TALD3_MOUSE
ID TALD3_MOUSE Reviewed; 1520 AA.
AC E9PV87; B2RWX3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein TALPID3;
GN Name=Talpid3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1060; THR-1064; SER-1068;
RP THR-1080 AND SER-1083, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21750036; DOI=10.1242/dev.063602;
RA Bangs F., Antonio N., Thongnuek P., Welten M., Davey M.G., Briscoe J.,
RA Tickle C.;
RT "Generation of mice with functional inactivation of talpid3, a gene first
RT identified in chicken.";
RL Development 138:3261-3272(2011).
RN [5]
RP FUNCTION, AND INTERACTION WITH CEP120.
RX PubMed=25251415; DOI=10.1371/journal.pone.0107943;
RA Wu C., Yang M., Li J., Wang C., Cao T., Tao K., Wang B.;
RT "Talpid3-binding centrosomal protein Cep120 is required for centriole
RT duplication and proliferation of cerebellar granule neuron progenitors.";
RL PLoS ONE 9:E107943-E107943(2014).
RN [6]
RP FUNCTION, 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).
CC -!- FUNCTION: Required for ciliogenesis and sonic hedgehog/SHH signaling
CC (PubMed:21750036). Required for the centrosomal recruitment of RAB8A
CC and for the targeting of centriole satellite proteins to centrosomes
CC such as of PCM1. May play a role in early ciliogenesis in the
CC disappearance of centriolar satellites that preceeds ciliary vesicle
CC formation (By similarity). Involved in regulation of cell intracellular
CC organization (PubMed:26386247). Involved in regulation of cell polarity
CC (By similarity). Required for asymmetrical localization of CEP120 to
CC daughter centrioles (PubMed:25251415). {ECO:0000250|UniProtKB:Q1G7G9,
CC ECO:0000269|PubMed:21750036, ECO:0000269|PubMed:25251415,
CC ECO:0000269|PubMed:26386247}.
CC -!- SUBUNIT: Interacts with CEP120 (PubMed:25251415). Interacts with
CC CCP110, CEP290, CEP97, KIF24 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BVV6, ECO:0000269|PubMed:25251415}.
CC -!- INTERACTION:
CC E9PV87; Q7TSG1: Cep120; NbExp=3; IntAct=EBI-11692182, EBI-2553947;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q9BVV6}. Photoreceptor inner
CC segment {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:26386247}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:26386247}. Note=In photoreceptor cells
CC 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:26386247}.
CC -!- TISSUE SPECIFICITY: Expressed in photoreceptor cells (at protein
CC level). {ECO:0000269|PubMed:26386247}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice die during organogenesis, lack
CC cilia, and have randomized left-right patterning, pericardial edema and
CC hemorrhages. {ECO:0000269|PubMed:21750036}.
CC -!- SIMILARITY: Belongs to the TALPID3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI50745.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC159620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150744; AAI50745.1; ALT_INIT; mRNA.
DR CCDS; CCDS49081.1; -.
DR RefSeq; NP_001156850.1; NM_001163378.1.
DR AlphaFoldDB; E9PV87; -.
DR SMR; E9PV87; -.
DR IntAct; E9PV87; 1.
DR STRING; 10090.ENSMUSP00000118956; -.
DR iPTMnet; E9PV87; -.
DR PhosphoSitePlus; E9PV87; -.
DR jPOST; E9PV87; -.
DR MaxQB; E9PV87; -.
DR PaxDb; E9PV87; -.
DR PeptideAtlas; E9PV87; -.
DR PRIDE; E9PV87; -.
DR ProteomicsDB; 263123; -.
DR Antibodypedia; 21; 15 antibodies from 11 providers.
DR Ensembl; ENSMUST00000149564; ENSMUSP00000118956; ENSMUSG00000034601.
DR GeneID; 76967; -.
DR KEGG; mmu:76967; -.
DR UCSC; uc007nun.2; mouse.
DR MGI; MGI:1924217; 2700049A03Rik.
DR VEuPathDB; HostDB:ENSMUSG00000034601; -.
DR eggNOG; ENOG502QUXJ; Eukaryota.
DR GeneTree; ENSGT00390000012397; -.
DR InParanoid; E9PV87; -.
DR OMA; VTDVMQD; -.
DR OrthoDB; 66287at2759; -.
DR TreeFam; TF332939; -.
DR BioGRID-ORCS; 76967; 5 hits in 72 CRISPR screens.
DR ChiTaRS; 2700049A03Rik; mouse.
DR PRO; PR:E9PV87; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; E9PV87; protein.
DR Bgee; ENSMUSG00000034601; Expressed in animal zygote and 161 other tissues.
