TALD3_HUMAN
ID TALD3_HUMAN Reviewed; 1533 AA.
AC Q9BVV6; B4DZB6; E7EWM8; J3KQH9; O60328; Q6NYC6; Q6UV20;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein TALPID3;
GN Name=KIAA0586; Synonyms=TALPID3;
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 4), AND VARIANT PRO-828.
RA Zhen Y., Huo R., Lu L., Xu M., Yin L.L., Xu Z.Y., Li J.M., Zhou Z.M.,
RA Sha J.H.;
RT "Cloning an isoform of KIAA0586 gene related to spermatogenesis.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-828.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT PRO-828.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-828.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP PRO-828.
RC TISSUE=Placenta, and Skin;
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 SUBCELLULAR LOCATION.
RX PubMed=19144723; DOI=10.1242/dev.028464;
RA Yin Y., Bangs F., Paton I.R., Prescott A., James J., Davey M.G.,
RA Whitley P., Genikhovich G., Technau U., Burt D.W., Tickle C.;
RT "The Talpid3 gene (KIAA0586) encodes a centrosomal protein that is
RT essential for primary cilia formation.";
RL Development 136:655-664(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, 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 [9]
RP FUNCTION, AND INTERACTION WITH CCP110; CEP290; CEP97 AND KIF24.
RX PubMed=24421332; DOI=10.1083/jcb.201304153;
RA Kobayashi T., Kim S., Lin Y.C., Inoue T., Dynlacht B.D.;
RT "The CP110-interacting proteins Talpid3 and Cep290 play overlapping and
RT distinct roles in cilia assembly.";
RL J. Cell Biol. 204:215-229(2014).
RN [10]
RP DEVELOPMENTAL STAGE, AND INVOLVEMENT IN SRTD14.
RX PubMed=26166481; DOI=10.1016/j.ajhg.2015.06.003;
RA Alby C., Piquand K., Huber C., Megarbane A., Ichkou A., Legendre M.,
RA Pelluard F., Encha-Ravazi F., Abi-Tayeh G., Bessieres B.,
RA El Chehadeh-Djebbar S., Laurent N., Faivre L., Sztriha L., Zombor M.,
RA Szabo H., Failler M., Garfa-Traore M., Bole C., Nitschke P., Nizon M.,
RA Elkhartoufi N., Clerget-Darpoux F., Munnich A., Lyonnet S., Vekemans M.,
RA Saunier S., Cormier-Daire V., Attie-Bitach T., Thomas S.;
RT "Mutations in KIAA0586 cause lethal ciliopathies ranging from a
RT hydrolethalus phenotype to short-rib polydactyly syndrome.";
RL Am. J. Hum. Genet. 97:311-318(2015).
RN [11]
RP INVOLVEMENT IN JBTS23.
RX PubMed=26026149; DOI=10.7554/elife.06602;
RA Roosing S., Hofree M., Kim S., Scott E., Copeland B., Romani M.,
RA Silhavy J.L., Rosti R.O., Schroth J., Mazza T., Miccinilli E., Zaki M.S.,
RA Swoboda K.J., Milisa-Drautz J., Dobyns W.B., Mikati M.A., Incecik F.,
RA Azam M., Borgatti R., Romaniello R., Boustany R.M., Clericuzio C.L.,
RA D'Arrigo S., Stroemme P., Boltshauser E., Stanzial F.,
RA Mirabelli-Badenier M., Moroni I., Bertini E., Emma F., Steinlin M.,
RA Hildebrandt F., Johnson C.A., Freilinger M., Vaux K.K., Gabriel S.B.,
RA Aza-Blanc P., Heynen-Genel S., Ideker T., Dynlacht B.D., Lee J.E.,
RA Valente E.M., Kim J., Gleeson J.G.;
RT "Functional genome-wide siRNA screen identifies KIAA0586 as mutated in
RT Joubert syndrome.";
RL Elife 4:E06602-E06602(2015).
RN [12]
RP SUBCELLULAR LOCATION, AND INVOLVEMENT IN JBTS23.
