IFT43_HUMAN
ID IFT43_HUMAN Reviewed; 208 AA.
AC Q96FT9; B3KPT6; B4DZI9; G3V385; O95418; Q9ULA9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Intraflagellar transport protein 43 homolog {ECO:0000305};
GN Name=IFT43 {ECO:0000312|HGNC:HGNC:29669}; Synonyms=C14orf179;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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 INTERACTION WITH WDR35.
RX PubMed=19450523; DOI=10.1016/j.cell.2009.04.053;
RA Cole D.G., Snell W.J.;
RT "SnapShot: Intraflagellar transport.";
RL Cell 137:784-784(2009).
RN [5]
RP IDENTIFICATION IN THE IFT-A COMPLEX.
RX PubMed=20889716; DOI=10.1101/gad.1966210;
RA Mukhopadhyay S., Wen X., Chih B., Nelson C.D., Lane W.S., Scales S.J.,
RA Jackson P.K.;
RT "TULP3 bridges the IFT-A complex and membrane phosphoinositides to promote
RT trafficking of G protein-coupled receptors into primary cilia.";
RL Genes Dev. 24:2180-2193(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP FUNCTION, AND INVOLVEMENT IN CED3.
RX PubMed=21378380; DOI=10.1136/jmg.2011.088864;
RA Arts H.H., Bongers E.M., Mans D.A., van Beersum S.E., Oud M.M., Bolat E.,
RA Spruijt L., Cornelissen E.A., Schuurs-Hoeijmakers J.H., de Leeuw N.,
RA Cormier-Daire V., Brunner H.G., Knoers N.V., Roepman R.;
RT "C14ORF179 encoding IFT43 is mutated in Sensenbrenner syndrome.";
RL J. Med. Genet. 48:390-395(2011).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22361696; DOI=10.1016/j.jprot.2012.01.030;
RA Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R., Uhlen M.,
RA Lundberg E.;
RT "Systematic validation of antibody binding and protein subcellular
RT localization using siRNA and confocal microscopy.";
RL J. Proteomics 75:2236-2251(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION IN THE IFT-A COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=27932497; DOI=10.1091/mbc.e16-11-0813;
RA Hirano T., Katoh Y., Nakayama K.;
RT "Intraflagellar transport-A complex mediates ciliary entry and retrograde
RT trafficking of ciliary G protein-coupled receptors.";
RL Mol. Biol. Cell 28:429-439(2017).
RN [12]
RP IDENTIFICATION IN THE IFT-A COMPLEX.
RX PubMed=29220510; DOI=10.1093/hmg/ddx421;
RA Takahara M., Katoh Y., Nakamura K., Hirano T., Sugawa M., Tsurumi Y.,
RA Nakayama K.;
RT "Ciliopathy-associated mutations of IFT122 impair ciliary protein
RT trafficking but not ciliogenesis.";
RL Hum. Mol. Genet. 27:516-528(2018).
RN [13]
RP FUNCTION, INVOLVEMENT IN SRTD18, VARIANT SRTD18 ARG-174, AND
RP CHARACTERIZATION OF VARIANT SRTD18 ARG-174.
RX PubMed=28400947; DOI=10.1186/s13630-017-0051-y;
RA Duran I., Taylor S.P., Zhang W., Martin J., Qureshi F., Jacques S.M.,
RA Wallerstein R., Lachman R.S., Nickerson D.A., Bamshad M., Cohn D.H.,
RA Krakow D.;
RT "Mutations in IFT-A satellite core component genes IFT43 and IFT121 produce
RT short rib polydactyly syndrome with distinctive campomelia.";
RL Cilia 6:7-7(2017).
RN [14]
RP INVOLVEMENT IN RP81, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP VARIANT RP81 LYS-34, AND CHARACTERIZATION OF VARIANT RP81 LYS-34.
RX PubMed=28973684; DOI=10.1093/hmg/ddx356;
RA Biswas P., Duncan J.L., Ali M., Matsui H., Naeem M.A., Raghavendra P.B.,
RA Frazer K.A., Arts H.H., Riazuddin S., Akram J., Hejtmancik J.F.,
RA Riazuddin S.A., Ayyagari R.;
RT "A mutation in IFT43 causes non-syndromic recessive retinal degeneration.";
RL Hum. Mol. Genet. 26:4741-4751(2017).
