLR VLDPEVTQQT VELKEECKDF VDKIGQFQKI VGGLIELVDQ
LAKEAENEKM KAIGARNLLK SIAKQREAQQ QQLQALIAEK KTQLERYRVE YEALCKVEAE
QNEFIDQFIF QK
