ID IF140_HUMAN Reviewed; 1462 AA. AC Q96RY7; A2A2A8; D3DU75; O60332; Q9UG52; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 182. DE RecName: Full=Intraflagellar transport protein 140 homolog {ECO:0000305}; DE AltName: Full=WD and tetratricopeptide repeats protein 2; GN Name=IFT140 {ECO:0000312|HGNC:HGNC:29077}; Synonyms=KIAA0590, WDTC2; 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), AND VARIANT VAL-1070. RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of RT the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). 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 1). RC TISSUE=Lymph; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1443, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP FUNCTION, AND 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 FUNCTION, SUBCELLULAR LOCATION, VARIANTS SRTD9 ARG-212; MET-233; MET-292; RP CYS-311; GLU-522; GLN-576 AND LYS-664, AND CHARACTERIZATION OF VARIANTS RP SRTD9 ARG-212; CYS-311 AND LYS-664. RX PubMed=22503633; DOI=10.1016/j.ajhg.2012.03.006; RA Perrault I., Saunier S., Hanein S., Filhol E., Bizet A.A., Collins F., RA Salih M.A., Gerber S., Delphin N., Bigot K., Orssaud C., Silva E., RA Baudouin V., Oud M.M., Shannon N., Le Merrer M., Roche O., Pietrement C., RA Goumid J., Baumann C., Bole-Feysot C., Nitschke P., Zahrate M., Beales P., RA Arts H.H., Munnich A., Kaplan J., Antignac C., Cormier-Daire V., RA Rozet J.M.; RT "Mainzer-Saldino syndrome is a ciliopathy caused by IFT140 mutations."; RL Am. J. Hum. Genet. 90:864-870(2012). RN [11] RP SUBCELLULAR LOCATION, VARIANTS HIS-110; THR-161; GLY-243; SER-459; HIS-514; RP GLY-787 AND ARG-1353, VARIANTS SRTD9 PHE-152; GLY-267; MET-292; GLU-522 AND RP ARG-1360, AND CHARACTERIZATION OF VARIANT SRTD9 MET-292. RX PubMed=23418020; DOI=10.1002/humu.22294; RA Schmidts M., Frank V., Eisenberger T., Al Turki S., Bizet A.A., Antony D., RA Rix S., Decker C., Bachmann N., Bald M., Vinke T., Toenshoff B., RA Di Donato N., Neuhann T., Hartley J.L., Maher E.R., Bogdanovic R., RA Peco-Antic A., Mache C., Hurles M.E., Joksic I., Guc-Scekic M., RA Dobricic J., Brankovic-Magic M., Bolz H.J., Pazour G.J., Beales P.L., RA Scambler P.J., Saunier S., Mitchison H.M., Bergmann C.; RT "Combined NGS approaches identify mutations in the intraflagellar transport RT gene IFT140 in skeletal ciliopathies with early progressive kidney RT Disease."; RL Hum. Mutat. 34:714-724(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [13] RP INTERACTION WITH TTC25. RX PubMed=25860617; DOI=10.1371/journal.pone.0124378; RA Xu Y., Cao J., Huang S., Feng D., Zhang W., Zhu X., Yan X.; RT "Characterization of tetratricopeptide repeat-containing proteins critical RT for cilia formation and function."; RL PLoS ONE 10:E0124378-E0124378(2015). RN [14] 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 [15] 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 [16] RP INVOLVEMENT IN RP80, AND VARIANTS RP80 LEU-71; ARG-329; PRO-418; RP 459-TRP--PRO-1462 DEL; MET-484; TRP-663; LYS-790; CYS-871; VAL-974; RP ARG-1276 AND PRO-1399. RX PubMed=26216056; DOI=10.1007/s00439-015-1586-x; RA Xu M., Yang L., Wang F., Li H., Wang X., Wang W., Ge Z., Wang K., Zhao L., RA Li H., Li Y., Sui R., Chen R.; RT "Mutations in human IFT140 cause non-syndromic retinal degeneration."; RL Hum. Genet. 134:1069-1078(2015). RN [17] RP INTERACTION WITH TTC21A. RX PubMed=30929735; DOI=10.1016/j.ajhg.2019.02.020; RA Liu W., He X., Yang S., Zouari R., Wang J., Wu H., Kherraf Z.E., Liu C., RA Coutton C., Zhao R., Tang D., Tang S., Lv M., Fang Y., Li W., Li H., RA Zhao J., Wang X., Zhao S., Zhang J., Arnoult C., Jin L., Zhang Z., RA Ray P.F., Cao Y., Zhang F.; RT "Bi-allelic mutations in TTC21A induce asthenoteratospermia in humans and RT mice."; RL Am. J. Hum. Genet. 104:738-748(2019). RN [18] RP VARIANT SRTD9 TRP-280. RX PubMed=24009529; DOI=10.1371/journal.pgen.1003746; RA Miller K.A., Ah-Cann C.J., Welfare M.F., Tan T.Y., Pope K., Caruana G., RA Freckmann M.L., Savarirayan R., Bertram J.F., Dobbie M.S., Bateman J.F., RA Farlie P.G.; RT "Cauli: a mouse strain with an Ift140 mutation that results in a skeletal RT ciliopathy modelling Jeune syndrome."; RL PLoS Genet. 