WDR35_HUMAN
ID WDR35_HUMAN Reviewed; 1181 AA.
AC Q9P2L0; B3KVI5; Q4ZG01; Q8NE11;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=WD repeat-containing protein 35 {ECO:0000305};
DE AltName: Full=Intraflagellar transport protein 121 homolog;
GN Name=WDR35 {ECO:0000312|HGNC:HGNC:29250};
GN Synonyms=IFT121 {ECO:0000303|PubMed:27932497, ECO:0000303|PubMed:29220510},
GN KIAA1336;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-983.
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-878.
RC TISSUE=Testis;
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 [7]
RP INTERACTION WITH IFT43.
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 [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=20193664; DOI=10.1016/j.bbrc.2010.02.133;
RA Feng G.G., Li C., Huang L., Tsunekawa K., Sato Y., Fujiwara Y., Komatsu T.,
RA Honda T., Fan J.H., Goto H., Koide T., Hasegawa T., Ishikawa N.;
RT "Naofen, a novel WD40-repeat protein, mediates spontaneous and tumor
RT necrosis factor-induced apoptosis.";
RL Biochem. Biophys. Res. Commun. 394:153-157(2010).
RN [9]
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 [10]
RP IDENTIFICATION IN THE IFT-A COMPLEX.
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 [11]
RP FUNCTION, AND 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 [12]
RP FUNCTION, AND VARIANT SRTD7 ARG-261.
RX PubMed=21473986; DOI=10.1016/j.ajhg.2011.03.015;
RA Mill P., Lockhart P.J., Fitzpatrick E., Mountford H.S., Hall E.A.,
RA Reijns M.A., Keighren M., Bahlo M., Bromhead C.J., Budd P., Aftimos S.,
RA Delatycki M.B., Savarirayan R., Jackson I.J., Amor D.J.;
RT "Human and mouse mutations in WDR35 cause short-rib polydactyly syndromes
RT due to abnormal ciliogenesis.";
RL Am. J. Hum. Genet. 88:508-515(2011).
RN [13]
RP VARIANTS CED2 GLY-626 AND THR-875.
RX PubMed=20817137; DOI=10.1016/j.ajhg.2010.08.004;
RA Gilissen C., Arts H.H., Hoischen A., Spruijt L., Mans D.A., Arts P.,
RA van Lier B., Steehouwer M., van Reeuwijk J., Kant S.G., Roepman R.,
RA Knoers N.V., Veltman J.A., Brunner H.G.;
RT "Exome sequencing identifies WDR35 variants involved in Sensenbrenner
RT syndrome.";
RL Am. J. Hum. Genet. 87:418-423(2010).
RN [14]
RP VARIANT SRTD7/20 LEU-311.
RX PubMed=27158779; DOI=10.1038/ng.3558;
RA Toriyama M., Lee C., Taylor S.P., Duran I., Cohn D.H., Bruel A.L.,
RA Tabler J.M., Drew K., Kelly M.R., Kim S., Park T.J., Braun D.A.,
RA Pierquin G., Biver A., Wagner K., Malfroot A., Panigrahi I., Franco B.,
RA Al-Lami H.A., Yeung Y., Choi Y.J., Duffourd Y., Faivre L., Riviere J.B.,
RA Chen J., Liu K.J., Marcotte E.M., Hildebrandt F., Thauvin-Robinet C.,
RA Krakow D., Jackson P.K., Wallingford J.B.;
RT "The ciliopathy-associated CPLANE proteins direct basal body recruitment of
RT intraflagellar transport machinery.";
RL Nat. Genet. 48:648-656(2016).
RN [15]
RP VARIANTS SRTD7 LEU-311; LYS-478 AND 527-GLN--GLY-1181 DEL, CHARACTERIZATION
RP OF VARIANTS SRTD7 LEU-311; LYS-478 AND 527-GLN--GLY-1181 DEL, AND FUNCTION.
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).
CC -!- FUNCTION: As a component of the IFT complex A (IFT-A), a complex
CC required for retrograde ciliary transport and entry into cilia of G
CC protein-coupled receptors (GPCRs), it is involved in ciliogenesis and
CC ciliary protein trafficking (PubMed:21473986, PubMed:28400947,
CC PubMed:29220510). May promote CASP3 activation and TNF-stimulated
CC apoptosis. {ECO:0000269|PubMed:20193664, ECO:0000269|PubMed:21473986,
CC ECO:0000269|PubMed:28400947, ECO:0000269|PubMed:29220510}.
