ID IF122_HUMAN Reviewed; 1241 AA. AC Q9HBG6; B3KW53; B4DEY9; B4DPW7; E7EQF4; E9PDG2; E9PDX2; G3XAB1; H7C3C0; AC Q53G36; Q8TC06; Q9BTB9; Q9BTY4; Q9HAT9; Q9HBG5; Q9NV68; Q9UF80; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 24-JAN-2024, entry version 183. DE RecName: Full=Intraflagellar transport protein 122 homolog {ECO:0000305}; DE AltName: Full=WD repeat-containing protein 10; DE AltName: Full=WD repeat-containing protein 140; GN Name=IFT122 {ECO:0000312|HGNC:HGNC:13556}; GN Synonyms=SPG, WDR10, WDR140; 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 [MRNA] (ISOFORM 5), AND TISSUE SPECIFICITY. RX PubMed=11242542; DOI=10.1089/10445490150504684; RA Gross C., De Baere E., Lo A., Chang W., Messiaen L.; RT "Cloning and characterization of human WDR10, a novel gene located at 3q21 RT encoding a WD-repeat protein that is highly expressed in pituitary and RT testis."; RL DNA Cell Biol. 20:41-52(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Shan Y.X., Li J.M., Sha J.H.; RT "The research of spermatogenesis related genes."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9; 10 AND 11). RC TISSUE=Cerebellum; 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 MRNA] (ISOFORM 8). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Lung, and 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 [8] 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 [9] RP IDENTIFICATION IN THE IFT-A COMPLEX, AND FUNCTION. 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 [10] RP INTERACTION WITH IFTAP. RX PubMed=30476139; DOI=10.1093/jb/mvy100; RA Takahara M., Kunii M., Nakamura K., Harada A., Hirano T., Katoh Y., RA Nakayama K.; RT "C11ORF74 interacts with the IFT-A complex and participates in ciliary RT BBSome localization."; RL J. Biochem. 165:257-267(2019). RN [11] RP VARIANTS CED1 CYS-7; PHE-322 AND GLY-502. RX PubMed=20493458; DOI=10.1016/j.ajhg.2010.04.012; RA Walczak-Sztulpa J., Eggenschwiler J., Osborn D., Brown D.A., Emma F., RA Klingenberg C., Hennekam R.C., Torre G., Garshasbi M., Tzschach A., RA Szczepanska M., Krawczynski M., Zachwieja J., Zwolinska D., Beales P.L., RA Ropers H.H., Latos-Bielenska A., Kuss A.W.; RT "Cranioectodermal dysplasia, Sensenbrenner syndrome, is a ciliopathy caused RT by mutations in the IFT122 gene."; RL Am. J. Hum. Genet. 86:949-956(2010). RN [12] RP VARIANT CED1 ARG-495. RX PubMed=23826986; DOI=10.1111/cge.12215; RA Tsurusaki Y., Yonezawa R., Furuya M., Nishimura G., Pooh R.K., RA Nakashima M., Saitsu H., Miyake N., Saito S., Matsumoto N.; RT "Whole exome sequencing revealed biallelic IFT122 mutations in a family RT with CED1 and recurrent pregnancy loss."; RL Clin. Genet. 85:592-594(2014). RN [13] RP VARIANT CED1 VAL-572, AND CHARACTERIZATION OF VARIANT CED1 VAL-572. RX PubMed=24689072; DOI=10.1002/mgg3.44; RA Alazami A.M., Seidahmed M.Z., Alzahrani F., Mohammed A.O., Alkuraya F.S.; RT "Novel IFT122 mutation associated with impaired ciliogenesis and RT cranioectodermal dysplasia."; RL Mol. Genet. Genomic Med. 2:103-106(2014). RN [14] RP VARIANTS CED1 LEU-391; CYS-570 AND PRO-712. RX PubMed=26792575; DOI=10.1002/ajmg.a.37570; RA Moosa S., Obregon M.G., Altmueller J., Thiele H., Nuernberg P., Fano V., RA Wollnik B.; RT "Novel IFT122 mutations in three Argentinian patients with cranioectodermal RT dysplasia: Expanding the mutational spectrum."; RL Am. J. Med. Genet. A 170A:1295-1301(2016). RN [15] RP FUNCTION, IDENTIFICATION IN THE IFT-A COMPLEX, DOMAIN, CHARACTERIZATION OF RP VARIANTS CED1 CYS-7; PHE-322; ARG-495; GLY-502 AND VAL-572, AND SUBCELLULAR RP LOCATION. 