CC -!- FUNCTION: As a component of IFT complex A (IFT-A), a complex required
CC for retrograde ciliary transport and entry into cilia of G protein-
CC coupled receptors (GPCRs), it is involved in ciliogenesis
CC (PubMed:28400947, PubMed:28973684). Involved in retrograde ciliary
CC transport along microtubules from the ciliary tip to the base
CC (PubMed:21378380). {ECO:0000269|PubMed:21378380,
CC ECO:0000269|PubMed:28400947, ECO:0000269|PubMed:28973684}.
CC -!- SUBUNIT: Component of the IFT complex A (IFT-A) complex
CC (PubMed:20889716, PubMed:27932497). IFT-A complex is divided into a
CC core subcomplex composed of IFT122:IFT140:WDR19 which is associated
CC with TULP3 and a peripheral subcomplex composed of IFT43:WDR35:TTC21B
CC (PubMed:27932497). Interacts directy with IFT122, WDR35 and TTC21B
CC (PubMed:29220510, PubMed:27932497, PubMed:19450523).
CC {ECO:0000269|PubMed:19450523, ECO:0000269|PubMed:20889716,
CC ECO:0000269|PubMed:27932497, ECO:0000269|PubMed:29220510}.
CC -!- INTERACTION:
CC Q96FT9; P25791: LMO2; NbExp=3; IntAct=EBI-10189681, EBI-739696;
CC Q96FT9; Q9P2L0: WDR35; NbExp=2; IntAct=EBI-10189681, EBI-766448;
CC Q96FT9; O75800: ZMYND10; NbExp=3; IntAct=EBI-10189681, EBI-747061;
CC Q96FT9-2; Q92993: KAT5; NbExp=3; IntAct=EBI-11944538, EBI-399080;
CC Q96FT9-2; P25791-3: LMO2; NbExp=3; IntAct=EBI-11944538, EBI-11959475;
CC Q96FT9-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11944538, EBI-11742507;
CC Q96FT9-2; P17252: PRKCA; NbExp=3; IntAct=EBI-11944538, EBI-1383528;
CC Q96FT9-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-11944538, EBI-9090795;
CC Q96FT9-2; P61981: YWHAG; NbExp=3; IntAct=EBI-11944538, EBI-359832;
CC Q96FT9-2; O75800: ZMYND10; NbExp=3; IntAct=EBI-11944538, EBI-747061;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22361696}. Cell projection, cilium
CC {ECO:0000269|PubMed:27932497, ECO:0000269|PubMed:28973684}.
CC Note=Associated with microtubules (PubMed:22361696). Localized at the
CC distal tip of the cilium (PubMed:28973684).
CC {ECO:0000269|PubMed:22361696, ECO:0000269|PubMed:28973684}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96FT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FT9-2; Sequence=VSP_021169;
CC Name=3;
CC IsoId=Q96FT9-3; Sequence=VSP_041319;
CC Name=4;
CC IsoId=Q96FT9-4; Sequence=VSP_047398;
CC -!- TISSUE SPECIFICITY: Expressed in the retina, predominantly in the
CC photoreceptor outer segment. {ECO:0000269|PubMed:28973684}.
CC -!- DISEASE: Cranioectodermal dysplasia 3 (CED3) [MIM:614099]: A disorder
CC primarily characterized by craniofacial, skeletal and ectodermal
CC abnormalities. Clinical features include craniosynostosis, narrow rib
CC cage, short limbs, brachydactyly, hypoplastic and widely spaced teeth,
CC sparse hair, skin laxity and abnormal nails. Nephronophthisis leading
CC to progressive renal failure, hepatic fibrosis, heart defects, and
CC retinitis pigmentosa have also been described.