CC -!- SUBUNIT: Component of the IFT complex A (IFT-A) complex
CC (PubMed:20889716, PubMed:27932497, PubMed:29220510). IFT-A complex is
CC divided into a core subcomplex composed of IFT122:IFT140:WDR19 which is
CC associated with TULP3 and a peripheral subcomplex composed of
CC IFT43:WDR35:TTC21B (PubMed:27932497, PubMed:29220510). Interacts
CC directy with IFT122, ITF43 and TTC21B (PubMed:29220510,
CC PubMed:27932497). Interacts with IFT43 (PubMed:19450523).
CC {ECO:0000269|PubMed:19450523, ECO:0000269|PubMed:20889716,
CC ECO:0000269|PubMed:27932497, ECO:0000269|PubMed:29220510}.
CC -!- INTERACTION:
CC Q9P2L0; Q96FT9: IFT43; NbExp=2; IntAct=EBI-766448, EBI-10189681;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8BND3}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q8BND3}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BND3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2L0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2L0-2; Sequence=VSP_009732;
CC -!- INDUCTION: By TNF. {ECO:0000269|PubMed:20193664}.
CC -!- DISEASE: Cranioectodermal dysplasia 2 (CED2) [MIM:613610]: A disorder
CC characterized by craniofacial, skeletal and ectodermal abnormalities.
CC Clinical features include short stature, dolichocephaly,
CC craniosynostosis, narrow thorax with pectus excavatum, short limbs,
CC brachydactyly, joint laxity, narrow palpebral fissures, telecanthus
CC with hypertelorism, low-set simple ears, everted lower lip, and short
CC neck. Teeth abnormalities include widely spaced, hypoplastic and fused
CC teeth. {ECO:0000269|PubMed:20817137}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Short-rib thoracic dysplasia 7 with or without polydactyly
CC (SRTD7) [MIM:614091]: A form of short-rib thoracic dysplasia, a group
CC of 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. SRTD7 hallmarks
CC are acromesomelic hypomineralization, campomelia, polysyndactyly,
CC laterality defects, and cystic kidneys. {ECO:0000269|PubMed:21473986,
CC ECO:0000269|PubMed:28400947}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. WDR35 mutations cause
CC short rib-polydactyly syndrome through impaired cilia formation.
CC Primary fibroblasts from SRTD7 patients lacking WDR35 fail to produce
CC cilia (PubMed:21473986). {ECO:0000269|PubMed:21473986}.
CC -!- DISEASE: Short-rib thoracic dysplasia 7/20 with polydactyly, digenic
CC (SRTD7/20) [MIM:614091]: A digenic form of short-rib thoracic dysplasia
CC caused by double heterozygosity for a mutation in the WDR35 gene and a
CC mutation in the INTU gene. Short-rib thoracic dysplasia is part of a
CC group of ciliopathies that are characterized by a constricted thoracic
CC cage, short ribs, shortened tubular bones, and a 'trident' appearance
CC of the acetabular roof. Polydactyly is variably present. Non-skeletal
CC involvement can include cleft lip/palate as well as anomalies of major
CC organs such as the brain, eye, heart, kidneys, liver, pancreas,
CC intestines, and genitalia. Some forms of the disease are lethal in the
CC neonatal period due to respiratory insufficiency secondary to a
CC severely restricted thoracic cage, whereas others are compatible with
CC life. Disease spectrum encompasses Ellis-van Creveld syndrome,
CC asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-Saldino
CC syndrome, and short rib-polydactyly syndrome.
CC {ECO:0000269|PubMed:27158779}. Note=The disease is caused by variants
CC affecting distinct genetic loci, including the gene represented in this
CC entry. SRTD7/20 can be caused by co-occurrence of WDR35 variant
CC p.Trp311Leu and INTU p.Gln276Ter. One such patient has been reported.
CC {ECO:0000269|PubMed:27158779}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92574.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB037757; BAA92574.2; ALT_INIT; mRNA.
DR EMBL; AK122917; BAG53797.1; -; mRNA.
DR EMBL; AC079145; AAX88936.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00841.1; -; Genomic_DNA.
DR EMBL; BC036659; AAH36659.1; -; mRNA.
DR CCDS; CCDS1695.1; -. [Q9P2L0-2]
DR CCDS; CCDS33152.1; -. [Q9P2L0-1]
DR RefSeq; NP_001006658.1; NM_001006657.1. [Q9P2L0-1]
DR RefSeq; NP_065830.2; NM_020779.3. [Q9P2L0-2]
DR AlphaFoldDB; Q9P2L0; -.
DR BioGRID; 121598; 37.
DR ComplexPortal; CPX-5021; IFT-A complex.
DR CORUM; Q9P2L0; -.
DR IntAct; Q9P2L0; 21.
