TULP3_HUMAN
ID TULP3_HUMAN Reviewed; 442 AA.
AC O75386; B3KNB7; B7Z6A2; D3DUQ4; F8WBZ9; Q8N5B0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Tubby-related protein 3 {ECO:0000305};
DE AltName: Full=Tubby-like protein 3;
GN Name=TULP3 {ECO:0000312|HGNC:HGNC:12425}; Synonyms=TUBL3;
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 1), AND TISSUE SPECIFICITY.
RX PubMed=9828123; DOI=10.1006/geno.1998.5567;
RA Nishina P.M., North M.A., Ikeda A., Yan Y., Naggert J.K.;
RT "Molecular characterization of a novel tubby gene family member, TULP3, in
RT mouse and humans.";
RL Genomics 54:215-220(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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]
RP FUNCTION IN G-PROTEIN SIGNALING, AND SUBCELLULAR LOCATION.
RX PubMed=11375483; DOI=10.1126/science.1061233;
RA Santagata S., Boggon T.J., Baird C.L., Gomez C.A., Zhao J., Shan W.S.,
RA Myszka D.G., Shapiro L.;
RT "G-protein signaling through tubby proteins.";
RL Science 292:2041-2050(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE IFT-A COMPLEX, AND
RP MUTAGENESIS OF 24-ARG--LEU-34 AND 268-LYS--ARG-270.
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 [8]
RP ASSOCIATION WITH 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 [9]
RP FUNCTION.
RX PubMed=31761534; DOI=10.1016/j.cell.2019.11.005;
RA Hilgendorf K.I., Johnson C.T., Mezger A., Rice S.L., Norris A.M.,
RA Demeter J., Greenleaf W.J., Reiter J.F., Kopinke D., Jackson P.K.;
RT "Omega-3 Fatty Acids Activate Ciliary FFAR4 to Control Adipogenesis.";
RL Cell 179:1289-1305(2019).
CC -!- FUNCTION: Negative regulator of the Shh signaling transduction pathway:
CC recruited to primary cilia via association with the IFT complex A (IFT-
CC A) and is required for recruitment of G protein-coupled receptor GPR161
CC to cilia, a promoter of PKA-dependent basal repression machinery in Shh
CC signaling. Binds to phosphorylated inositide (phosphoinositide) lipids.
CC Both IFT-A- and phosphoinositide-binding properties are required to
CC regulate ciliary G protein-coupled receptor trafficking. Not involved
CC in ciliogenesis. During adipogenesis, regulates ciliary trafficking of
CC FFAR4 in preadipocytes. {ECO:0000269|PubMed:11375483,
CC ECO:0000269|PubMed:20889716, ECO:0000269|PubMed:31761534}.
CC -!- SUBUNIT: Associates with the IFT complex A (IFT-A).
CC {ECO:0000269|PubMed:20889716, ECO:0000269|PubMed:27932497}.
CC -!- INTERACTION:
CC O75386; Q6NXT1: ANKRD54; NbExp=8; IntAct=EBI-5357290, EBI-10102770;
CC O75386; Q9BYV9: BACH2; NbExp=4; IntAct=EBI-5357290, EBI-1642333;
CC O75386; O75031: HSF2BP; NbExp=3; IntAct=EBI-5357290, EBI-7116203;
CC O75386; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-5357290, EBI-10172150;
CC O75386; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-5357290, EBI-10172290;
CC O75386; P43360: MAGEA6; NbExp=7; IntAct=EBI-5357290, EBI-1045155;
CC O75386; O43586: PSTPIP1; NbExp=6; IntAct=EBI-5357290, EBI-1050964;
CC O75386; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-5357290, EBI-1378139;
CC O75386; Q93009: USP7; NbExp=2; IntAct=EBI-5357290, EBI-302474;
CC O75386; P12520: vpr; Xeno; NbExp=2; IntAct=EBI-5357290, EBI-6164519;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell membrane. Cell projection, cilium
CC {ECO:0000269|PubMed:27932497}. Cytoplasm {ECO:0000250}. Secreted
CC {ECO:0000250}. Note=Does not have a cleavable signal peptide and is
CC secreted by a non-conventional pathway (By similarity). Translocates
CC from the plasma membrane to the nucleus upon activation of guanine
CC nucleotide-binding protein G(q) subunit alpha. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75386-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75386-2; Sequence=VSP_054752;
CC Name=3;
CC IsoId=O75386-3; Sequence=VSP_055761, VSP_055762, VSP_055763;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in testis, ovaries,
CC thyroid, and spinal chord. {ECO:0000269|PubMed:9828123}.
