TTC8_HUMAN
ID TTC8_HUMAN Reviewed; 541 AA.
AC Q8TAM2; A6NFG2; B3KWA5; Q67B97; Q86SY0; Q86TV9; Q86U26; Q8NDH9; Q96DG8;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Tetratricopeptide repeat protein 8;
DE Short=TPR repeat protein 8;
DE AltName: Full=Bardet-Biedl syndrome 8 protein;
GN Name=TTC8; Synonyms=BBS8;
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] (ISOFORMS 3 AND 4), VARIANT BBS8 197-GLU-TYR-198
RP DEL, AND VARIANT RP51 38-ASP--HIS-47 DEL.
RX PubMed=14520415; DOI=10.1038/nature02030;
RA Ansley S.J., Badano J.L., Blacque O.E., Hill J., Hoskins B.E., Leitch C.C.,
RA Kim J.C., Ross A.J., Eichers E.R., Teslovich T.M., Mah A.K., Johnsen R.C.,
RA Cavender J.C., Lewis R.A., Leroux M.R., Beales P.L., Katsanis N.;
RT "Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl
RT syndrome.";
RL Nature 425:628-633(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 102-541 (ISOFORM 3), AND VARIANT RP51
RP 38-ASP--HIS-47 DEL.
RC TISSUE=Cervix carcinoma, Neuroblastoma, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT RP51 38-ASP--HIS-47
RP DEL.
RA Smaoui N., Li S., Belghith N., Chaabouni M., M'Rad R., Maazoul F.,
RA Chaabouni H., Hejtmancik J.F.;
RT "Mutations in BBS8, a novel gene containing TPR motifs causes Bardet-Biedl
RT syndrome.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Amygdala;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT RP51
RP 38-ASP--HIS-47 DEL.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT RP51
RP 38-ASP--HIS-47 DEL.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT RP51
RP 38-ASP--HIS-47 DEL.
RC TISSUE=Brain, Pituitary, and Placenta;
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 [9]
RP INVOLVEMENT IN BBS8.
RX PubMed=16308660; DOI=10.1007/s10038-005-0320-2;
RA Stoetzel C., Laurier V., Faivre L., Megarbane A., Perrin-Schmitt F.,
RA Verloes A., Bonneau D., Mandel J.-L., Cossee M., Dollfus H.;
RT "BBS8 is rarely mutated in a cohort of 128 Bardet-Biedl syndrome
RT families.";
RL J. Hum. Genet. 51:81-84(2006).
RN [10]
RP INTERACTION WITH CCDC28B.
RX PubMed=16327777; DOI=10.1038/nature04370;
RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S.,
RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.;
RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome.";
RL Nature 439:326-330(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17574030; DOI=10.1016/j.cell.2007.03.053;
RA Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J., Merdes A.,
RA Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C., Jackson P.K.;
RT "A core complex of BBS proteins cooperates with the GTPase Rab8 to promote
RT ciliary membrane biogenesis.";
RL Cell 129:1201-1213(2007).
RN [12]
RP FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
RA Sheffield V.C.;
RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and
RT Smoothened.";
RL PLoS Genet. 7:E1002358-E1002358(2011).
RN [13]
RP INTERACTION WITH PKD1.
RX PubMed=24939912; DOI=10.1093/hmg/ddu267;
RA Su X., Driscoll K., Yao G., Raed A., Wu M., Beales P.L., Zhou J.;
RT "Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of
RT polycystic kidney disease 1 protein.";
RL Hum. Mol. Genet. 23:5441-5451(2014).
RN [14]
RP VARIANT RP51 38-ASP--HIS-47 DEL.