DR STRING; 9606.ENSP00000314444; -.
DR GlyGen; Q9P2L0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2L0; -.
DR PhosphoSitePlus; Q9P2L0; -.
DR BioMuta; WDR35; -.
DR DMDM; 48474987; -.
DR EPD; Q9P2L0; -.
DR jPOST; Q9P2L0; -.
DR MassIVE; Q9P2L0; -.
DR MaxQB; Q9P2L0; -.
DR PaxDb; Q9P2L0; -.
DR PeptideAtlas; Q9P2L0; -.
DR PRIDE; Q9P2L0; -.
DR ProteomicsDB; 83843; -. [Q9P2L0-1]
DR ProteomicsDB; 83844; -. [Q9P2L0-2]
DR Antibodypedia; 50378; 65 antibodies from 22 providers.
DR DNASU; 57539; -.
DR Ensembl; ENST00000281405.9; ENSP00000281405.5; ENSG00000118965.16. [Q9P2L0-2]
DR Ensembl; ENST00000345530.8; ENSP00000314444.5; ENSG00000118965.16. [Q9P2L0-1]
DR GeneID; 57539; -.
DR KEGG; hsa:57539; -.
DR MANE-Select; ENST00000281405.9; ENSP00000281405.5; NM_020779.4; NP_065830.2. [Q9P2L0-2]
DR UCSC; uc002rdi.5; human. [Q9P2L0-1]
DR CTD; 57539; -.
DR DisGeNET; 57539; -.
DR GeneCards; WDR35; -.
DR GeneReviews; WDR35; -.
DR HGNC; HGNC:29250; WDR35.
DR HPA; ENSG00000118965; Low tissue specificity.
DR MalaCards; WDR35; -.
DR MIM; 613602; gene.
DR MIM; 613610; phenotype.
DR MIM; 614091; phenotype.
DR neXtProt; NX_Q9P2L0; -.
DR OpenTargets; ENSG00000118965; -.
DR Orphanet; 1515; Cranioectodermal dysplasia.
DR Orphanet; 498497; Short rib-polydactyly syndrome type 5.
DR Orphanet; 93271; Short rib-polydactyly syndrome, Verma-Naumoff type.
DR PharmGKB; PA134928987; -.
DR VEuPathDB; HostDB:ENSG00000118965; -.
DR eggNOG; KOG2041; Eukaryota.
DR GeneTree; ENSGT00940000155745; -.
DR InParanoid; Q9P2L0; -.
DR OMA; HCASPME; -.
DR OrthoDB; 95796at2759; -.
DR PhylomeDB; Q9P2L0; -.
DR TreeFam; TF314076; -.
DR PathwayCommons; Q9P2L0; -.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q9P2L0; -.
DR BioGRID-ORCS; 57539; 14 hits in 1083 CRISPR screens.
DR ChiTaRS; WDR35; human.
DR GenomeRNAi; 57539; -.
DR Pharos; Q9P2L0; Tbio.
DR PRO; PR:Q9P2L0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9P2L0; protein.
DR Bgee; ENSG00000118965; Expressed in bronchial epithelial cell and 193 other tissues.
DR ExpressionAtlas; Q9P2L0; baseline and differential.
DR Genevisible; Q9P2L0; HS.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0030991; C:intraciliary transport particle A; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:MGI.
DR GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR017233; WDR35.