RX PubMed=26386247; DOI=10.7554/elife.08077;
RA Stephen L.A., Tawamie H., Davis G.M., Tebbe L., Nuernberg P., Nuernberg G.,
RA Thiele H., Thoenes M., Boltshauser E., Uebe S., Rompel O., Reis A.,
RA Ekici A.B., McTeir L., Fraser A.M., Hall E.A., Mill P., Daudet N.,
RA Cross C., Wolfrum U., Jamra R.A., Davey M.G., Bolz H.J.;
RT "TALPID3 controls centrosome and cell polarity and the human ortholog
RT KIAA0586 is mutated in Joubert syndrome (JBTS23).";
RL Elife 4:0-0(2015).
RN [13]
RP INVOLVEMENT IN JBTS23, AND VARIANT JBTS23 VAL-566.
RX PubMed=26096313; DOI=10.1002/humu.22821;
RG University of Washington Center for Mendelian Genomics;
RA Bachmann-Gagescu R., Phelps I.G., Dempsey J.C., Sharma V.A., Ishak G.E.,
RA Boyle E.A., Wilson M., Marques Lourenco C., Arslan M., Shendure J.,
RA Doherty D.;
RT "KIAA0586 is Mutated in Joubert Syndrome.";
RL Hum. Mutat. 36:831-835(2015).
RN [14]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN JBTS23.
RX PubMed=26386044; DOI=10.1136/jmedgenet-2015-103316;
RG NISC Comparative Sequencing Program;
RA Malicdan M.C., Vilboux T., Stephen J., Maglic D., Mian L., Konzman D.,
RA Guo J., Yildirimli D., Bryant J., Fischer R., Zein W.M., Snow J.,
RA Vemulapalli M., Mullikin J.C., Toro C., Solomon B.D., Niederhuber J.E.,
RA Gahl W.A., Gunay-Aygun M.;
RT "Mutations in human homologue of chicken talpid3 gene (KIAA0586) cause a
RT hybrid ciliopathy with overlapping features of Jeune and Joubert
RT syndromes.";
RL J. Med. Genet. 52:830-839(2015).
RN [15]
RP INVOLVEMENT IN JBTS23, AND VARIANT JBTS23 LYS-403.
RX PubMed=26429889; DOI=10.1136/jmedgenet-2015-103336;
RA Perles Z., Moon S., Ta-Shma A., Yaacov B., Francescatto L., Edvardson S.,
RA Rein A.J., Elpeleg O., Katsanis N.;
RT "A human laterality disorder caused by a homozygous deleterious mutation in
RT MMP21.";
RL J. Med. Genet. 52:840-847(2015).
CC -!- FUNCTION: Required for ciliogenesis and sonic hedgehog/SHH signaling.
CC Required for the centrosomal recruitment of RAB8A and for the targeting
CC of centriole satellite proteins to centrosomes such as of PCM1. May
CC play a role in early ciliogenesis in the disappearance of centriolar
CC satellites that preceeds ciliary vesicle formation (PubMed:24421332).
CC Involved in regulation of cell intracellular organization. Involved in
CC regulation of cell polarity (By similarity). Required for asymmetrical
CC localization of CEP120 to daughter centrioles (By similarity).
CC {ECO:0000250|UniProtKB:E9PV87, ECO:0000250|UniProtKB:Q1G7G9,
CC ECO:0000269|PubMed:24421332}.
CC -!- SUBUNIT: Interacts with CCP110, CEP290, CEP97, KIF24.
CC {ECO:0000269|PubMed:24421332}.
CC -!- INTERACTION:
CC Q9BVV6; O43303: CCP110; NbExp=6; IntAct=EBI-11286926, EBI-1566217;
CC Q9BVV6; Q8TAP6: CEP76; NbExp=2; IntAct=EBI-11286926, EBI-742887;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:19144723}. Photoreceptor inner
CC segment {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:24421332, ECO:0000269|PubMed:26386247}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:26386247}.
CC Note=Forms a ring-like structure at the extreme distal end of both
CC mother and daughter centrioles (PubMed:24421332). In photoreceptor
CC cells localized to the joint between the inner and outer segments,
CC specifically localized at the mother centriole (basal body) and the
CC adjacent centriole as well as between the two centrioles but not in the
CC connecting cilium (PubMed:26386247). {ECO:0000269|PubMed:24421332,
CC ECO:0000269|PubMed:26386247}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BVV6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVV6-2; Sequence=VSP_040642, VSP_040643;
CC Name=3;
CC IsoId=Q9BVV6-3; Sequence=VSP_046005, VSP_046006, VSP_046007;
CC Name=4;
CC IsoId=Q9BVV6-4; Sequence=VSP_046387, VSP_046006;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:26386044). Expressed
CC in photoreceptor cells (at protein level) (PubMed:26386247).