DR ExpressionAtlas; E9PV87; baseline and differential.
DR Genevisible; E9PV87; MM.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO: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:UniProtKB.
DR GO; GO:0070201; P:regulation of establishment of protein localization; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
DR InterPro; IPR029246; TALPID3.
DR PANTHER; PTHR15721; PTHR15721; 1.
DR Pfam; PF15324; TALPID3; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..1520
FT /note="Protein TALPID3"
FT /id="PRO_0000420181"
FT REGION 322..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..572
FT /note="Required for centrosomal localization"
FT /evidence="ECO:0000250"
FT REGION 568..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 487..519
FT /evidence="ECO:0000255"
FT COMPBIAS 351..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVV6"
FT MOD_RES 1060
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1064
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1080
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 1127
FT /note="A -> V (in Ref. 2; AAI50745)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="L -> F (in Ref. 2; AAI50745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1520 AA; 166721 MW; F7EA706275AF985C CRC64;
MKNVEFSLER GQRLKMPARK LREIVSPNQG NKLAVVEDEL PRVPPALAAN KRLAVETRTS
SNGTLCGSLD LTSARLYHQP LLESPPASKK SDFSKDAVVR QLPLNKTEEN NAPKANDIFI
SQYTMGQKDA LRTVLKQKAQ SMPVFKAVKV HLFEDTSTEK NTVAQETETP PNRIDSATTV
AAATAAAIAT AAPLIKVQSD LEAKVNCVGE LLTKLQETDK QLQRVTEHQA SVQSKQEKVH
CHDHDKQMNA FMEQHIRHLE KLQQQQIDIQ THFIDAALKA SSLQLGMSTS RAVGKYSGKL
GSPSVGSSVF SHNTFVSKRV PLSEDTDFDG QKSPLETPAP RRFAPVPVSR DGKITKRESP
TEEKENMEMN SPKGNVRLLE QVLNSNECLT RKTESSDITS LTQPKMGWNL EKRDSTETLH
SQIFPSSEER GTAQVPVPKY NDVVHDLGQK KQASDMLQIK QSPVTLRLSD HPHNPALLQT
TNTRSVLKDA AKILRGVQNN KKVLEENLEA IVRAKDGAAM YSFINALATN REMSEKIRIR
KQVDEWIKII SAEIQDELMR KDYEQKRFDP KNQRNKKALT MSRDIKANNQ EKTVNRSVIP
RSHYQKQTQE QFTSPPVRNL PASGPQKERS GLLKSATTLQ DEDYMLQIYG KPVYQGHRST
LKKGPYLRFS SPSPKAKPQR PRVIELVKGT KVKSAKTQTD FHAASRMKMD SKIQHPITAL
PHADQQYMVS PSREMPTVSG TLEGHLIPMA ILLGQTQSNS DSMPPAGVTV NKPRPVTVTT
SIPPASRKGN AGVKKPNVAI VEMKSEKKDP PQLSVQILPS VDIDSVSYSS TDGASSPPSP
KEASLPPLHT WIQTPDFMKV DEEEVPLPGT NFDEVIDVIQ EEEKRDEIPE CSAPMLEFNR
SVKVVPTKYN GPSFPPVVSA YHPTTDILDK VIERKETLEN SLIQWVEQEI MSRIISGLFP
LQQQARLDAS VSVSEASEPS ASDIVAGTSS GALQRMVDAR VPVNSDMVSH FVNEALTETI
AVMLADREAE RQRAAATSVP GDLSGTETNL LARVCAPVAT PQPTPPCSPS PVREHVRVKT
PDSSPCESDP DAASSIKEIR VEKGSDMPAV MLVSTPTRTP VATPPPAAAL TPTLSETSID
KLKLSSPELP KPWDSGDLPL DEENPNSLQE LPHPRAVVMS VANEEPESVD FSAQPAPPEP
APSAPLPEGT KAPSLQRVPS SGSSTLENTL STVTETETLD RHISEGEILF SCGQNLATKR
PGDLFLMNIN DSLSSTLQDA LEMEDDPPSE GQVIRRPHKK RHEDAIVALL TKQQRELLVS
QQEEDLDNSV GELSEGQRLV LKAAEDISAG PSGQMLPPTS PAEPSYQHAD PRLVLQQSDM
ASGNICEDLC ASHGPMSLRE LELQPDSNLI LPITHTTTAV SDGNLPEAAE DFSQYQQKQD
SDIKQVEHKP IQRHLTSVRN KPDSTLSQHQ GGPADLLLIA HVSPARMSVT LPSANLEDCS
QSLSTSSMHG GTESSGTDTF