9:E1003746-E1003746(2013). RN [19] RP VARIANT RP80 LYS-664. RX PubMed=26359340; DOI=10.1136/bjophthalmol-2015-307555; RA Bifari I.N., Elkhamary S.M., Bolz H.J., Khan A.O.; RT "The ophthalmic phenotype of IFT140-related ciliopathy ranges from isolated RT to syndromic congenital retinal dystrophy."; RL Br. J. Ophthalmol. 100:829-833(2016). RN [20] RP VARIANTS RP80 TYR-333; THR-341; PRO-440; MET-484 AND PRO-939, VARIANT RP ARG-777, CHARACTERIZATION RP80 PRO-440; MET-484; LYS-664 AND PRO-939, RP CHARACTERIZATION OF VARIANT ARG-777, AND SUBCELLULAR LOCATION. RX PubMed=26968735; DOI=10.1167/iovs.15-17976; RA Hull S., Owen N., Islam F., Tracey-White D., Plagnol V., Holder G.E., RA Michaelides M., Carss K., Raymond F.L., Rozet J.M., Ramsden S.C., RA Black G.C., Perrault I., Sarkar A., Moosajee M., Webster A.R., Arno G., RA Moore A.T.; RT "Nonsyndromic Retinal Dystrophy due to Bi-Allelic Mutations in the Ciliary RT Transport Gene IFT140."; RL Invest. Ophthalmol. Vis. Sci. 57:1053-1062(2016). RN [21] RP VARIANTS SRTD9 ARG-212 AND 760-ARG--PRO-1462 DEL. RX PubMed=28288023; DOI=10.1097/mcd.0000000000000169; RG DDD Study; RA Bayat A., Kerr B., Douzgou S.; RT "The evolving craniofacial phenotype of a patient with Sensenbrenner RT syndrome caused by IFT140 compound heterozygous mutations."; RL Clin. Dysmorphol. 26:247-251(2017). RN [22] RP VARIANT SRTD9 ARG-212, CHARACTERIZATION OF VARIANT SRTD9 ARG-212, AND RP FUNCTION. RX PubMed=28724397; DOI=10.1186/s40246-017-0111-9; RA Helm B.M., Willer J.R., Sadeghpour A., Golzio C., Crouch E., Vergano S.S., RA Katsanis N., Davis E.E.; RT "Partial uniparental isodisomy of chromosome 16 unmasks a deleterious RT biallelic mutation in IFT140 that causes Mainzer-Saldino syndrome."; RL Hum. Genomics 11:16-16(2017). CC -!- FUNCTION: Component of the IFT complex A (IFT-A), a complex required CC for retrograde ciliary transport and entry into cilia of G protein- CC coupled receptors (GPCRs) (PubMed:20889716, PubMed:22503633). Plays a CC pivotal role in proper development and function of ciliated cells CC through its role in ciliogenesis and/or cilium maintenance CC (PubMed:22503633). Required for the development and maintenance of the CC outer segments of rod and cone photoreceptor cells. Plays a role in CC maintenance and the delivery of opsin to the outer segment of CC photoreceptor cells (By similarity). {ECO:0000250|UniProtKB:E9PY46, CC ECO:0000269|PubMed:20889716, ECO:0000269|PubMed:22503633, CC ECO:0000269|PubMed:28724397}. CC -!- SUBUNIT: Component of the IFT complex A (IFT-A) (PubMed:20889716). IFT- CC A complex is divided into a core subcomplex composed of CC IFT122:IFT140:WDR19 which is associated with TULP3 and a peripheral CC subcomplex composed of IFT43:WDR35:TTC21B (PubMed:27932497, CC PubMed:29220510). Interacts (via C-terminal region) with IFT122 (via C- CC terminal region) (PubMed:29220510). Interacts with TTC25 CC (PubMed:25860617). Interacts with TTC21A (PubMed:30929735). CC {ECO:0000269|PubMed:20889716, ECO:0000269|PubMed:25860617, CC ECO:0000269|PubMed:27932497, ECO:0000269|PubMed:29220510, CC ECO:0000269|PubMed:30929735}. CC -!- INTERACTION: CC Q96RY7; Q8NEZ3: WDR19; NbExp=8; IntAct=EBI-308494, EBI-11903679; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000269|PubMed:22503633, ECO:0000269|PubMed:26968735}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:23418020}. Cell projection, cilium CC {ECO:0000269|PubMed:22503633, ECO:0000269|PubMed:26968735, CC ECO:0000269|PubMed:27932497}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96RY7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96RY7-2; Sequence=VSP_056392; CC -!- DISEASE: Short-rib thoracic dysplasia 9 with or without polydactyly CC (SRTD9) [MIM:266920]: 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. SRTD9 is CC characterized by phalangeal cone-shaped epiphyses, chronic renal CC disease, nearly constant retinal dystrophy, and mild radiographic CC abnormality of the proximal femur. Occasional features include short CC stature, cerebellar ataxia, and hepatic fibrosis. CC {ECO:0000269|PubMed:22503633, ECO:0000269|PubMed:23418020, CC ECO:0000269|PubMed:24009529, ECO:0000269|PubMed:28288023, CC ECO:0000269|PubMed:28724397}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Retinitis pigmentosa 80 (RP80) [MIM:617781]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. RP80 inheritance is autosomal CC recessive. {ECO:0000269|PubMed:26216056, ECO:0000269|PubMed:26359340, CC ECO:0000269|PubMed:26968735}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAA25516.2; 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; AB011162; BAA25516.2; ALT_INIT; mRNA. DR EMBL; AE006467; AAK61285.1; -; Genomic_DNA. DR EMBL; AL080069; CAB45696.1; -; mRNA. DR EMBL; AL031705; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z97633; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z97652; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133297; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85642.