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). 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 required in ciliogenesis and CC ciliary protein trafficking (PubMed:27932497, PubMed:29220510). CC Involved in cilia formation during neuronal patterning. Acts as a CC negative regulator of Shh signaling. Required to recruit TULP3 to CC primary cilia (By similarity). {ECO:0000250|UniProtKB:Q6NWV3, CC ECO:0000269|PubMed:27932497, ECO:0000269|PubMed:29220510}. 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, PubMed:29220510). Interacts with IFT43:WDR35; the CC interaction connects the 2 IFT-A subcomplexes (PubMed:29220510). CC Interacts with IFTAP; the interaction associates IFTAP with IFT-A CC complex (PubMed:30476139). {ECO:0000269|PubMed:20889716, CC ECO:0000269|PubMed:27932497, ECO:0000269|PubMed:29220510, CC ECO:0000269|PubMed:30476139}. CC -!- INTERACTION: CC Q9HBG6; Q8NEZ3: WDR19; NbExp=5; IntAct=EBI-2805994, EBI-11903679; CC Q9HBG6; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-2805994, EBI-6248094; CC Q9HBG6-3; Q7Z4L5: TTC21B; NbExp=2; IntAct=EBI-26854447, EBI-2851301; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium CC {ECO:0000269|PubMed:29220510}. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000269|PubMed:29220510}. Note=Localizes to photoreceptor CC connecting cilia. {ECO:0000250|UniProtKB:Q6NWV3}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Name=1; CC IsoId=Q9HBG6-1; Sequence=Displayed; CC Name=3; CC IsoId=Q9HBG6-3; Sequence=VSP_041161; CC Name=4; CC IsoId=Q9HBG6-4; Sequence=VSP_043310, VSP_041161, VSP_043311; CC Name=5; CC IsoId=Q9HBG6-5; Sequence=VSP_045224; CC Name=6; CC IsoId=Q9HBG6-6; Sequence=VSP_045224, VSP_041161, VSP_043311; CC Name=7; CC IsoId=Q9HBG6-7; Sequence=VSP_056773, VSP_041161; CC Name=8; CC IsoId=Q9HBG6-8; Sequence=VSP_056773; CC Name=9; CC IsoId=Q9HBG6-9; Sequence=VSP_056774, VSP_041161, VSP_056777, CC VSP_043311; CC Name=10; CC IsoId=Q9HBG6-10; Sequence=VSP_056775, VSP_056776, VSP_043311; CC Name=11; CC IsoId=Q9HBG6-11; Sequence=VSP_041161, VSP_056778; CC -!- TISSUE SPECIFICITY: Expressed in many tissues. Predominant expression CC in testis and pituitary. {ECO:0000269|PubMed:11242542}. CC -!- DOMAIN: Forms the trimeric core subcomplex IFT122:IFT140:WDR19 via the CC C-terminal region, whereas it interacts with IFT43:WDR35 via the N- CC terminal region containing the WD repeats. CC {ECO:0000269|PubMed:29220510}. CC -!- DISEASE: Cranioectodermal dysplasia 1 (CED1) [MIM:218330]: A disorder CC characterized by craniofacial, skeletal and ectodermal abnormalities. CC Clinical features include dolichocephaly (with or without sagittal CC suture synostosis), scaphocephaly, short stature, limb shortening, CC short ribs, narrow chest, brachydactyly, renal failure and hepatic CC fibrosis, small and abnormally shaped teeth, sparse hair, skin laxity CC and abnormal nails. {ECO:0000269|PubMed:20493458, CC ECO:0000269|PubMed:23826986, ECO:0000269|PubMed:24689072, CC ECO:0000269|PubMed:26792575, ECO:0000269|PubMed:29220510}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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; AF244930; AAG15427.1; -; mRNA. DR EMBL; AF244931; AAG15428.1; -; mRNA. DR EMBL; AF302154; AAG13415.1; -; mRNA. DR EMBL; AK001759; BAA91888.1; -; mRNA. DR EMBL; AK293852; BAG57250.1; -; mRNA. DR EMBL; AK298526; BAG60729.1; -; mRNA. DR EMBL; AK124140; BAG54015.1; -; mRNA. DR EMBL; AK223095; BAD96815.1; -; mRNA. DR EMBL; AC080007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL449212; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79246.