CC {ECO:0000269|PubMed:21378380}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Retinitis pigmentosa 81 (RP81) [MIM:617871]: A form of
CC retinitis pigmentosa, a retinal dystrophy belonging to the group of
CC pigmentary retinopathies. Retinitis pigmentosa is characterized by
CC retinal pigment deposits visible on fundus examination and primary loss
CC of rod photoreceptor cells followed by secondary loss of cone
CC photoreceptors. Patients typically have night vision blindness and loss
CC of midperipheral visual field. As their condition progresses, they lose
CC their far peripheral visual field and eventually central vision as
CC well. RP81 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:28973684}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Short-rib thoracic dysplasia 18 with polydactyly (SRTD18)
CC [MIM:617866]: A form of short-rib thoracic dysplasia, a group of
CC autosomal recessive ciliopathies that are characterized by a
CC constricted thoracic cage, short ribs, shortened tubular bones, and a
CC 'trident' appearance of the acetabular roof. Polydactyly is variably
CC present. Non-skeletal involvement can include cleft lip/palate as well
CC as anomalies of major organs such as the brain, eye, heart, kidneys,
CC liver, pancreas, intestines, and genitalia. Some forms of the disease
CC are lethal in the neonatal period due to respiratory insufficiency
CC secondary to a severely restricted thoracic cage, whereas others are
CC compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC Saldino syndrome, and short rib-polydactyly syndrome.
CC {ECO:0000269|PubMed:28400947}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the IFT43 family. {ECO:0000305}.
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DR EMBL; AK056735; BAG51798.1; -; mRNA.
DR EMBL; AK302944; BAG64101.1; -; mRNA.
DR EMBL; AF107885; AAC79728.1; -; Genomic_DNA.
DR EMBL; AC008015; AAF03245.1; -; Genomic_DNA.
DR EMBL; BC010436; AAH10436.1; -; mRNA.
DR CCDS; CCDS41973.1; -. [Q96FT9-1]
DR CCDS; CCDS58330.1; -. [Q96FT9-4]
DR CCDS; CCDS9847.1; -. [Q96FT9-2]
DR RefSeq; NP_001096034.1; NM_001102564.1. [Q96FT9-1]
DR RefSeq; NP_001242924.1; NM_001255995.1. [Q96FT9-4]
DR RefSeq; NP_443105.2; NM_052873.2. [Q96FT9-2]
DR AlphaFoldDB; Q96FT9; -.
DR BioGRID; 125202; 26.
DR ComplexPortal; CPX-5021; IFT-A complex.
DR IntAct; Q96FT9; 22.
DR iPTMnet; Q96FT9; -.
DR PhosphoSitePlus; Q96FT9; -.
DR BioMuta; IFT43; -.
DR DMDM; 334302894; -.
DR EPD; Q96FT9; -.
DR jPOST; Q96FT9; -.
DR MassIVE; Q96FT9; -.
DR MaxQB; Q96FT9; -.
DR PeptideAtlas; Q96FT9; -.
DR PRIDE; Q96FT9; -.
DR ProteomicsDB; 32865; -.
DR ProteomicsDB; 76555; -. [Q96FT9-1]
DR ProteomicsDB; 76556; -. [Q96FT9-2]
DR ProteomicsDB; 76557; -. [Q96FT9-3]
DR Antibodypedia; 191; 87 antibodies from 20 providers.
DR DNASU; 112752; -.
DR Ensembl; ENST00000238628.10; ENSP00000238628.6; ENSG00000119650.13. [Q96FT9-2]
DR Ensembl; ENST00000314067.11; ENSP00000324177.6; ENSG00000119650.13. [Q96FT9-1]
DR Ensembl; ENST00000542766.5; ENSP00000440064.1; ENSG00000119650.13. [Q96FT9-1]
DR Ensembl; ENST00000556742.1; ENSP00000451096.1; ENSG00000119650.13. [Q96FT9-4]
DR GeneID; 112752; -.
DR KEGG; hsa:112752; -.
DR MANE-Select; ENST00000314067.11; ENSP00000324177.6; NM_001102564.3; NP_001096034.1.
DR UCSC; uc001xse.4; human. [Q96FT9-1]
DR CTD; 112752; -.
DR DisGeNET; 112752; -.
DR GeneCards; IFT43; -.
DR GeneReviews; IFT43; -.
DR HGNC; HGNC:29669; IFT43.
DR HPA; ENSG00000119650; Low tissue specificity.
DR MalaCards; IFT43; -.
DR MIM; 614068; gene.
DR MIM; 614099; phenotype.
DR MIM; 617866; phenotype.
DR MIM; 617871; phenotype.
DR neXtProt; NX_Q96FT9; -.