RX PubMed=20451172; DOI=10.1016/j.ajhg.2010.04.001;
RA Riazuddin S.A., Iqbal M., Wang Y., Masuda T., Chen Y., Bowne S.,
RA Sullivan L.S., Waseem N.H., Bhattacharya S., Daiger S.P., Zhang K.,
RA Khan S.N., Riazuddin S., Hejtmancik J.F., Sieving P.A., Zack D.J.,
RA Katsanis N.;
RT "A splice-site mutation in a retina-specific exon of BBS8 causes
RT nonsyndromic retinitis pigmentosa.";
RL Am. J. Hum. Genet. 86:805-812(2010).
CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC required for sorting of specific membrane proteins to the primary
CC cilia. The BBSome complex is required for ciliogenesis but is
CC dispensable for centriolar satellite function. This ciliogenic function
CC is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC the primary cilium and promotes extension of the ciliary membrane.
CC Firstly the BBSome associates with the ciliary membrane and binds to
CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC carrier vesicles to the base of the ciliary membrane. The BBSome
CC complex, together with the LTZL1, controls SMO ciliary trafficking and
CC contributes to the sonic hedgehog (SHH) pathway regulation. Required
CC for proper BBSome complex assembly and its ciliary localization.
CC {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with PCM1. Interacts with
CC CCDC28B. Interacts with PKD1 (PubMed:24939912).
CC {ECO:0000269|PubMed:16327777, ECO:0000269|PubMed:17574030,
CC ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:24939912}.
CC -!- INTERACTION:
CC Q8TAM2; Q3SYG4: BBS9; NbExp=2; IntAct=EBI-2892638, EBI-2826852;
CC Q8TAM2; Q15051: IQCB1; NbExp=5; IntAct=EBI-2892638, EBI-2805823;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17574030}. Cell projection,
CC cilium membrane {ECO:0000269|PubMed:17574030}. Cytoplasm
CC {ECO:0000269|PubMed:22072986}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:17574030}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q8VD72}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8TAM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAM2-2; Sequence=VSP_007821;
CC Name=3;
CC IsoId=Q8TAM2-3; Sequence=VSP_007822, VSP_007823;
CC Name=4;
CC IsoId=Q8TAM2-4; Sequence=VSP_007823;
CC Name=5;
CC IsoId=Q8TAM2-6; Sequence=VSP_041151, VSP_041152;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Retinitis pigmentosa 51 (RP51) [MIM:613464]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:14520415,
CC ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
CC ECO:0000269|PubMed:20451172, ECO:0000269|Ref.2, ECO:0000269|Ref.3,
CC ECO:0000269|Ref.7}. Note=The disease is caused by variants affecting
CC the gene represented in this entry.
CC -!- DISEASE: Bardet-Biedl syndrome 8 (BBS8) [MIM:615985]: A syndrome
CC characterized by usually severe pigmentary retinopathy, early-onset
CC obesity, polydactyly, hypogenitalism, renal malformation and
CC intellectual disability. Secondary features include diabetes mellitus,
CC hypertension and congenital heart disease. Bardet-Biedl syndrome
CC inheritance is autosomal recessive, but three mutated alleles (two at
CC one locus, and a third at a second locus) may be required for clinical
CC manifestation of some forms of the disease.
CC {ECO:0000269|PubMed:14520415, ECO:0000269|PubMed:16308660}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD61928.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=CAD62360.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY366523; AAR02192.1; -; mRNA.
DR EMBL; AY366524; AAR02193.1; -; mRNA.
DR EMBL; BX161472; CAD61928.1; ALT_SEQ; mRNA.
DR EMBL; BX248071; CAD62360.1; ALT_INIT; mRNA.
DR EMBL; BX248248; CAD62576.1; -; mRNA.
DR EMBL; AY373972; AAR19043.1; -; mRNA.
DR EMBL; AK124675; BAG54067.1; -; mRNA.
DR EMBL; AL833901; CAD38757.2; -; mRNA.
DR EMBL; AL121768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81400.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81402.1; -; Genomic_DNA.
DR EMBL; BC001563; AAH01563.1; -; mRNA.
DR EMBL; BC026351; AAH26351.1; -; mRNA.