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79247.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79249.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79250.1; -; Genomic_DNA. DR EMBL; BC028353; AAH28353.1; -; mRNA. DR EMBL; BC003045; AAH03045.2; -; mRNA. DR EMBL; BC004238; AAH04238.1; -; mRNA. DR CCDS; CCDS3059.1; -. [Q9HBG6-3] DR CCDS; CCDS3060.1; -. [Q9HBG6-5] DR CCDS; CCDS3061.1; -. [Q9HBG6-1] DR CCDS; CCDS3062.1; -. [Q9HBG6-4] DR CCDS; CCDS63770.1; -. [Q9HBG6-6] DR PIR; T43484; T43484. DR RefSeq; NP_001267470.1; NM_001280541.1. [Q9HBG6-6] DR RefSeq; NP_001267474.1; NM_001280545.1. [Q9HBG6-8] DR RefSeq; NP_001267475.1; NM_001280546.1. [Q9HBG6-7] DR RefSeq; NP_060732.2; NM_018262.3. [Q9HBG6-3] DR RefSeq; NP_443711.2; NM_052985.3. [Q9HBG6-5] DR RefSeq; NP_443715.1; NM_052989.2. [Q9HBG6-1] DR RefSeq; NP_443716.1; NM_052990.2. [Q9HBG6-4] DR PDB; 8BBE; EM; 3.50 A; C=1-1241. DR PDB; 8BBF; EM; 8.00 A; C=1-1241. DR PDB; 8BBG; EM; 3.50 A; C=1-1241. DR PDB; 8FGW; EM; 3.70 A; B=1-1241. DR PDB; 8FH3; EM; 4.30 A; B=1-1241. DR PDBsum; 8BBE; -. DR PDBsum; 8BBF; -. DR PDBsum; 8BBG; -. DR PDBsum; 8FGW; -. DR PDBsum; 8FH3; -. DR AlphaFoldDB; Q9HBG6; -. DR EMDB; EMD-15954; -. DR EMDB; EMD-15955; -. DR EMDB; EMD-29073; -. DR EMDB; EMD-29078; -. DR SMR; Q9HBG6; -. DR BioGRID; 120882; 86. DR ComplexPortal; CPX-5021; Intraflagellar transport complex A. DR CORUM; Q9HBG6; -. DR IntAct; Q9HBG6; 26. DR STRING; 9606.ENSP00000296266; -. DR TCDB; 1.X.1.1.1; the intraflagellar transporter-a complex (ift-a) family. DR iPTMnet; Q9HBG6; -. DR PhosphoSitePlus; Q9HBG6; -. DR BioMuta; IFT122; -. DR DMDM; 212276436; -. DR EPD; Q9HBG6; -. DR jPOST; Q9HBG6; -. DR MassIVE; Q9HBG6; -. DR MaxQB; Q9HBG6; -. DR PaxDb; 9606-ENSP00000296266; -. DR PeptideAtlas; Q9HBG6; -. DR ProteomicsDB; 17562; -. DR ProteomicsDB; 19657; -. DR ProteomicsDB; 33699; -. DR ProteomicsDB; 3996; -. DR ProteomicsDB; 45277; -. DR ProteomicsDB; 4822; -. DR ProteomicsDB; 81540; -. [Q9HBG6-1] DR ProteomicsDB; 81542; -. [Q9HBG6-3] DR ProteomicsDB; 81543; -. [Q9HBG6-4] DR Pumba; Q9HBG6; -. DR Antibodypedia; 33252; 76 antibodies from 20 providers. DR DNASU; 55764; -. DR Ensembl; ENST00000296266.7; ENSP00000296266.3; ENSG00000163913.14. [Q9HBG6-5] DR Ensembl; ENST00000347300.6; ENSP00000323973.3; ENSG00000163913.14. [Q9HBG6-3] DR Ensembl; ENST00000348417.7; ENSP00000324005.4; ENSG00000163913.14. [Q9HBG6-1] DR Ensembl; ENST00000349441.6; ENSP00000324165.3; ENSG00000163913.14. [Q9HBG6-4] DR Ensembl; ENST00000507564.5; ENSP00000425536.1; ENSG00000163913.14. [Q9HBG6-6] DR Ensembl; ENST00000689005.1; ENSP00000510168.1; ENSG00000163913.14. [Q9HBG6-10] DR Ensembl; ENST00000693233.1; ENSP00000509186.1; ENSG00000163913.14. [Q9HBG6-7] DR GeneID; 55764; -. DR KEGG; hsa:55764; -. DR MANE-Select; ENST00000348417.7; ENSP00000324005.4; NM_052989.3; NP_443715.1. DR UCSC; uc003eml.5; human. [Q9HBG6-1] DR AGR; HGNC:13556; -. DR CTD; 55764; -. DR DisGeNET; 55764; -. DR GeneCards; IFT122; -. DR GeneReviews; IFT122; -. DR HGNC; HGNC:13556; IFT122. DR HPA; ENSG00000163913; Tissue enhanced (testis). DR MalaCards; IFT122; -. DR MIM; 218330; phenotype. DR MIM; 606045; gene. DR neXtProt; NX_Q9HBG6; -. DR OpenTargets; ENSG00000163913; -. DR Orphanet; 1515; Cranioectodermal dysplasia. DR Orphanet; 93268; Short rib-polydactyly syndrome, Beemer-Langer type. DR PharmGKB; PA37798; -. DR VEuPathDB; HostDB:ENSG00000163913; -. DR eggNOG; KOG1538; Eukaryota. DR GeneTree; ENSGT00390000001016; -. DR HOGENOM; CLU_008896_0_0_1; -. DR InParanoid; Q9HBG6; -. DR