CC {ECO:0000269|PubMed:26386044, ECO:0000269|PubMed:26386247}.
CC -!- DEVELOPMENTAL STAGE: Expressed as early as 6 weeks of gestation
CC (Carnegie stage 16). Ubiquitously expressed during fetal development
CC and postnatally in all adult tissues tested.
CC {ECO:0000269|PubMed:26166481}.
CC -!- DISEASE: Joubert syndrome 23 (JBTS23) [MIM:616490]: A mild form of
CC Joubert syndrome, a disorder presenting with cerebellar ataxia,
CC oculomotor apraxia, hypotonia, neonatal breathing abnormalities and
CC psychomotor delay. Neuroradiologically, it is characterized by
CC cerebellar vermian hypoplasia/aplasia, thickened and reoriented
CC superior cerebellar peduncles, and an abnormally large interpeduncular
CC fossa, giving the appearance of a molar tooth on transaxial slices
CC (molar tooth sign). Additional variable features include retinal
CC dystrophy, renal disease, liver fibrosis, and polydactyly.
CC {ECO:0000269|PubMed:26026149, ECO:0000269|PubMed:26096313,
CC ECO:0000269|PubMed:26386044, ECO:0000269|PubMed:26386247,
CC ECO:0000269|PubMed:26429889}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Some patients with
CC biallelic KIAA0586 mutations manifest a disease phenotype with features
CC of Joubert syndrome and additional findings of a small thorax and
CC respiratory problems consistent with Jeune syndrome (Joubert-Jeune
CC ciliopathy). {ECO:0000269|PubMed:26386044}.
CC -!- DISEASE: Short-rib thoracic dysplasia 14 with polydactyly (SRTD14)
CC [MIM:616546]: A form of short-rib thoracic dysplasia, a group of
CC 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:26166481}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TALPID3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25512.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY359881; AAQ63404.1; -; mRNA.
DR EMBL; AB011158; BAA25512.2; ALT_INIT; mRNA.
DR EMBL; AK302836; BAG64028.1; -; mRNA.
DR EMBL; AL135752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80740.1; -; Genomic_DNA.
DR EMBL; BC000900; AAH00900.1; -; mRNA.
DR EMBL; BC066647; AAH66647.2; -; mRNA.
DR CCDS; CCDS45115.1; -. [Q9BVV6-2]
DR CCDS; CCDS58320.1; -. [Q9BVV6-3]
DR CCDS; CCDS58321.1; -. [Q9BVV6-1]
DR CCDS; CCDS58322.1; -. [Q9BVV6-4]
DR PIR; T00344; T00344.
DR RefSeq; NP_001231118.1; NM_001244189.1. [Q9BVV6-3]
DR RefSeq; NP_001231119.1; NM_001244190.1. [Q9BVV6-1]
DR RefSeq; NP_001231120.1; NM_001244191.1.
DR RefSeq; NP_001231121.1; NM_001244192.1. [Q9BVV6-4]
DR RefSeq; NP_001231122.1; NM_001244193.1.
DR RefSeq; NP_055564.3; NM_014749.4. [Q9BVV6-2]
DR AlphaFoldDB; Q9BVV6; -.
DR SMR; Q9BVV6; -.
DR BioGRID; 115130; 23.
DR IntAct; Q9BVV6; 16.
DR MINT; Q9BVV6; -.
DR STRING; 9606.ENSP00000346359; -.
DR iPTMnet; Q9BVV6; -.
DR PhosphoSitePlus; Q9BVV6; -.
DR BioMuta; KIAA0586; -.
DR DMDM; 327478601; -.
DR EPD; Q9BVV6; -.
DR jPOST; Q9BVV6; -.
DR MassIVE; Q9BVV6; -.
DR MaxQB; Q9BVV6; -.
DR PeptideAtlas; Q9BVV6; -.
DR PRIDE; Q9BVV6; -.
DR ProteomicsDB; 18876; -.
DR ProteomicsDB; 79236; -. [Q9BVV6-1]
DR ProteomicsDB; 79237; -. [Q9BVV6-2]
DR Antibodypedia; 21; 15 antibodies from 11 providers.
DR DNASU; 9786; -.