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85644.1; -; Genomic_DNA. DR EMBL; BC035577; AAH35577.1; -; mRNA. DR CCDS; CCDS10439.1; -. [Q96RY7-1] DR PIR; T00345; T00345. DR RefSeq; NP_055529.2; NM_014714.3. [Q96RY7-1] DR RefSeq; XP_006721053.1; XM_006720990.3. [Q96RY7-1] DR RefSeq; XP_006721054.1; XM_006720991.3. [Q96RY7-1] DR RefSeq; XP_016879399.1; XM_017023910.1. DR PDB; 8BBF; EM; 8.00 A; B=1-1462. DR PDB; 8BBG; EM; 3.50 A; B=1-1462. DR PDB; 8FGW; EM; 3.70 A; E=1-1462. DR PDB; 8FH3; EM; 4.30 A; E=1-1462. DR PDBsum; 8BBF; -. DR PDBsum; 8BBG; -. DR PDBsum; 8FGW; -. DR PDBsum; 8FH3; -. DR AlphaFoldDB; Q96RY7; -. DR EMDB; EMD-29073; -. DR EMDB; EMD-29078; -. DR SMR; Q96RY7; -. DR BioGRID; 115090; 77. DR ComplexPortal; CPX-5021; Intraflagellar transport complex A. DR CORUM; Q96RY7; -. DR IntAct; Q96RY7; 24. DR MINT; Q96RY7; -. DR STRING; 9606.ENSP00000406012; -. DR iPTMnet; Q96RY7; -. DR PhosphoSitePlus; Q96RY7; -. DR BioMuta; IFT140; -. DR DMDM; 74761083; -. DR EPD; Q96RY7; -. DR jPOST; Q96RY7; -. DR MassIVE; Q96RY7; -. DR MaxQB; Q96RY7; -. DR PaxDb; 9606-ENSP00000406012; -. DR PeptideAtlas; Q96RY7; -. DR ProteomicsDB; 78049; -. [Q96RY7-1] DR Pumba; Q96RY7; -. DR Antibodypedia; 23147; 96 antibodies from 21 providers. DR DNASU; 9742; -. DR Ensembl; ENST00000361339.9; ENSP00000354895.5; ENSG00000187535.14. [Q96RY7-2] DR Ensembl; ENST00000426508.7; ENSP00000406012.2; ENSG00000187535.14. [Q96RY7-1] DR GeneID; 9742; -. DR KEGG; hsa:9742; -. DR MANE-Select; ENST00000426508.7; ENSP00000406012.2; NM_014714.4; NP_055529.2. DR UCSC; uc002cmb.4; human. [Q96RY7-1] DR AGR; HGNC:29077; -. DR CTD; 9742; -. DR DisGeNET; 9742; -. DR GeneCards; IFT140; -. DR GeneReviews; IFT140; -. DR HGNC; HGNC:29077; IFT140. DR HPA; ENSG00000187535; Low tissue specificity. DR MalaCards; IFT140; -. DR MIM; 266920; phenotype. DR MIM; 614620; gene. DR MIM; 617781; phenotype. DR neXtProt; NX_Q96RY7; -. DR OpenTargets; ENSG00000187535; -. DR Orphanet; 730; Autosomal dominant polycystic kidney disease. DR Orphanet; 474; Jeune syndrome. DR Orphanet; 65; Leber congenital amaurosis. DR Orphanet; 791; Retinitis pigmentosa. DR Orphanet; 140969; Saldino-Mainzer syndrome. DR PharmGKB; PA142671665; -. DR VEuPathDB; HostDB:ENSG00000187535; -. DR eggNOG; KOG3617; Eukaryota. DR GeneTree; ENSGT00940000153417; -. DR HOGENOM; CLU_001853_0_0_1; -. DR InParanoid; Q96RY7; -. DR OMA; DFDLIWN; -. DR OrthoDB; 5479064at2759; -. DR PhylomeDB; Q96RY7; -. DR TreeFam; TF105851; -. DR PathwayCommons; Q96RY7; -. DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR SignaLink; Q96RY7; -. DR BioGRID-ORCS; 9742; 24 hits in 1154 CRISPR screens. DR ChiTaRS; IFT140; human. DR GenomeRNAi; 9742; -. DR Pharos; Q96RY7; Tbio. DR PRO; PR:Q96RY7; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q96RY7; Protein. DR Bgee; ENSG00000187535; Expressed in right uterine tube and 136 other cell types or tissues. DR ExpressionAtlas; Q96RY7; baseline and differential. DR GO; GO:0005930; C:axoneme; ISS:UniProtKB. DR GO; GO:0005814; C:centriole; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. 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:0120199; C:cone photoreceptor outer segment; IEA:Ensembl. DR GO; GO:0030991; C:intraciliary transport particle A; IDA:UniProtKB. DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl. DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl. DR GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl. DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl. DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:UniProtKB. DR GO; GO:0021532; P:neural tube patterning; IEA:Ensembl. DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl. DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl. DR GO; GO:0061512; P:protein localization to cilium; IMP:UniProtKB. DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IEA:Ensembl. DR Gene3D; 1.25.40.470; -; 2. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR15722; IFT140/172-RELATED; 1. DR PANTHER; PTHR15722:SF7; INTRAFLAGELLAR TRANSPORT PROTEIN 140 HOMOLOG; 1. DR SMART; SM00320; WD40; 3. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q96RY7; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Disease variant; KW Phosphoprotein; Reference proteome; Repeat; Retinitis pigmentosa; KW TPR repeat; WD repeat. FT CHAIN 1..1462 FT /note="Intraflagellar transport protein 140 homolog" FT /id="PRO_0000051046" FT REPEAT 4..48 FT /note="WD 1" FT REPEAT 51..90 FT /note="WD 2" FT REPEAT 93..132 FT /note="WD 3" FT REPEAT 139..188 FT /note="WD 4" FT REPEAT 221..259 FT /note="WD 5" FT REPEAT 266..305 FT /note="WD 6" FT REPEAT 322..361 FT /note="WD 7" FT REPEAT 772..807 FT /note="TPR 1" FT REPEAT 869..904 FT /note="TPR 2" FT REPEAT 906..934 FT /note="TPR 3" FT REPEAT 955..988 FT /note="TPR 4" FT REPEAT 1010..1043 FT /note="TPR 5" FT REPEAT 1078..1111 FT /note="TPR 6" FT REPEAT 1123..1156 FT /note="TPR 7" FT REPEAT 1189..1222 FT /note="TPR 8" FT REPEAT 1376..1409 FT /note="TPR 9" FT REGION 1434..1462 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1443 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 1..806 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_056392" FT VARIANT 71 FT /note="P -> L (in RP80; uncertain significance; FT dbSNP:rs772757427)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080667" FT VARIANT 110 FT /note="R -> H (in dbSNP:rs371077545)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_070999" FT VARIANT 152 FT /note="L -> F (in SRTD9; dbSNP:rs1403669200)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071000" FT VARIANT 161 FT /note="P -> T (in dbSNP:rs148462329)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071001" FT VARIANT 165 FT /note="D -> A (in dbSNP:rs35588860)" FT /id="VAR_053396" FT VARIANT 212 FT /note="G -> R (in SRTD9; partial to complete loss of basal FT body localization and increase of cytoplasmic localization; FT partial loss of function; dbSNP:rs201188361)" FT /evidence="ECO:0000269|PubMed:22503633, FT ECO:0000269|PubMed:28288023, ECO:0000269|PubMed:28724397" FT /id="VAR_068523" FT VARIANT 233 FT /note="I -> M (in SRTD9)" FT /evidence="ECO:0000269|PubMed:22503633" FT /id="VAR_068524" FT VARIANT 243 FT /note="E -> G (in dbSNP:rs539181813)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071002" FT VARIANT 267 FT /note="E -> G (in SRTD9; disease phenotype consistent with FT Mainzer-Saldino syndrome)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071003" FT VARIANT 279 FT /note="R -> P (in dbSNP:rs4786350)" FT /id="VAR_053397" FT VARIANT 280 FT /note="R -> Q (in dbSNP:rs35404373)" FT /id="VAR_053398" FT VARIANT 280 FT /note="R -> W (in SRTD9; dbSNP:rs8058674)" FT /evidence="ECO:0000269|PubMed:24009529" FT /id="VAR_078817" FT VARIANT 292 FT /note="V -> M (in SRTD9; impairs centrosomal localization; FT dbSNP:rs431905521)" FT /evidence="ECO:0000269|PubMed:22503633, FT ECO:0000269|PubMed:23418020" FT /id="VAR_068525" FT VARIANT 311 FT /note="Y -> C (in SRTD9; partial to complete loss of basal FT body localization and increase of cytoplasmic localization; FT dbSNP:rs387907193)" FT /evidence="ECO:0000269|PubMed:22503633" FT /id="VAR_068526" FT VARIANT 329 FT /note="C -> R (in RP80; uncertain significance; FT dbSNP:rs1441549097)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080668" FT VARIANT 333 FT /note="C -> Y (in RP80; uncertain significance; FT dbSNP:rs773372123)" FT /evidence="ECO:0000269|PubMed:26968735" FT /id="VAR_080669" FT VARIANT 341 FT /note="A -> T (in RP80; uncertain significance; FT dbSNP:rs200292484)" FT /evidence="ECO:0000269|PubMed:26968735" FT /id="VAR_080670" FT VARIANT 398 FT /note="V -> I (in dbSNP:rs34762152)" FT /id="VAR_053399" FT VARIANT 418 FT /note="A -> P (in RP80; uncertain significance; FT dbSNP:rs770890983)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080671" FT VARIANT 440 FT /note="L -> P (in RP80; uncertain significance; also found FT in