OMA; GDSFDTW; -. DR OrthoDB; 5484092at2759; -. DR PhylomeDB; Q9HBG6; -. DR TreeFam; TF105855; -. DR PathwayCommons; Q9HBG6; -. DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR SignaLink; Q9HBG6; -. DR BioGRID-ORCS; 55764; 11 hits in 1152 CRISPR screens. DR ChiTaRS; IFT122; human. DR GenomeRNAi; 55764; -. DR Pharos; Q9HBG6; Tbio. DR PRO; PR:Q9HBG6; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9HBG6; Protein. DR Bgee; ENSG00000163913; Expressed in right testis and 166 other cell types or tissues. DR ExpressionAtlas; Q9HBG6; baseline and differential. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. 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:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0097730; C:non-motile cilium; IBA:GO_Central. DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB. DR GO; GO:0048593; P:camera-type eye morphogenesis; ISS:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0010172; P:embryonic body morphogenesis; ISS:UniProtKB. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; ISS:BHF-UCL. DR GO; GO:0035050; P:embryonic heart tube development; ISS:UniProtKB. DR GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:BHF-UCL. DR GO; GO:0072594; P:establishment of protein localization to organelle; ISS:BHF-UCL. DR GO; GO:0035720; P:intraciliary anterograde transport; ISS:BHF-UCL. DR GO; GO:0035721; P:intraciliary retrograde transport; ISS:UniProtKB. DR GO; GO:0042073; P:intraciliary transport; IMP:UniProtKB. DR GO; GO:0060173; P:limb development; ISS:UniProtKB. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB. DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB. DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central. DR GO; GO:0061512; P:protein localization to cilium; IMP:UniProtKB. DR GO; GO:0007227; P:signal transduction downstream of smoothened; ISS:BHF-UCL. DR GO; GO:0021513; P:spinal cord dorsal/ventral patterning; ISS:BHF-UCL. DR Gene3D; 1.25.40.470; -; 2. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3. DR InterPro; IPR039857; Ift122/121. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR12764:SF4; INTRAFLAGELLAR TRANSPORT PROTEIN 122 HOMOLOG; 1. DR PANTHER; PTHR12764; WD REPEAT DOMAIN-RELATED; 1. DR Pfam; PF00400; WD40; 2. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q9HBG6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; KW Developmental protein; Disease variant; Ectodermal dysplasia; KW Reference proteome; Repeat; WD repeat. FT CHAIN 1..1241 FT /note="Intraflagellar transport protein 122 homolog" FT /id="PRO_0000051045" FT REPEAT 10..50 FT /note="WD 1" FT REPEAT 51..91 FT /note="WD 2" FT REPEAT 93..129 FT /note="WD 3" FT REPEAT 131..169 FT /note="WD 4" FT REPEAT 278..317 FT /note="WD 5" FT REPEAT 319..359 FT /note="WD 6" FT REPEAT 512..551 FT /note="WD 7" FT REGION 222..246 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 229..245 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..150 FT /note="Missing (in isoform 7 and isoform 8)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_056773" FT VAR_SEQ 65..116 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043310" FT VAR_SEQ 65..116 FT /note="GKRFASGSADKSVIIWTSKLEGILKYTHNDAIQCVSYNPITHQLASCSSSDF FT -> VLCIE (in isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056774" FT VAR_SEQ 66..117 FT /note="Missing (in isoform 10)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056775" FT VAR_SEQ 91 FT /note="T -> TSWSVMSSLHLHLPFLGLHKTVRVTATDKAPKGQGGRIDCLRPSVQN FT QPGQK (in isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:11242542" FT /id="VSP_045224" FT VAR_SEQ 139..247 FT /note="SWTNDGQYLALGMFNGIISIRNKNGEEKVKIERPGGSLSPIWSICWNPSSRW FT ESFWMNRENEDAEDVIVNRYIQEIPSTLKSAVYSSQGSEAEEEEPEEEDDSPRDDNL FT -> R (in isoform 10)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056776" FT VAR_SEQ 188..247 FT /note="SRWESFWMNRENEDAEDVIVNRYIQEIPSTLKSAVYSSQGSEAEEEEPEEED FT DSPRDDNL -> R (in isoform 3, isoform 4, isoform 6, isoform FT 7, isoform 9 and isoform 11)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_041161" FT VAR_SEQ 665..682 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056777" FT VAR_SEQ 930 FT /note="Q -> QA (in isoform 4, isoform 6, isoform 9 and FT isoform 10)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_043311" FT VAR_SEQ 1053..1241 FT /note="Missing (in isoform 11)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056778" FT VARIANT 7 FT /note="W -> C (in CED1; perturbed ciliary protein FT trafficking; no effect on interaction with ITF43:WDR35; FT fail to assemble IFT-A complex at the cilia base; no effect FT on ciliogenesis; dbSNP:rs267607193)" FT /evidence="ECO:0000269|PubMed:20493458, FT ECO:0000269|PubMed:29220510" FT /id="VAR_063584" FT VARIANT 322 FT /note="S -> F (in CED1; no effect on interaction with FT ITF43:WDR35; dbSNP:rs267607192)" FT /evidence="ECO:0000269|PubMed:20493458, FT ECO:0000269|PubMed:29220510" FT /id="VAR_063585" FT VARIANT 391 FT /note="V -> L (in CED1; uncertain significance; FT dbSNP:rs777418707)" FT /evidence="ECO:0000269|PubMed:26792575" FT /id="VAR_081601" FT VARIANT 495 FT /note="G -> R (in CED1; strongly decreases interaction with FT ITF43:WDR35; dbSNP:rs397515568)" FT /evidence="ECO:0000269|PubMed:23826986, FT ECO:0000269|PubMed:29220510" FT /id="VAR_081602" FT VARIANT 502 FT /note="V -> G (in CED1; strongly decreases interaction with FT ITF43:WDR35; dbSNP:rs267607191)" FT /evidence="ECO:0000269|PubMed:20493458, FT ECO:0000269|PubMed:29220510" FT /id="VAR_063586" FT VARIANT 570 FT /note="F -> C (in CED1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26792575" FT /id="VAR_081603" FT VARIANT 572 FT /note="G -> V (in CED1; decreased ciliogenesis; perturbed FT ciliary protein trafficking; strongly decreases interaction FT with ITF43:WDR35; fail to assemble IFT-A complex at the FT cilia base; dbSNP:rs786205566)" FT /evidence="ECO:0000269|PubMed:24689072, FT ECO:0000269|PubMed:29220510" FT /id="VAR_081604" FT VARIANT 712 FT /note="L -> P (in CED1; uncertain significance; FT dbSNP:rs1224050823)" FT /evidence="ECO:0000269|PubMed:26792575" FT /id="VAR_081605" FT CONFLICT 238 FT /note="E -> D (in Ref. 7; AAH28353)" FT /evidence="ECO:0000305" FT CONFLICT 273 FT /note="I -> T (in Ref. 1; AAG15427)" FT /evidence="ECO:0000305" FT CONFLICT 489 FT /note="L -> S (in Ref. 3; BAD96815)" FT /evidence="ECO:0000305" FT CONFLICT 687 FT /note="R -> Q (in Ref. 1; AAG15428)" FT /evidence="ECO:0000305" FT CONFLICT 773 FT /note="S -> P (in Ref. 4; BAG54015)" FT /evidence="ECO:0000305" FT CONFLICT 843 FT /note="E -> G (in Ref. 4; BAG54015)" FT /evidence="ECO:0000305" FT CONFLICT 907 FT /note="A -> V (in Ref. 1; AAG15428)" FT /evidence="ECO:0000305" FT CONFLICT 996 FT /note="V -> VR (in Ref. 1; AAG15427 and 3; BAG60729)" FT /evidence="ECO:0000305" FT CONFLICT 1182 FT /note="L -> F (in Ref. 3; BAA91888 and 4; BAG54015)" FT /evidence="ECO:0000305" FT STRAND 3..10 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 24..31 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 40..42 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 103..105 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 144..151 