ID IFT81_HUMAN Reviewed; 676 AA. AC Q8WYA0; Q2YDY1; Q8NB51; Q9BSV2; Q9UNY8; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=Intraflagellar transport protein 81 homolog; DE AltName: Full=Carnitine deficiency-associated protein expressed in ventricle 1; DE Short=CDV-1; GN Name=IFT81; Synonyms=CDV1; 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 {ECO:0000312|EMBL:AAL50343.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDV-1R). RC TISSUE=Lymphocyte; RX PubMed=11130971; DOI=10.1007/s003350010207; RA Higashi M., Kobayashi K., Iijima M., Wakana S., Horiuchi M., Yasuda T., RA Yoshida G., Kanmura Y., Saheki T.; RT "Genomic organization and mapping of mouse CDV (carnitine deficiency- RT associated gene expressed in ventricle)-1 and its related CDV-1R gene."; RL Mamm. Genome 11:1053-1057(2000). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDV-1R), AND TISSUE SPECIFICITY. RC TISSUE=Testis {ECO:0000269|PubMed:12549821}; RX PubMed=12549821; DOI=10.1023/a:1021232518628; RA Peng J., Yu L., Horiuchi M., Zhang P., Huang X., Zhang Y., Li D., RA Jalil M.A., Zhao S.; RT "Identification of human CDV-1R and mouse Cdv-1R, two novel proteins with RT putative signal peptides, especially highly expressed in testis and RT increased with the male sex maturation."; RL Mol. Biol. Rep. 29:353-362(2002). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDV-1). RA Hu G.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305} 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND CDV-1). RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAH29349.1}, and Uterus RC {ECO:0000312|EMBL:AAH04536.2}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-676 (ISOFORM CDV-1R). RC TISSUE=Fetal brain {ECO:0000269|PubMed:14702039}; 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 [7] RP INTERACTION WITH IFT74. RX PubMed=15955805; DOI=10.1074/jbc.m505062200; RA Lucker B.F., Behal R.H., Qin H., Siron L.C., Taggart W.D., Rosenbaum J.L., RA Cole D.G.; RT "Characterization of the intraflagellar transport complex B core: direct RT interaction of the IFT81 and IFT74/72 subunits."; RL J. Biol. Chem. 280:27688-27696(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE IFT COMPLEX B, RP INTERACTION WITH TUBULIN AND IFT74, AND MUTAGENESIS OF 73-LYS--LYS-75 AND RP 113-LYS-LYS-114. RX PubMed=23990561; DOI=10.1126/science.1240985; RA Bhogaraju S., Cajanek L., Fort C., Blisnick T., Weber K., Taschner M., RA Mizuno N., Lamla S., Bastin P., Nigg E.A., Lorentzen E.; RT "Molecular basis of tubulin transport within the cilium by IFT74 and RT IFT81."; RL Science 341:1009-1012(2013). RN [12] RP FUNCTION, INVOLVEMENT IN SRTD19, AND VARIANTS SRTD19 PHE-29; LEU-435 DEL; RP 262-LEU--LEU-676 DEL AND 512-ARG--LEU-676 DEL. RX PubMed=27666822; DOI=10.1038/srep34232; RA Duran I., Taylor S.P., Zhang W., Martin J., Forlenza K.N., Spiro R.P., RA Nickerson D.A., Bamshad M., Cohn D.H., Krakow D.; RT "Destabilization of the IFT-B cilia core complex due to mutations in IFT81 RT causes a spectrum of short-rib polydactyly syndrome."; RL Sci. Rep. 6:34232-34232(2016). RN [13] RP INTERACTION WITH RABL2B AND IFT74. RX PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016; RA Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J., Jackson P.K.; RT "The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar RT transport at the ciliary base."; RL Dev. Cell 42:1-15(2017). RN [14] RP INTERACTION WITH RABL2B AND IFT74. RX