DR EMBL; BC095433; AAH95433.1; -; mRNA.
DR CCDS; CCDS32137.1; -. [Q8TAM2-4]
DR RefSeq; NP_001275710.1; NM_001288781.1.
DR RefSeq; NP_001275711.1; NM_001288782.1.
DR RefSeq; NP_001275712.1; NM_001288783.1.
DR RefSeq; NP_653197.2; NM_144596.3. [Q8TAM2-4]
DR RefSeq; NP_938051.1; NM_198309.3.
DR RefSeq; NP_938052.1; NM_198310.3.
DR RefSeq; XP_006720098.1; XM_006720035.1.
DR RefSeq; XP_006720100.1; XM_006720037.2.
DR RefSeq; XP_011534734.1; XM_011536432.1.
DR AlphaFoldDB; Q8TAM2; -.
DR SMR; Q8TAM2; -.
DR BioGRID; 125811; 26.
DR ComplexPortal; CPX-1908; BBSome complex.
DR CORUM; Q8TAM2; -.
DR DIP; DIP-60359N; -.
DR IntAct; Q8TAM2; 16.
DR STRING; 9606.ENSP00000482306; -.
DR iPTMnet; Q8TAM2; -.
DR PhosphoSitePlus; Q8TAM2; -.
DR BioMuta; TTC8; -.
DR DMDM; 308153511; -.
DR EPD; Q8TAM2; -.
DR jPOST; Q8TAM2; -.
DR MassIVE; Q8TAM2; -.
DR MaxQB; Q8TAM2; -.
DR PaxDb; Q8TAM2; -.
DR PeptideAtlas; Q8TAM2; -.
DR PRIDE; Q8TAM2; -.
DR ProteomicsDB; 73893; -. [Q8TAM2-1]
DR ProteomicsDB; 73894; -. [Q8TAM2-2]
DR ProteomicsDB; 73895; -. [Q8TAM2-3]
DR ProteomicsDB; 73896; -. [Q8TAM2-4]
DR ProteomicsDB; 73897; -. [Q8TAM2-6]
DR Antibodypedia; 141; 215 antibodies from 30 providers.
DR DNASU; 123016; -.
DR Ensembl; ENST00000354441.10; ENSP00000346427.6; ENSG00000165533.19. [Q8TAM2-2]
DR Ensembl; ENST00000380656.7; ENSP00000370031.2; ENSG00000165533.19. [Q8TAM2-4]
DR GeneID; 123016; -.
DR KEGG; hsa:123016; -.
DR MANE-Select; ENST00000380656.7; ENSP00000370031.2; NM_144596.4; NP_653197.2. [Q8TAM2-4]
DR UCSC; uc001xxi.5; human. [Q8TAM2-1]
DR CTD; 123016; -.
DR DisGeNET; 123016; -.
DR GeneCards; TTC8; -.
DR GeneReviews; TTC8; -.
DR HGNC; HGNC:20087; TTC8.
DR HPA; ENSG00000165533; Low tissue specificity.
DR MalaCards; TTC8; -.
DR MIM; 608132; gene.
DR MIM; 613464; phenotype.
DR MIM; 615985; phenotype.
DR neXtProt; NX_Q8TAM2; -.
DR OpenTargets; ENSG00000165533; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA134877629; -.
DR VEuPathDB; HostDB:ENSG00000165533; -.
DR eggNOG; KOG1129; Eukaryota.
DR GeneTree; ENSGT00940000156816; -.
DR InParanoid; Q8TAM2; -.
DR OrthoDB; 637646at2759; -.
DR PhylomeDB; Q8TAM2; -.
DR TreeFam; TF314892; -.
DR PathwayCommons; Q8TAM2; -.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; Q8TAM2; -.
DR SIGNOR; Q8TAM2; -.
DR BioGRID-ORCS; 123016; 4 hits in 1076 CRISPR screens.
DR ChiTaRS; TTC8; human.