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 165..170 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 189..192 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 259..261 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 262..267 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 272..278 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 292..299 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 302..308 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 313..317 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 324..329 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 333..340 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 343..350 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 362..367 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 368..370 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 371..376 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 382..386 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 393..397 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 400..404 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 409..417 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 424..430 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 437..441 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 443..450 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 453..458 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 463..468 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 473..478 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 487..492 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 495..501 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 505..512 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 518..522 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 526..532 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 534..536 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 538..542 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 543..546 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 547..553 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 556..560 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 562..564 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 567..572 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 575..580 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 585..589 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 592..598 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 601..605 FT /evidence="ECO:0007829|PDB:8BBE" FT STRAND 607..610 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 618..626 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 630..637 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 643..655 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 659..669 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 672..685 FT /evidence="ECO:0007829|PDB:8BBE" FT TURN 686..688 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 692..702 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 706..715 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 719..728 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 732..735 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 736..738 FT /evidence="ECO:0007829|PDB:8BBE" FT HELIX 744..760 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 764..773 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 777..787 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 790..799 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 805..817 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 821..831 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 834..843 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 847..856 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 858..860 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 861..874 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 878..887 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 891..907 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 911..928 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 932..934 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 935..963 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 964..966 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 971..984 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 995..1009 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1012..1022 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1029..1043 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1047..1049 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1051..1053 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 1058..1061 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 1075..1077 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 1085..1087 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1092..1098 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1104..1110 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1150..1156 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1166..1168 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1170..1175 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 1178..1180 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1181..1184 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1193..1198 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1204..1206 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 1208..1210 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1213..1215 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1216..1226 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 1230..1232 FT /evidence="ECO:0007829|PDB:8BBG" SQ SEQUENCE 1241 AA; 141825 MW; 6C3C543369A6BDF5 CRC64; MRAVLTWRDK AEHCINDIAF KPDGTQLILA AGSRLLVYDT SDGTLLQPLK GHKDTVYCVA YAKDGKRFAS GSADKSVIIW TSKLEGILKY THNDAIQCVS YNPITHQLAS CSSSDFGLWS PEQKSVSKHK SSSKIICCSW TNDGQYLALG MFNGIISIRN KNGEEKVKIE RPGGSLSPIW SICWNPSSRW ESFWMNRENE DAEDVIVNRY IQEIPSTLKS AVYSSQGSEA EEEEPEEEDD SPRDDNLEER NDILAVADWG QKVSFYQLSG KQIGKDRALN FDPCCISYFT KGEYILLGGS DKQVSLFTKD GVRLGTVGEQ NSWVWTCQAK PDSNYVVVGC QDGTISFYQL IFSTVHGLYK DRYAYRDSMT DVIVQHLITE QKVRIKCKEL VKKIAIYRNR LAIQLPEKIL IYELYSEDLS DMHYRVKEKI IKKFECNLLV VCANHIILCQ EKRLQCLSFS GVKEREWQME SLIRYIKVIG GPPGREGLLV GLKNGQILKI FVDNLFAIVL LKQATAVRCL DMSASRKKLA VVDENDTCLV YDIDTKELLF QEPNANSVAW NTQCEDMLCF SGGGYLNIKA STFPVHRQKL QGFVVGYNGS KIFCLHVFSI SAVEVPQSAP MYQYLDRKLF KEAYQIACLG VTDTDWRELA MEALEGLDFE TAKKAFIRVQ DLRYLELISS IEERKKRGET NNDLFLADVF SYQGKFHEAA KLYKRSGHEN LALEMYTDLC MFEYAKDFLG SGDPKETKML ITKQADWARN IKEPKAAVEM YISAGEHVKA IEICGDHGWV DMLIDIARKL DKAEREPLLL CATYLKKLDS PGYAAETYLK MGDLKSLVQL HVETQRWDEA FALGEKHPEF KDDIYMPYAQ WLAENDRFEE AQKAFHKAGR QREAVQVLEQ LTNNAVAESR FNDAAYYYWM LSMQCLDIAQ DPAQKDTMLG KFYHFQRLAE LYHGYHAIHR HTEDPFSVHR PETLFNISRF LLHSLPKDTP SGISKVKILF TLAKQSKALG AYRLARHAYD KLRGLYIPAR FQKSIELGTL TIRAKPFHDS EELVPLCYRC STNNPLLNNL GNVCINCRQP FIFSASSYDV LHLVEFYLEE GITDEEAISL IDLEVLRPKR DDRQLEIANN SSQILRLVET KDSIGDEDPF TAKLSFEQGG SEFVPVVVSR LVLRSMSRRD VLIKRWPPPL RWQYFRSLLP DASITMCPSC FQMFHSEDYE LLVLQHGCCP YCRRCKDDPG P //