PubMed=28428259; DOI=10.1091/mbc.e17-01-0017; RA Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.; RT "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and RT participates in ciliary assembly."; RL Mol. Biol. Cell 28:1652-1666(2017). CC -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B: CC together with IFT74, forms a tubulin-binding module that specifically CC mediates transport of tubulin within the cilium. Binds tubulin via its CC CH (calponin-homology)-like region (PubMed:23990561). Required for CC ciliogenesis (PubMed:27666822, PubMed:23990561). Required for proper CC regulation of SHH signaling (PubMed:27666822). Plays an important role CC during spermatogenesis by modulating the assembly and elongation of the CC sperm flagella (By similarity). {ECO:0000250|UniProtKB:O35594, CC ECO:0000269|PubMed:23990561, ECO:0000269|PubMed:27666822}. CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20, CC IFT22, IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, CC IFT81, and IFT88 (PubMed:23990561). Interacts with IFT74; the CC interaction is direct: within the IFT complex B, IFT74 and IFT81 CC mediate the transport of tubulin within the cilium (PubMed:15955805, CC PubMed:23990561). Interacts with tubulin; the interaction is direct CC (PubMed:23990561). Interacts with IFT57 and IFT70B (By similarity). CC Interacts with RABL2/RABL2A; binding is equal in the presence of GTP or CC GDP (By similarity). Interacts with IFT88 (PubMed:23990561). Interacts CC (via the IFT74/IFT81 heterodimer) with RABL2B (PubMed:28625565, CC PubMed:28428259). Interacts with CFAP61 (By similarity). CC {ECO:0000250|UniProtKB:E9Q9D5, ECO:0000250|UniProtKB:O35594, CC ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:23990561, CC ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565}. CC -!- INTERACTION: CC Q8WYA0-3; Q96LB3-2: IFT74; NbExp=3; IntAct=EBI-11944793, EBI-12066130; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium CC {ECO:0000305|PubMed:23990561}. Cytoplasm CC {ECO:0000250|UniProtKB:O35594}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=CDV-1R {ECO:0000269|PubMed:11130971, ECO:0000269|PubMed:12549821}; CC IsoId=Q8WYA0-1; Sequence=Displayed; CC Name=2 {ECO:0000305}; CC IsoId=Q8WYA0-3; Sequence=VSP_050695, VSP_050696; CC Name=CDV-1; CC IsoId=Q8WYA0-4; Sequence=VSP_018784; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, moderately in ovary, CC heart, liver, skeletal muscle, kidney and pancreas, low in prostate, CC brain, placenta and lung and not detected in spleen, thymus, small CC intestine and colon. Isoform CDV-1R is abundantly expressed in testis. CC {ECO:0000269|PubMed:12549821}. CC -!- DOMAIN: The CH (calponin-homology)-like region shows high similarity to CC a CH (calponin-homology) domain and mediates binding to the globular CC domain of tubulin. {ECO:0000269|PubMed:23990561}. CC -!- DISEASE: Short-rib thoracic dysplasia 19 with or without polydactyly CC (SRTD19) [MIM:617895]: 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. CC {ECO:0000269|PubMed:27666822}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform CDV-1]: Produced by alternative initiation at CC Met-570 of isoform CDV-1R. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the IFT81 family. {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; AF250326; AAL50343.1; -; mRNA. DR EMBL; AF332010; AAO32947.1; -; mRNA. DR EMBL; AF139540; AAP97269.1; -; mRNA. DR EMBL; AF078932; AAD48091.1; -; mRNA. DR EMBL; CH471054; EAW97898.1; -; Genomic_DNA. DR EMBL; BC004536; AAH04536.2; -; mRNA. DR EMBL; BC029349; AAH29349.1; -; mRNA. DR EMBL; BC108257; AAI08258.1; -; mRNA. DR EMBL; AK091549; BAC03690.1; ALT_SEQ; mRNA. DR CCDS; CCDS41831.1; -. [Q8WYA0-1] DR CCDS; CCDS9142.1; -. [Q8WYA0-3] DR RefSeq; NP_001137251.1; NM_001143779.1. [Q8WYA0-1] DR RefSeq; NP_001334875.1; NM_001347946.1. [Q8WYA0-3] DR RefSeq; NP_054774.2; NM_014055.3. [Q8WYA0-1] DR RefSeq; NP_113661.2; NM_031473.3. [Q8WYA0-3] DR RefSeq; XP_016874706.1; XM_017019217.1. [Q8WYA0-1] DR AlphaFoldDB; Q8WYA0; -. DR SMR; Q8WYA0; -. DR BioGRID; 118802; 71. DR ComplexPortal; CPX-5022; Intraflagellar transport complex B. DR CORUM; Q8WYA0; -. DR IntAct; Q8WYA0; 46. DR MINT; Q8WYA0; -. DR STRING; 9606.ENSP00000242591; -. DR TCDB; 1.X.1.1.1; the intraflagellar transporter-a complex (ift-a) family. DR iPTMnet; Q8WYA0; -. DR PhosphoSitePlus; Q8WYA0; -. DR BioMuta; IFT81; -. DR DMDM; 48474907; -. DR EPD; Q8WYA0; -. DR jPOST; Q8WYA0; -. DR MassIVE; Q8WYA0; -. DR MaxQB; Q8WYA0; -. DR PaxDb; 9606-ENSP00000242591; -. DR PeptideAtlas; Q8WYA0; -. DR ProteomicsDB; 75140; -. [Q8WYA0-1] DR ProteomicsDB; 75141; -. [Q8WYA0-3] DR ProteomicsDB; 75142; -. [Q8WYA0-4] DR Pumba; Q8WYA0; -. DR Antibodypedia; 18491; 184 antibodies from 26 providers. DR DNASU; 28981; -. DR Ensembl; ENST00000242591.10; ENSP00000242591.5; ENSG00000122970.16. [Q8WYA0-1] DR Ensembl; ENST00000361948.8; ENSP00000355372.4; ENSG00000122970.16. [Q8WYA0-3] DR Ensembl; ENST00000552912.5; ENSP00000449718.1; ENSG00000122970.16. [Q8WYA0-1] DR GeneID; 28981; -. DR KEGG; hsa:28981; -. DR MANE-Select; ENST00000242591.10; ENSP00000242591.5; NM_014055.4; NP_054774.2. DR UCSC; uc001tqh.4; human. [Q8WYA0-1] DR AGR; HGNC:14313; -. DR CTD; 28981; -. DR DisGeNET; 28981; -. DR GeneCards; IFT81; -. DR HGNC; HGNC:14313; IFT81. DR HPA; ENSG00000122970; Low tissue specificity. DR MalaCards; IFT81; -. DR MIM; 605489; gene. DR MIM; 617895; phenotype. DR neXtProt; NX_Q8WYA0; -. DR OpenTargets; ENSG00000122970; -. DR PharmGKB; PA26349; -. DR VEuPathDB; HostDB:ENSG00000122970; -. DR eggNOG; ENOG502QSBR; Eukaryota. DR GeneTree; ENSGT00390000000999; -. DR HOGENOM; CLU_017012_1_0_1; -. DR InParanoid; Q8WYA0; -. DR OMA; WILTHME; -. DR OrthoDB; 276306at2759; -. DR PhylomeDB; Q8WYA0; -. DR TreeFam; TF314635; -. DR PathwayCommons; Q8WYA0; -. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR SignaLink; Q8WYA0; -. DR BioGRID-ORCS; 28981; 20 hits in 1151 CRISPR screens. DR ChiTaRS; IFT81; human. DR GeneWiki; IFT81; -. DR GenomeRNAi; 28981; -. DR Pharos; Q8WYA0; Tbio. DR PRO; PR:Q8WYA0; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q8WYA0; Protein. DR Bgee; ENSG00000122970; Expressed in bronchial epithelial cell and 184 other cell types or tissues. DR ExpressionAtlas; Q8WYA0; baseline and differential. DR GO; GO:0005814; C:centriole; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IBA:GO_Central. DR GO; GO:0036064; C:ciliary basal body; IDA:CACAO. DR GO; GO:0097542; C:ciliary tip; TAS:Reactome. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal. DR GO; GO:0031514; C:motile cilium; ISS:BHF-UCL. DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl. DR GO; GO:0097228; C:sperm principal piece; IEA:Ensembl. DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0035720; P:intraciliary anterograde transport; NAS:ComplexPortal. DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central. DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IMP:UniProtKB. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:UniProtKB. DR GO; GO:0120316; P:sperm flagellum assembly; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR Gene3D; 1.10.418.70; Intraflagellar transport protein 81, N-terminal domain; 1. DR InterPro; IPR029600; IFT81. DR InterPro; IPR041146; IFT81_CH. DR InterPro; IPR043016; IFT81_N_sf. DR PANTHER; PTHR15614; INTRAFLAGELLAR TRANSPORT PROTEIN 81 HOMOLOG; 1. DR PANTHER; PTHR15614:SF2; INTRAFLAGELLAR TRANSPORT PROTEIN 81 HOMOLOG; 1. DR Pfam; PF18383; IFT81_CH; 1. DR Genevisible; Q8WYA0; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative initiation; Alternative splicing; Cell projection; KW Ciliopathy; Cilium; Cilium biogenesis/degradation; Coiled coil; Cytoplasm; KW Differentiation; Disease variant; Phosphoprotein; Reference proteome; KW Spermatogenesis. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..676 FT /note="Intraflagellar transport protein 81 homolog" FT /id="PRO_0000020916" FT REGION 2..121 FT /note="CH (calponin-homology)-like region" FT COILED 132..258 FT /evidence="ECO:0000255" FT COILED 306..389 FT /evidence="ECO:0000255" FT COILED 416..456 FT /evidence="ECO:0000255" FT COILED 490..622 FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 61 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18088087" FT VAR_SEQ 1..569 FT /note="Missing (in isoform CDV-1)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_018784" FT VAR_SEQ 397..431 FT /note="FKRYVNKLRSKSTVFKKKHQIIAELKAEFGLLQRT -> RQDLTLSPRLECG FT GVIMAYCSLKLLGSSDPPTSAS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_050695" FT VAR_SEQ 432..676 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_050696" FT VARIANT 29 FT /note="L -> F (in SRTD19; dbSNP:rs751222088)" FT /evidence="ECO:0000269|PubMed:27666822" FT /id="VAR_080485" FT VARIANT 262..676 FT /note="Missing (in SRTD19)" FT /evidence="ECO:0000269|PubMed:27666822" FT /id="VAR_080487" FT VARIANT 435 FT /note="Missing (in SRTD19; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27666822" FT /id="VAR_080793" FT VARIANT 512..676 FT /note="Missing (in SRTD19)" FT /evidence="ECO:0000269|PubMed:27666822" FT /id="VAR_080488" FT MUTAGEN 73..75 FT /note="KYK->EYE: Abolishes tubulin-binding and impaired FT ciliogenesis; when associated with 113-E-E-114." FT /evidence="ECO:0000269|PubMed:23990561" FT MUTAGEN 113..114 FT /note="KK->EE: Abolishes tubulin-binding and impaired FT ciliogenesis; when associated with 73-E--E-75." FT /evidence="ECO:0000269|PubMed:23990561" FT CONFLICT 59 FT /note="E -> K (in Ref. 6; BAC03690)" FT /evidence="ECO:0000305" SQ SEQUENCE 676 AA; 79746 MW; E5EBD887A6BF953E CRC64; MSDQIKFIMD SLNKEPFRKN YNLITFDSLE PMQLLQVLSD VLAEIDPKQL VDIREEMPEQ TAKRMLSLLG ILKYKPSGNA TDMSTFRQGL VIGSKPVIYP VLHWLLQRTN ELKKRAYLAR FLIKLEVPSE FLQDETVADT NKQYEELMEA FKTLHKEYEQ LKISGFSTAE IRKDISAMEE EKDQLIKRVE HLKKRVETAQ NHQWMLKIAR QLRVEKEREE YLAQQKQEQK NQLFHAVQRL QRVQNQLKSM RQAAADAKPE SLMKRLEEEI KFNLYMVTEK FPKELENKKK ELHFLQKVVS EPAMGHSDLL ELESKINEIN TEINQLIEKK MMRNEPIEGK LSLYRQQASI ISRKKEAKAE ELQEAKEKLA SLEREASVKR NQTREFDGTE VLKGDEFKRY VNKLRSKSTV FKKKHQIIAE LKAEFGLLQR TEELLKQRHE NIQQQLQTME EKKGISGYSY TQEELERVSA LKSEVDEMKG RTLDDMSEMV KKLYSLVSEK KSALASVIKE LRQLRQKYQE LTQECDEKKS QYDSCAAGLE SNRSKLEQEV RRLREECLQE ESRYHYTNCM IKNLEVQLRR ATDEMKAYIS SDQQEKRKAI REQYTKNTAE QENLGKKLRE KQKVIRESHG PNMKQAKMWR DLEQLMECKK QCFLKQQSQT SIGQVIQEGG EDRLIL //