IFT81_HUMAN
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 03-AUG-2022, entry version 161.
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
RC Uterus {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, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT80, 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 TTC30B (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). {ECO:0000250|UniProtKB:E9Q9D5,
CC ECO:0000250|UniProtKB:O35594, ECO:0000269|PubMed:15955805,
CC ECO:0000269|PubMed:23990561, ECO:0000269|PubMed:28428259,
CC 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 mediated 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}.
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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; 65.
DR ComplexPortal; CPX-5022; IFT-B complex.
DR CORUM; Q8WYA0; -.
DR IntAct; Q8WYA0; 45.
DR MINT; Q8WYA0; -.
DR STRING; 9606.ENSP00000242591; -.
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; Q8WYA0; -.
DR PeptideAtlas; Q8WYA0; -.
DR PRIDE; Q8WYA0; -.
DR ProteomicsDB; 75140; -. [Q8WYA0-1]
DR ProteomicsDB; 75141; -. [Q8WYA0-3]
DR ProteomicsDB; 75142; -. [Q8WYA0-4]
DR Antibodypedia; 18491; 160 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 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 PhylomeDB; Q8WYA0; -.
DR TreeFam; TF314635; -.
DR PathwayCommons; Q8WYA0; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q8WYA0; -.
DR BioGRID-ORCS; 28981; 18 hits in 1075 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 182 other tissues.
DR ExpressionAtlas; Q8WYA0; baseline and differential.
DR Genevisible; Q8WYA0; HS.
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; IC: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; -; 1.
DR InterPro; IPR029600; IFT81.
DR InterPro; IPR041146; IFT81_CH.
DR InterPro; IPR043016; IFT81_N_sf.
DR PANTHER; PTHR15614; PTHR15614; 1.
DR Pfam; PF18383; IFT81_CH; 1.
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; unknown pathological
FT 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