DR Ensembl; ENST00000261244.9; ENSP00000261244.5; ENSG00000100578.18. [Q9BVV6-2]
DR Ensembl; ENST00000354386.10; ENSP00000346359.6; ENSG00000100578.18. [Q9BVV6-3]
DR Ensembl; ENST00000423743.7; ENSP00000399427.3; ENSG00000100578.18. [Q9BVV6-4]
DR Ensembl; ENST00000619416.4; ENSP00000478083.1; ENSG00000100578.18. [Q9BVV6-1]
DR GeneID; 9786; -.
DR KEGG; hsa:9786; -.
DR UCSC; uc001xdt.5; human. [Q9BVV6-1]
DR CTD; 9786; -.
DR DisGeNET; 9786; -.
DR GeneCards; KIAA0586; -.
DR GeneReviews; KIAA0586; -.
DR HGNC; HGNC:19960; KIAA0586.
DR HPA; ENSG00000100578; Low tissue specificity.
DR MalaCards; KIAA0586; -.
DR MIM; 610178; gene.
DR MIM; 616490; phenotype.
DR MIM; 616546; phenotype.
DR neXtProt; NX_Q9BVV6; -.
DR OpenTargets; ENSG00000100578; -.
DR Orphanet; 475; Joubert syndrome.
DR Orphanet; 397715; Joubert syndrome with Jeune asphyxiating thoracic dystrophy.
DR PharmGKB; PA134992213; -.
DR VEuPathDB; HostDB:ENSG00000100578; -.
DR eggNOG; ENOG502QUXJ; Eukaryota.
DR GeneTree; ENSGT00390000012397; -.
DR InParanoid; Q9BVV6; -.
DR OrthoDB; 66287at2759; -.
DR PhylomeDB; Q9BVV6; -.
DR TreeFam; TF332939; -.
DR PathwayCommons; Q9BVV6; -.
DR SignaLink; Q9BVV6; -.
DR BioGRID-ORCS; 9786; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; KIAA0586; human.
DR GenomeRNAi; 9786; -.
DR Pharos; Q9BVV6; Tbio.
DR PRO; PR:Q9BVV6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BVV6; protein.
DR Bgee; ENSG00000100578; Expressed in right testis and 162 other tissues.
DR ExpressionAtlas; Q9BVV6; baseline and differential.
DR Genevisible; Q9BVV6; HS.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
DR InterPro; IPR029246; TALPID3.
DR PANTHER; PTHR15721; PTHR15721; 1.
DR Pfam; PF15324; TALPID3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Ciliopathy;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Joubert syndrome; Phosphoprotein; Reference proteome.
FT CHAIN 1..1533
FT /note="Protein TALPID3"
FT /id="PRO_0000050766"
FT REGION 32..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..554
FT /note="Required for centrosomal localization"
FT /evidence="ECO:0000250"
FT REGION 546..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 182..223
FT /evidence="ECO:0000255"
FT COILED 467..501
FT /evidence="ECO:0000255"
FT COMPBIAS 38..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1042
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PV87"
FT MOD_RES 1046
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PV87"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PV87"
FT MOD_RES 1063
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PV87"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PV87"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_046387"
FT VAR_SEQ 1
FT /note="M -> MKGSEVSLEKKKKIKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040642"
FT VAR_SEQ 1
FT /note="M -> MFWCGTCFVTNNMKGSEVSLEKKKKIKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046005"
