TTC17_DANRE
ID TTC17_DANRE Reviewed; 1198 AA.
AC E7F211;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Tetratricopeptide repeat protein 17;
DE Short=TPR repeat protein 17;
GN Name=ttc17;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24475127; DOI=10.1371/journal.pone.0086476;
RA Bontems F., Fish R.J., Borlat I., Lembo F., Chocu S., Chalmel F.,
RA Borg J.P., Pineau C., Neerman-Arbez M., Bairoch A., Lane L.;
RT "C2orf62 and TTC17 Are Involved in Actin Organization and Ciliogenesis in
RT Zebrafish and Human.";
RL PLoS ONE 9:E86476-E86476(2014).
CC -!- FUNCTION: Plays a role in primary ciliogenesis by modulating actin
CC polymerization. {ECO:0000269|PubMed:24475127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes curved
CC body, a lack of defined brain structures or necrosis in the developing
CC brain, and eye formation defects at 24 hpf. At 48 hpf, show a reduction
CC in number of ciliated cells within the olfactory organ.
CC {ECO:0000269|PubMed:24475127}.
CC -!- SIMILARITY: Belongs to the TTC17 family. {ECO:0000305}.
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DR EMBL; CR376774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E7F211; -.
DR STRING; 7955.ENSDARP00000065863; -.
DR PaxDb; E7F211; -.
DR PeptideAtlas; E7F211; -.
DR Ensembl; ENSDART00000065864; ENSDARP00000065863; ENSDARG00000044812.
DR ZFIN; ZDB-GENE-100422-15; ttc17.
DR eggNOG; KOG4507; Eukaryota.
DR GeneTree; ENSGT00390000006196; -.
DR HOGENOM; CLU_008510_0_0_1; -.
DR InParanoid; E7F211; -.
DR OMA; PFRINTF; -.
DR OrthoDB; 310025at2759; -.
DR PhylomeDB; E7F211; -.
DR TreeFam; TF315005; -.
DR PRO; PR:E7F211; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000044812; Expressed in early embryo and 25 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0044782; P:cilium organization; IMP:UniProtKB.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 3: Inferred from homology;
KW Cell membrane; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1198
FT /note="Tetratricopeptide repeat protein 17"
FT /id="PRO_0000426009"
FT REPEAT 313..346
FT /note="TPR 1"
FT REPEAT 630..663
FT /note="TPR 2"
FT REPEAT 700..733
FT /note="TPR 3"
FT REPEAT 1071..1105
FT /note="TPR 4"
FT REPEAT 1108..1141
FT /note="TPR 5"
FT REPEAT 1142..1175
FT /note="TPR 6"
FT REGION 771..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..399
FT /evidence="ECO:0000255"
FT COMPBIAS 822..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 134999 MW; D61EAE5F7FD56C7E CRC64;
MTRSFRVEWT DGRKMADDKS NSIGDNSTNK RLWSSSIRGS ALIFICALLA EPARATTHWV
VTEDGKIQQQ VDSPLNLKHP HHLVLFMQQE TRVNYLKKLE KQLVAQKIHI EENEDRDTGL
EQRHYKEDAD CVTAKVPLGD LDLYDGTFIS LESKDINPEQ FLDLMSALPP DLEKPDCAKL
LDLPYSIHAF QHLRGVQEKV NLTSPLLSKD DPIFTSLCLK LGQSVDEVGH RIHQALLKNS
SSWVLYNLAS FYWRIKNEPR RAVDCVVRAL HFSPRQHKDV ALVNMANVLH RAHFSADAAI
LAHAALDLTT DLLTSHYTLG NIYAMLGEYN HSVLCYEQAL QAQPGFEQAL RRKHAVLCQQ
KLEQRLEAQH RSLQRTLNEL KEYQKQHDHY LRQQEMLDKH KLIQEEQILR NIIHETQMAK
EAQLGNHQMC HMGQQKFTLH CPFDLPVRYH RGELFENVHY IQFGEEVSVA SSVALVSELS
VNESHSPQQS YTVSLGREPA AHWDKETTTT DESRTVLWPR RSDCAQRFPT IPPAYLLPTY
YLPPESRNLK ALNILLESIS PPPSAKMPDC SLKNVVGNRD PLESMSWALE KELRDPQAAE
VLLKRSGGRS LEQTGALIAQ ALEKMSGPRW MMQNEAGLFW RAKGNGTQAL VCLRQALHSA
PPQHRDLPLV NTANLLLHYG LHSEAHELLQ QALQINQSEP HTLLSLVNVH LSQGNLTGAL
AVFRQALSLS VHCGQCRASL PLMRCLQFYP FLYNLQHQAC SSGGACEVEE DSELEDWDTG
SSSSGRQEVW DSDAMPVSAL EDSLLFEKVV VDSNGSGEAS GQDRTREPKA EGGEEEEQDW
RLREELIGAF EGALDMNGKT GDLRGIRVLK NDRVMGARGG GPCFGNCEDD EGAEWITFQV
KRVKKPKSDA SEGWVGEGDV RQTEPTASNS ILEISGPTIP SPGPSERWKD YSSLGWPGPE
ECQRTRRVDL TTVASTWLAV SAKNIDITEH IDFATPLQEP AVEPVCNANL PASMHTLDHL
SGVANRGGIH YTGESQLREV LQNLGKDKFP SQSFEQVGTR IAKVLEKNQT SWVLSSMAAL
YWRVKGQGKR AIDCLRQALN YAPHHMKDVP LISLANIFQN ARLWEDALTV ARMAVEIAPH
FVVNHFTLAN VYIAMEEFEK AMHWYESTLK LQPEFGPAKD RLRTIQCYLL SKRDRRAP