DR OpenTargets; ENSG00000119650; -.
DR Orphanet; 1515; Cranioectodermal dysplasia.
DR PharmGKB; PA145149677; -.
DR VEuPathDB; HostDB:ENSG00000119650; -.
DR GeneTree; ENSGT00390000012060; -.
DR HOGENOM; CLU_104337_0_0_1; -.
DR InParanoid; Q96FT9; -.
DR OMA; RKTGWGD; -.
DR TreeFam; TF323566; -.
DR PathwayCommons; Q96FT9; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q96FT9; -.
DR BioGRID-ORCS; 112752; 12 hits in 1029 CRISPR screens.
DR ChiTaRS; IFT43; human.
DR GenomeRNAi; 112752; -.
DR Pharos; Q96FT9; Tbio.
DR PRO; PR:Q96FT9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96FT9; protein.
DR Bgee; ENSG00000119650; Expressed in right uterine tube and 172 other tissues.
DR ExpressionAtlas; Q96FT9; baseline and differential.
DR Genevisible; Q96FT9; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030991; C:intraciliary transport particle A; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:UniProtKB.
DR InterPro; IPR029302; IFT43.
DR PANTHER; PTHR33724; PTHR33724; 1.
DR Pfam; PF15305; IFT43; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Ciliopathy;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant;
KW Ectodermal dysplasia; Phosphoprotein; Reference proteome;
KW Retinitis pigmentosa.
FT CHAIN 1..208
FT /note="Intraflagellar transport protein 43 homolog"
FT /id="PRO_0000254041"
FT REGION 18..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 72..98
FT /note="KFRRKASEEIEDFRLRPQSLNGSDYGG -> NGTQTGKQQLDLNACYHKTHH
FT RDLGLASLEEA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021169"
FT VAR_SEQ 83..208
FT /note="DFRLRPQSLNGSDYGGDIPIIPDLEEVQEEDFVLQVAAPPSIQIKRVMTYRD
FT LDNDLMKYSAIQTLDGEIDLKLLTKVLAPEHEVREDDVGWDWDHLFTEVSSEVLTEWDP
FT LQTEKEDPAGQARHT -> EYVSSILILMVSYVDLGQQCSLGGHDLFHLC (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047398"
FT VAR_SEQ 99..208
FT /note="DIPIIPDLEEVQEEDFVLQVAAPPSIQIKRVMTYRDLDNDLMKYSAIQTLDG
FT EIDLKLLTKVLAPEHEVREDDVGWDWDHLFTEVSSEVLTEWDPLQTEKEDPAGQARHT
FT -> AVPKQANNSWI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041319"
FT VARIANT 34
FT /note="E -> K (in RP81; results in cilia shortening;
FT dbSNP:rs140366557)"
FT /evidence="ECO:0000269|PubMed:28973684"
FT /id="VAR_080629"
FT VARIANT 85
FT /note="R -> H (in dbSNP:rs2302858)"
FT /id="VAR_056839"
FT VARIANT 174
FT /note="W -> R (in SRTD18; patient cells show reduced amount
FT of IFT43 protein and do not have cilia;
FT dbSNP:rs1555369050)"
FT /evidence="ECO:0000269|PubMed:28400947"
FT /id="VAR_080630"
FT CONFLICT 13
FT /note="Y -> C (in Ref. 1; BAG64101)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="D -> Y (in Ref. 1; BAG64101)"
FT /evidence="ECO:0000305"
FT VARIANT Q96FT9-2:94
FT /note="D -> N (in dbSNP:rs17783366)"
FT /evidence="ECO:0000305"
FT /id="VAR_082868"
SQ SEQUENCE 208 AA; 23529 MW; 53586B5CAEF51A13 CRC64;
MEDLLDLDEE LRYSLATSRA KMGRRAQQES AQAENHLNGK NSSLTLTGET SSAKLPRCRQ
GGWAGDSVKA SKFRRKASEE IEDFRLRPQS LNGSDYGGDI PIIPDLEEVQ EEDFVLQVAA
PPSIQIKRVM TYRDLDNDLM KYSAIQTLDG EIDLKLLTKV LAPEHEVRED DVGWDWDHLF
TEVSSEVLTE WDPLQTEKED PAGQARHT