DR PANTHER; PTHR16517:SF1; PTHR16517:SF1; 1.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR PIRSF; PIRSF037536; WD_repeat_p35; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant;
KW Ectodermal dysplasia; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1181
FT /note="WD repeat-containing protein 35"
FT /id="PRO_0000051384"
FT REPEAT 4..43
FT /note="WD 1"
FT REPEAT 61..100
FT /note="WD 2"
FT REPEAT 105..143
FT /note="WD 3"
FT REPEAT 147..185
FT /note="WD 4"
FT REPEAT 193..241
FT /note="WD 5"
FT REPEAT 246..288
FT /note="WD 6"
FT VAR_SEQ 399..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009732"
FT VARIANT 18
FT /note="Q -> R (in dbSNP:rs1060742)"
FT /id="VAR_053428"
FT VARIANT 261
FT /note="W -> R (in SRTD7; dbSNP:rs431905505)"
FT /evidence="ECO:0000269|PubMed:21473986"
FT /id="VAR_065955"
FT VARIANT 311
FT /note="W -> L (in SRTD7 and SRTD7/20; the SRTD7/20 patient
FT also carries variant INTU 276-Q--L-942 del; chondrocyte
FT cell lines from a patient show a reduction of cilia
FT indicating a defect in ciliogenesis; dbSNP:rs200649783)"
FT /evidence="ECO:0000269|PubMed:27158779,
FT ECO:0000269|PubMed:28400947"
FT /id="VAR_076784"
FT VARIANT 478
FT /note="R -> K (in SRTD7; chondrocyte cell lines from the
FT patient show a reduction of cilia indicating a defect in
FT ciliogenesis; dbSNP:rs1558342399)"
FT /evidence="ECO:0000269|PubMed:28400947"
FT /id="VAR_080632"
FT VARIANT 527..1181
FT /note="Missing (in SRTD7; chondrocyte cell lines from the
FT patient show a reduction of cilia indicating a defect in
FT ciliogenesis)"
FT /evidence="ECO:0000269|PubMed:28400947"
FT /id="VAR_080633"
FT VARIANT 626
FT /note="E -> G (in CED2; dbSNP:rs267607174)"
FT /evidence="ECO:0000269|PubMed:20817137"
FT /id="VAR_064581"
FT VARIANT 875
FT /note="A -> T (in CED2; dbSNP:rs267607175)"
FT /evidence="ECO:0000269|PubMed:20817137"
FT /id="VAR_064582"
FT VARIANT 878
FT /note="A -> P (in dbSNP:rs2293669)"
FT /id="VAR_062102"
FT VARIANT 878
FT /note="A -> T (in dbSNP:rs2293669)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_062103"
FT VARIANT 983
FT /note="E -> G (in dbSNP:rs1191778)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_053429"
FT CONFLICT 1078
FT /note="S -> G (in Ref. 6; AAH36659)"
FT /evidence="ECO:0000305"
FT CONFLICT 1171
FT /note="S -> G (in Ref. 3; BAG53797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1181 AA; 133547 MW; 1C0FFAAD0287F129 CRC64;
MFFYLSKKIS IPNNVKLQCV SWNKEQGFIA CGGEDGLLKV LKLETQTDDA KLRGLAAPSN
LSMNQTLEGH SGSVQVVTWN EQYQKLTTSD ENGLIIVWML YKGSWIEEMI NNRNKSVVRS
MSWNADGQKI CIVYEDGAVI VGSVDGNRIW GKDLKGIQLS HVTWSADSKV LLFGMANGEI
HIYDNQGNFM IKMKLSCLVN VTGAISIAGI HWYHGTEGYV EPDCPCLAVC FDNGRCQIMR
HENDQNPVLI DTGMYVVGIQ WNHMGSVLAV AGFQKAAMQD KDVNIVQFYT PFGEHLGTLK
VPGKEISALS WEGGGLKIAL AVDSFIYFAN IRPNYKWGYC SNTVVYAYTR PDRPEYCVVF
WDTKNNEKYV KYVKGLISIT TCGDFCILAT KADENHPQEE NEMETFGATF VLVLCNSIGT
PLDPKYIDIV PLFVAMTKTH VIAASKEAFY TWQYRVAKKL TALEINQITR SRKEGRERIY
HVDDTPSGSM DGVLDYSKTI QGTRDPICAI TASDKILIVG RESGTIQRYS LPNVGLIQKY
SLNCRAYQLS LNCNSSRLAI IDISGVLTFF DLDARVTDST GQQVVGELLK LERRDVWDMK
WAKDNPDLFA MMEKTRMYVF RNLDPEEPIQ TSGYICNFED LEIKSVLLDE ILKDPEHPNK
DYLINFEIRS LRDSRALIEK VGIKDASQFI EDNPHPRLWR LLAEAALQKL DLYTAEQAFV
RCKDYQGIKF VKRLGKLLSE SMKQAEVVGY FGRFEEAERT YLEMDRRDLA IGLRLKLGDW
FRVLQLLKTG SGDADDSLLE QANNAIGDYF ADRQKWLNAV QYYVQGRNQE RLAECYYMLE
DYEGLENLAI SLPENHKLLP EIAQMFVRVG MCEQAVTAFL KCSQPKAAVD TCVHLNQWNK
AVELAKNHSM KEIGSLLARY ASHLLEKNKT LDAIELYRKA NYFFDAAKLM FKIADEEAKK
GSKPLRVKKL YVLSALLIEQ YHEQMKNAQR GKVKGKSSEA TSALAGLLEE EVLSTTDRFT
DNAWRGAEAY HFFILAQRQL YEGCVDTALK TALHLKDYED IIPPVEIYSL LALCACASRA
FGTCSKAFIK LKSLETLSSE QKQQYEDLAL EIFTKHTSKD NRKPELDSLM EGGEGKLPTC
VATGSPITEY QFWMCSVCKH GVLAQEISHY SFCPLCHSPV G