CC -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
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DR EMBL; AF045583; AAC95431.1; -; mRNA.
DR EMBL; AK024246; BAG51279.1; -; mRNA.
DR EMBL; AK299990; BAH13188.1; -; mRNA.
DR EMBL; AC005911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88876.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88877.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88878.1; -; Genomic_DNA.
DR EMBL; BC032587; AAH32587.1; -; mRNA.
DR CCDS; CCDS53737.1; -. [O75386-2]
DR CCDS; CCDS8519.1; -. [O75386-1]
DR RefSeq; NP_001153880.1; NM_001160408.1. [O75386-2]
DR RefSeq; NP_003315.2; NM_003324.4. [O75386-1]
DR AlphaFoldDB; O75386; -.
DR SMR; O75386; -.
DR BioGRID; 113140; 338.
DR IntAct; O75386; 112.
DR MINT; O75386; -.
DR STRING; 9606.ENSP00000380321; -.
DR iPTMnet; O75386; -.
DR PhosphoSitePlus; O75386; -.
DR BioMuta; TULP3; -.
DR EPD; O75386; -.
DR jPOST; O75386; -.
DR MassIVE; O75386; -.
DR MaxQB; O75386; -.
DR PaxDb; O75386; -.
DR PeptideAtlas; O75386; -.
DR PRIDE; O75386; -.
DR ProteomicsDB; 30981; -.
DR ProteomicsDB; 49959; -. [O75386-1]
DR ProteomicsDB; 6762; -.
DR Antibodypedia; 10458; 269 antibodies from 23 providers.
DR DNASU; 7289; -.
DR Ensembl; ENST00000397132.6; ENSP00000380321.2; ENSG00000078246.17. [O75386-2]
DR Ensembl; ENST00000448120.7; ENSP00000410051.2; ENSG00000078246.17. [O75386-1]
DR Ensembl; ENST00000540184.5; ENSP00000444110.1; ENSG00000078246.17. [O75386-3]
DR GeneID; 7289; -.
DR KEGG; hsa:7289; -.
DR MANE-Select; ENST00000448120.7; ENSP00000410051.2; NM_003324.5; NP_003315.2.
DR UCSC; uc001qlj.3; human. [O75386-1]
DR CTD; 7289; -.
DR DisGeNET; 7289; -.
DR GeneCards; TULP3; -.
DR HGNC; HGNC:12425; TULP3.
DR HPA; ENSG00000078246; Low tissue specificity.
DR MIM; 604730; gene.
DR neXtProt; NX_O75386; -.
DR OpenTargets; ENSG00000078246; -.
DR PharmGKB; PA37087; -.
DR VEuPathDB; HostDB:ENSG00000078246; -.
DR eggNOG; KOG2502; Eukaryota.
DR GeneTree; ENSGT00940000158155; -.
DR HOGENOM; CLU_1570112_0_0_1; -.
DR InParanoid; O75386; -.
DR OMA; CVVFHEE; -.
DR OrthoDB; 1445357at2759; -.
DR PhylomeDB; O75386; -.
DR TreeFam; TF314076; -.
DR PathwayCommons; O75386; -.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR SignaLink; O75386; -.
DR SIGNOR; O75386; -.
DR BioGRID-ORCS; 7289; 11 hits in 1098 CRISPR screens.
DR ChiTaRS; TULP3; human.
DR GenomeRNAi; 7289; -.
DR Pharos; O75386; Tbio.
DR PRO; PR:O75386; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75386; protein.
DR Bgee; ENSG00000078246; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; O75386; baseline and differential.
DR Genevisible; O75386; HS.
DR GO; GO:0097731; C:9+0 non-motile cilium; IDA:MGI.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:MGI.