FT VAR_SEQ 122
FT /note="K -> NVSLCLTGWSDHSGVITTHCSLYLLRLMRSSHLSLPSSWDYR (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_046006"
FT VAR_SEQ 538..613
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040643"
FT VAR_SEQ 1485..1532
FT /note="GKAVPLSASQMPPAKMSVMLPSVNLEDCSQSLSLSTMQEDMESSGADT ->
FT LGVHVKKVSCIGKLGLWRFVIQIISSPRWESSATLRFTDAPCQDVSDAAVSEPRGLLSV
FT SESQHNAGGHGVFGGRYLLNGKRQPAQCLCHW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046007"
FT VARIANT 403
FT /note="R -> K (in JBTS23; unknown pathological
FT significance; dbSNP:rs772739103)"
FT /evidence="ECO:0000269|PubMed:26429889"
FT /id="VAR_076328"
FT VARIANT 566
FT /note="D -> V (in JBTS23)"
FT /evidence="ECO:0000269|PubMed:26096313"
FT /id="VAR_074596"
FT VARIANT 828
FT /note="L -> P (in dbSNP:rs1748986)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9628581,
FT ECO:0000269|Ref.1, ECO:0000269|Ref.5"
FT /id="VAR_069108"
FT CONFLICT 1041
FT /note="P -> A (in Ref. 2; BAA25512, 3; BAG64028, 5;
FT EAW80740 and 6; AAH66647)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9BVV6-3:1568
FT /note="L -> P (in Ref. 3; BAG64028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1533 AA; 169307 MW; 031F5F28D63FD612 CRC64;
MPVKRLREVV SQNHGDHLVL LKDELPCVPP ALSANKRLPV GTGTSLNGTS RGSSDLTSAR
NCYQPLLENP MVSESDFSKD VAVQVLPLDK IEENNKQKAN DIFISQYTMG QKDALRTVLK
QKAQSMPVFK EVKVHLLEDA GIEKDAVTQE TRISPSGIDS ATTVAAATAA AIATAAPLIK
VQSDLEAKVN SVTELLSKLQ ETDKHLQRVT EQQTSIQRKQ EKLHCHDHEK QMNVFMEQHI
RHLEKLQQQQ IDIQTHFISA ALKTSSFQPV SMPSSRAVEK YSVKPEHPNL GSCNPSLYNT
FASKQAPLKE VEDTSFDKQK SPLETPAPRR FAPVPVSRDD ELSKRENLLE EKENMEVSCH
RGNVRLLEQI LNNNDSLTRK SESSNTTSLT RSKIGWTPEK TNRFPSCEEL ETTKVTMQKS
DDVLHDLGQK EKETNSMVQP KESLSMLKLP DLPQNSVKLQ TTNTTRSVLK DAEKILRGVQ
NNKKVLEENL EAIIRAKDGA AMYSLINALS TNREMSEKIR IRKTVDEWIK TISAEIQDEL
SRTDYEQKRF DQKNQRTKKG QNMTKDIRTN TQDKTVNKSV IPRKHSQKQI EEHFRNLPMR
GMPASSLQKE RKEGLLKATT VIQDEDYMLQ VYGKPVYQGH RSTLKKGPYL RFNSPSPKSR
PQRPKVIERV KGTKVKSIRT QTDFYATKPK KMDSKMKHSV PVLPHGDQQY LFSPSREMPT
FSGTLEGHLI PMAILLGQTQ SNSDTMPPAG VIVSKPHPVT VTTSIPPSSR KVETGVKKPN
IAIVEMKSEK KDPPQLTVQV LPSVDIDSIS NSSADVLSPL SSPKEASLPP VQTWIKTPEI
MKVDEEEVKF PGTNFDEIID VIQEEEKCDE IPDSEPILEF NRSVKADSTK YNGPPFPPVA
STFQPTADIL DKVIERKETL ENSLIQWVEQ EIMSRIISGL FPVQQQIAPS ISVSVSETSE
PLTSDIVEGT SSGALQLFVD AGVPVNSNVI KHFVNEALAE TIAVMLGDRE AKKQGPVATG
VSGDASTNET YLPARVCTPL PTPQPTPPCS PSSPAKECVL VKTPDSSPCD SDHDMAFPVK
EICAEKGDDM PAIMLVNTPT VTPTTTPPPA AAVFTPTLSD ISIDKLKVSS PELPKPWGDG
DLPLEEENPN SPQEELHPRA IVMSVAKDEE PESMDFPAQP PPPEPVPFMP FPAGTKAPSP
SQMPGSDSST LESTLSVTVT ETETLDKPIS EGEILFSCGQ KLAPKILEDI GLYLTNLNDS
LSSTLHDAVE MEDDPPSEGQ VIRMSHKKFH ADAILSFAKQ NQESAVSQQA VYHSEDLENS
VGELSEGQRP QLTAAAENIL MGHSLYMQPP VTNTQSLDQQ CDPKPLSRQF DTVSGSIYED
SCASHGPMSL GELELEPNSK LVLPTTLLTA QENDVNLPVA AEDFSQYQLK QNQDVKQVEH
KPSQSYLRVR NKSDIAPSQQ QVSPGDMDRT QIELNPYLTC VFSGGKAVPL SASQMPPAKM
SVMLPSVNLE DCSQSLSLST MQEDMESSGA DTF