a patient with Leber congenital amaurosis and renal FT failure; uncertain significance; decreased localization to FT the basal body; dbSNP:rs1555491448)" FT /evidence="ECO:0000269|PubMed:26968735" FT /id="VAR_080672" FT VARIANT 451 FT /note="A -> V (in dbSNP:rs8060532)" FT /id="VAR_053400" FT VARIANT 459..1462 FT /note="Missing (in RP80; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080673" FT VARIANT 459 FT /note="W -> S (in dbSNP:rs778311141)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071004" FT VARIANT 484 FT /note="T -> M (in RP80; uncertain significance; decreased FT localization to the basal body; dbSNP:rs758052634)" FT /evidence="ECO:0000269|PubMed:26216056, FT ECO:0000269|PubMed:26968735" FT /id="VAR_080674" FT VARIANT 514 FT /note="L -> H (in dbSNP:rs150903791)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071005" FT VARIANT 522 FT /note="G -> E (in SRTD9; dbSNP:rs199826737)" FT /evidence="ECO:0000269|PubMed:22503633, FT ECO:0000269|PubMed:23418020" FT /id="VAR_068527" FT VARIANT 561 FT /note="S -> N (in dbSNP:rs8050974)" FT /id="VAR_062098" FT VARIANT 576 FT /note="R -> Q (in SRTD9; dbSNP:rs373111085)" FT /evidence="ECO:0000269|PubMed:22503633" FT /id="VAR_068528" FT VARIANT 621 FT /note="R -> Q (in dbSNP:rs11648609)" FT /id="VAR_053401" FT VARIANT 663 FT /note="C -> W (in RP80; uncertain significance; FT dbSNP:rs781117803)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080675" FT VARIANT 664 FT /note="E -> K (in SRTD9 and RP80; uncertain significance; FT partial to complete loss of basal body localization and FT increase of cytoplasmic localization; dbSNP:rs387907192)" FT /evidence="ECO:0000269|PubMed:22503633, FT ECO:0000269|PubMed:26359340, ECO:0000269|PubMed:26968735" FT /id="VAR_068529" FT VARIANT 670 FT /note="P -> S (in dbSNP:rs34900355)" FT /id="VAR_053402" FT VARIANT 760..1462 FT /note="Missing (in SRTD9; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28288023" FT /id="VAR_080676" FT VARIANT 777 FT /note="L -> R (no effect on localization to the basal body; FT dbSNP:rs34535263)" FT /evidence="ECO:0000269|PubMed:26968735" FT /id="VAR_080677" FT VARIANT 787 FT /note="D -> G (in dbSNP:rs144938800)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071006" FT VARIANT 790 FT /note="E -> K (in RP80; uncertain significance; FT dbSNP:rs751323480)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080678" FT VARIANT 871 FT /note="R -> C (in RP80; uncertain significance; FT dbSNP:rs767213195)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080679" FT VARIANT 939 FT /note="S -> P (in RP80; uncertain significance; decreased FT localization to the basal body; dbSNP:rs145549969)" FT /evidence="ECO:0000269|PubMed:26968735" FT /id="VAR_080680" FT VARIANT 974 FT /note="A -> V (in RP80; uncertain significance; FT dbSNP:rs745576178)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080681" FT VARIANT 1070 FT /note="A -> V (in dbSNP:rs2235638)" FT /evidence="ECO:0000269|PubMed:9628581" FT /id="VAR_053403" FT VARIANT 1276 FT /note="G -> R (in RP80; uncertain significance; FT dbSNP:rs200065348)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080682" FT VARIANT 1353 FT /note="P -> R (in dbSNP:rs146666187)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071007" FT VARIANT 1360 FT /note="C -> R (in SRTD9; disease phenotype consistent with FT Mainzer-Saldino syndrome; dbSNP:rs431905520)" FT /evidence="ECO:0000269|PubMed:23418020" FT /id="VAR_071008" FT VARIANT 1399 FT /note="L -> P (in RP80; uncertain significance; FT dbSNP:rs559371453)" FT /evidence="ECO:0000269|PubMed:26216056" FT /id="VAR_080683" FT CONFLICT 542 FT /note="H -> L (in Ref. 1; BAA25516)" FT /evidence="ECO:0000305" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 17..23 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 25..35 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 41..47 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 71..80 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 90..93 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 94..97 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 115..122 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 126..132 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 143..147 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 