DR GeneWiki; TTC8; -.
DR GenomeRNAi; 123016; -.
DR Pharos; Q8TAM2; Tbio.
DR PRO; PR:Q8TAM2; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8TAM2; protein.
DR Bgee; ENSG00000165533; Expressed in left ovary and 174 other tissues.
DR ExpressionAtlas; Q8TAM2; baseline and differential.
DR Genevisible; Q8TAM2; HS.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL.
DR GO; GO:0060170; C:ciliary membrane; IDA:ComplexPortal.
DR GO; GO:0005929; C:cilium; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097730; C:non-motile cilium; IBA:GO_Central.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; TAS:BHF-UCL.
DR GO; GO:0048560; P:establishment of anatomical structure orientation; IMP:BHF-UCL.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0021772; P:olfactory bulb development; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0061326; P:renal tubule development; IEA:Ensembl.
DR GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR GO; GO:0050893; P:sensory processing; TAS:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR028796; BBS8.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44177; PTHR44177; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Bardet-Biedl syndrome; Cell membrane;
KW Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Disease variant; Intellectual disability;
KW Membrane; Obesity; Protein transport; Reference proteome; Repeat;
KW Retinitis pigmentosa; TPR repeat; Transport.
FT CHAIN 1..541
FT /note="Tetratricopeptide repeat protein 8"
FT /id="PRO_0000106388"
FT REPEAT 14..47
FT /note="TPR 1"
FT REPEAT 251..284
FT /note="TPR 2"
FT REPEAT 285..317
FT /note="TPR 3"
FT REPEAT 318..351
FT /note="TPR 4"
FT REPEAT 352..385
FT /note="TPR 5"
FT REPEAT 386..419
FT /note="TPR 6"
FT REPEAT 423..456
FT /note="TPR 7"
FT REPEAT 457..490
FT /note="TPR 8"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 39..329
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_007821"
FT VAR_SEQ 164..193
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14520415,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_007822"
FT VAR_SEQ 194..196
FT /note="ALF -> VCT (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041151"
FT VAR_SEQ 197..541
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041152"
FT VAR_SEQ 209..234
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14520415,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_007823"
FT VARIANT 38..47
FT /note="Missing (in RP51)"
FT /id="VAR_063705"
FT VARIANT 197..198
FT /note="Missing (in BBS8)"
FT /evidence="ECO:0000269|PubMed:14520415"
FT /id="VAR_017247"
FT CONFLICT 177
FT /note="L -> I (in Ref. 4; BAG54067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 61534 MW; 013CFB0FDEBF385B CRC64;
MSSEMEPLLL AWSYFRRRKF QLCADLCTQM LEKSPYDQEP DPELPVHQAA WILKARALTE
MVYIDEIDVD QEGIAEMMLD ENAIAQVPRP GTSLKLPGTN QTGGPSQAVR PITQAGRPIT
GFLRPSTQSG RPGTMEQAIR TPRTAYTARP ITSSSGRFVR LGTASMLTSP DGPFINLSRL
NLTKYSQKPK LAKALFEYIF HHENDVKTIH LEDVVLHLGI YPFLLRNKNH IEKNALDLAA
LSTEHSQYKD WWWKVQIGKC YYRLGMYREA EKQFKSALKQ QEMVDTFLYL AKVYVSLDQP
VTALNLFKQG LDKFPGEVTL LCGIARIYEE MNNMSSAAEY YKEVLKQDNT HVEAIACIGS
NHFYSDQPEI ALRFYRRLLQ MGIYNGQLFN NLGLCCFYAQ QYDMTLTSFE RALSLAENEE
EAADVWYNLG HVAVGIGDTN LAHQCFRLAL VNNNNHAEAY NNLAVLEMRK GHVEQARALL
QTASSLAPHM YEPHFNFATI SDKIGDLQRS YVAAQKSEAA FPDHVDTQHL IKQLRQHFAM
L