DR GO; GO:0120160; F:intraciliary transport particle A binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; NAS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0060434; P:bronchus morphogenesis; IEA:Ensembl.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IEA:Ensembl.
DR GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0061548; P:ganglion development; IEA:Ensembl.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:UniProtKB.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
DR GO; GO:0021914; P:negative regulation of smoothened signaling pathway involved in ventral spinal cord patterning; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0061512; P:protein localization to cilium; IDA:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
DR Gene3D; 3.20.90.10; -; 1.
DR InterPro; IPR025659; Tubby-like_C.
DR InterPro; IPR000007; Tubby_C.
DR InterPro; IPR018066; Tubby_C_CS.
DR InterPro; IPR005398; Tubby_N.
DR Pfam; PF01167; Tub; 1.
DR Pfam; PF16322; Tub_N; 1.
DR PRINTS; PR01573; SUPERTUBBY.
DR PRINTS; PR01574; TUBBYPROTEIN.
DR SUPFAM; SSF54518; SSF54518; 1.
DR PROSITE; PS01200; TUB_1; 1.
DR PROSITE; PS01201; TUB_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium; Cytoplasm;
KW Developmental protein; Membrane; Nucleus; Reference proteome; Secreted.
FT CHAIN 1..442
FT /note="Tubby-related protein 3"
FT /id="PRO_0000186470"
FT REGION 23..68
FT /note="Required for association with the IFT complex A
FT (IFT-A)"
FT REGION 101..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055761"
FT VAR_SEQ 165..189
FT /note="DTGTSGSATAAQPADNLLGDIDDLE -> FSSFCQKTEDTGYRHFRFCYCRP
FT TS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055762"
FT VAR_SEQ 190..442
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055763"
FT VAR_SEQ 437..442
FT /note="SKLACE -> KCIQTLRMQELCELHRQHHSAASLVHRTVCQRWVGHPWRLLP
FT QTSLLWTDLSPPPVVPAPHQISM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054752"
FT MUTAGEN 24..34
FT /note="RQAKLDYQRLL->AQAAADYAALA: In mut12; abolishes
FT association with the IFT complex A (IFT-A) without
FT affecting phosphoinositide binding. Impaired localization
FT to cilia."
FT /evidence="ECO:0000269|PubMed:20889716"
FT MUTAGEN 268..270
FT /note="KLR->ALA: In TULP3KR; abolishes phosphoinositide
FT binding and impairs localization to cilia. Still associates
FT with the IFT complex A (IFT-A)."
FT /evidence="ECO:0000269|PubMed:20889716"
FT CONFLICT 168..181
FT /note="TSGSATAAQPADNL -> IPVLLLPPNQLITF (in Ref. 1;
FT AAC95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="D -> Y (in Ref. 5; AAH32587)"
FT /evidence="ECO:0000305"
FT CONFLICT 193..194
FT /note="YS -> LV (in Ref. 1; AAC95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..226
FT /note="PTYYMYLE -> SHLLYVLG (in Ref. 1; AAC95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="I -> L (in Ref. 1; AAC95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..431
FT /note="GIG -> AIS (in Ref. 1; AAC95431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49642 MW; 13DBC83305BFAC1D CRC64;
MEASRCRLSP SGDSVFHEEM MKMRQAKLDY QRLLLEKRQR KKRLEPFMVQ PNPEARLRRA
KPRASDEQTP LVNCHTPHSN VILHGIDGPA AVLKPDEVHA PSVSSSVVEE DAENTVDTAS
KPGLQERLQK HDISESVNFD EETDGISQSA CLERPNSASS QNSTDTGTSG SATAAQPADN
LLGDIDDLED FVYSPAPQGV TVRCRIIRDK RGMDRGLFPT YYMYLEKEEN QKIFLLAARK
RKKSKTANYL ISIDPVDLSR EGESYVGKLR SNLMGTKFTV YDRGICPMKG RGLVGAAHTR
QELAAISYET NVLGFKGPRK MSVIIPGMTL NHKQIPYQPQ NNHDSLLSRW QNRTMENLVE
LHNKAPVWNS DTQSYVLNFR GRVTQASVKN FQIVHKNDPD YIVMQFGRVA DDVFTLDYNY
PLCAVQAFGI GLSSFDSKLA CE