166..174 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 178..184 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 205..209 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 212..217 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 223..228 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 233..239 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 244..249 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 266..272 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 296..304 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 305..308 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 317..319 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 327..333 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 334..337 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 338..343 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 346..354 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 365..368 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 381..386 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 389..391 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 393..399 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 401..408 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 417..423 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 437..441 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 447..451 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 453..459 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 461..470 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 473..481 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 487..490 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 493..498 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 501..505 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 511..516 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 519..521 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 524..530 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 533..538 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 541..547 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 549..552 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 554..561 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 562..565 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 571..577 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 581..589 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 597..603 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 604..607 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 608..613 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 614..616 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 619..623 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 625..627 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 633..635 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 641..645 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 647..653 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 660..666 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 677..679 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 691..700 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 701..703 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 704..712 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 717..724 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 727..732 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 734..737 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 738..740 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 754..758 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 760..762 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 770..785 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 788..794 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 795..797 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 801..814 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 817..826 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 830..839 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 845..855 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 859..868 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 872..882 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 885..894 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 897..899 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 900..913 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 917..926 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 930..937 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 942..952 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 955..967 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 971..980 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 984..993 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 997..1007 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1010..1022 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1026..1035 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1039..1049 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1052..1061 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1064..1077 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1081..1090 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1094..1103 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1107..1116 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1123..1135 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1139..1148 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1152..1161 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1168..1173 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1181..1183 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1185..1201 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1205..1214 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1219..1228 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1231..1241 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1244..1254 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1259..1261 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1263..1275 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1279..1295 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1300..1316 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1322..1348 FT /evidence="ECO:0007829|PDB:8BBG" FT TURN 1349..1351 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1353..1364 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1369..1371 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1375..1388 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1392..1405 FT /evidence="ECO:0007829|PDB:8BBG" FT STRAND 1407..1409 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1411..1414 FT /evidence="ECO:0007829|PDB:8BBG" FT HELIX 1417..1424 FT /evidence="ECO:0007829|PDB:8BBG" SQ SEQUENCE 1462 AA; 165193 MW; 2F3CCBD998F80E3B CRC64; MALYYDHQIE APDAAGSPSF ISWHPVHPFL AVAYISTTST GSVDIYLEQG ECVPDTHVER PFRVASLCWH PTRLVLAVGW ETGEVTVFNK QDKEQHTMPL THTADITVLR WSPSGNCLLS GDRLGVLLLW RLDQRGRVQG TPLLKHEYGK HLTHCIFRLP PPGEDLVQLA KAAVSGDEKA LDMFNWKKSS SGSLLKMGSH EGLLFFVSLM DGTVHYVDEK GKTTQVVSAD STIQMLFYME KREALVVVTE NLRLSLYTVP PEGKAEEVMK VKLSGKTGRR ADIALIEGSL LVMAVGEAAL RFWDIERGEN YILSPDEKFG FEKGENMNCV CYCKVKGLLA AGTDRGRVAM WRKVPDFLGS PGAEGKDRWA LQTPTELQGN ITQIQWGSRK NLLAVNSVIS VAILSERAMS SHFHQQVAAM QVSPSLLNVC FLSTGVAHSL RTDMHISGVF ATKDAVAVWN GRQVAIFELS GAAIRSAGTF LCETPVLAMH EENVYTVESN RVQVRTWQGT VKQLLLFSET EGNPCFLDIC GNFLVVGTDL AHFKSFDLSR REAKAHCSCR SLAELVPGVG GIASLRCSSS GSTISILPSK ADNSPDSKIC FYDVEMDTVT VFDFKTGQID RRETLSFNEQ ETNKSHLFVD EGLKNYVPVN HFWDQSEPRL FVCEAVQETP RSQPQSANGQ PQDGRAGPAA DVLILSFFIS EEHGFLLHES FPRPATSHSL LGMEVPYYYF TRKPEEADRE DEVEPGCHHI PQMVSRRPLR DFVGLEDCDK ATRDAMLHFS FFVTIGDMDE AFKSIKLIKS EAVWENMARM CVKTQRLDVA KVCLGNMGHA RGARALREAE QEPELEARVA VLATQLGMLE DAEQLYRKCK RHDLLNKFYQ AAGRWQEALQ VAEHHDRVHL RSTYHRYAGH LEASADCSRA LSYYEKSDTH RFEVPRMLSE DLPSLELYVN KMKDKTLWRW WAQYLESQGE MDAALHYYEL ARDHFSLVRI HCFQGNVQKA AQIANETGNL AASYHLARQY ESQEEVGQAV HFYTRAQAFK NAIRLCKENG LDDQLMNLAL LSSPEDMIEA ARYYEEKGVQ MDRAVMLYHK AGHFSKALEL AFATQQFVAL QLIAEDLDET SDPALLARCS DFFIEHSQYE RAVELLLAAR KYQEALQLCL GQNMSITEEM AEKMTVAKDS SDLPEESRRE LLEQIADCCM RQGSYHLATK KYTQAGNKLK AMRALLKSGD TEKITFFASV SRQKEIYIMA ANYLQSLDWR KEPEIMKNII GFYTKGRALD LLAGFYDACA QVEIDEYQNY DKAHGALTEA YKCLAKAKAK SPLDQETRLA QLQSRMALVK RFIQARRTYT EDPKESIKQC ELLLEEPDLD STIRIGDVYG FLVEHYVRKE EYQTAYRFLE EMRRRLPLAN MSYYVSPQAV DAVHRGLGLP LPRTVPEQVR HNSMEDAREL DEEVVEEADD DP //