TTC8_MOUSE
ID TTC8_MOUSE Reviewed; 515 AA.
AC Q8VD72; Q9DCP7;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Tetratricopeptide repeat protein 8;
DE Short=TPR repeat protein 8;
DE AltName: Full=Bardet-Biedl syndrome 8 protein homolog;
GN Name=Ttc8; Synonyms=Bbs8;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 DEVELOPMENTAL STAGE.
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 [4]
RP IDENTIFICATION IN THE BBSOME COMPLEX.
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 [5]
RP IDENTIFICATION OF ISOFORM 2, AND TISSUE SPECIFICITY.
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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=25243405; DOI=10.1371/journal.pone.0108470;
RA Broekhuis J.R., Verhey K.J., Jansen G.;
RT "Regulation of cilium length and intraflagellar transport by the RCK-
RT kinases ICK and MOK in renal epithelial cells.";
RL PLoS ONE 9:E108470-E108470(2014).
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 (By
CC similarity). {ECO:0000250}.
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. {ECO:0000250|UniProtKB:Q8TAM2,
CC ECO:0000269|PubMed:22072986}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TAM2}. Cell
CC projection, cilium membrane {ECO:0000250|UniProtKB:Q8TAM2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TAM2}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q8TAM2}. Cell projection, cilium
CC {ECO:0000269|PubMed:25243405}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VD72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VD72-2; Sequence=VSP_007825;
CC -!- TISSUE SPECIFICITY: Isoform 1 is retina-specific whereas isoform 2 is
CC ubiquitously expressed. {ECO:0000269|PubMed:20451172}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 12 dpc in ciliated structures,
CC including maturing (stages X and XI) spermatids, the connecting cilium
CC of the retina and bronchial epithelial cells. At 14 and 16 dpc,
CC detected in the telencephalon, with prominent expression at the
CC developing ependymal cell layer and the olfactory epithelium.
CC {ECO:0000269|PubMed:14520415}.
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DR EMBL; AK002597; BAB22218.1; -; mRNA.
DR EMBL; AK081697; BAC38298.1; -; mRNA.
DR EMBL; BC017523; AAH17523.1; -; mRNA.
DR CCDS; CCDS26101.1; -. [Q8VD72-2]
DR CCDS; CCDS26102.1; -. [Q8VD72-1]
DR RefSeq; NP_083829.1; NM_029553.3. [Q8VD72-2]
DR RefSeq; NP_938053.1; NM_198311.1. [Q8VD72-1]
DR AlphaFoldDB; Q8VD72; -.
DR SMR; Q8VD72; -.
DR ComplexPortal; CPX-1909; BBSome complex.
DR DIP; DIP-60354N; -.
DR IntAct; Q8VD72; 4.
DR STRING; 10090.ENSMUSP00000078148; -.
DR iPTMnet; Q8VD72; -.
DR PhosphoSitePlus; Q8VD72; -.
DR MaxQB; Q8VD72; -.
DR PaxDb; Q8VD72; -.
DR PRIDE; Q8VD72; -.
DR ProteomicsDB; 300158; -. [Q8VD72-1]
DR ProteomicsDB; 300159; -. [Q8VD72-2]
DR Antibodypedia; 141; 215 antibodies from 30 providers.
DR DNASU; 76260; -.
DR Ensembl; ENSMUST00000079146; ENSMUSP00000078148; ENSMUSG00000021013. [Q8VD72-1]
DR Ensembl; ENSMUST00000085109; ENSMUSP00000082190; ENSMUSG00000021013. [Q8VD72-2]
DR GeneID; 76260; -.
DR KEGG; mmu:76260; -.
DR UCSC; uc007oro.2; mouse. [Q8VD72-1]
DR UCSC; uc007orp.2; mouse. [Q8VD72-2]
DR CTD; 123016; -.
DR MGI; MGI:1923510; Ttc8.
DR VEuPathDB; HostDB:ENSMUSG00000021013; -.
DR eggNOG; KOG1129; Eukaryota.
DR GeneTree; ENSGT00940000156816; -.
DR HOGENOM; CLU_025029_0_0_1; -.
DR InParanoid; Q8VD72; -.
DR OMA; QMGVNSA; -.
DR OrthoDB; 637646at2759; -.
DR PhylomeDB; Q8VD72; -.
DR TreeFam; TF314892; -.
DR Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR BioGRID-ORCS; 76260; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ttc8; mouse.
DR PRO; PR:Q8VD72; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8VD72; protein.
DR Bgee; ENSMUSG00000021013; Expressed in retinal neural layer and 239 other tissues.
DR ExpressionAtlas; Q8VD72; baseline and differential.
DR Genevisible; Q8VD72; MM.
DR GO; GO:0034464; C:BBSome; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0097730; C:non-motile cilium; IBA:GO_Central.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IGI:MGI.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:FlyBase.
DR GO; GO:0048560; P:establishment of anatomical structure orientation; ISO:MGI.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IMP:MGI.
DR GO; GO:0061326; P:renal tubule development; IMP:MGI.
DR GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR Gene3D; 1.25.40.10; -; 2.
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; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Membrane;
KW Protein transport; Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..515
FT /note="Tetratricopeptide repeat protein 8"
FT /id="PRO_0000106389"
FT REPEAT 4..37
FT /note="TPR 1"
FT REPEAT 225..258
FT /note="TPR 2"
FT REPEAT 259..291
FT /note="TPR 3"
FT REPEAT 292..325
FT /note="TPR 4"
FT REPEAT 326..359
FT /note="TPR 5"
FT REPEAT 360..393
FT /note="TPR 6"
FT REPEAT 397..430
FT /note="TPR 7"
FT REPEAT 432..464
FT /note="TPR 8"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..109
FT /note="Polar residues"
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 38..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007825"
SQ SEQUENCE 515 AA; 58440 MW; 9A8ACDF59BB641C1 CRC64;
MGSEMEPLLR AWSYFRRRKF QLCADLCTQM LEKSPYDQEP APDLPVSQAA WILKARALTE
MVYIDEIDVD QEGIAEMILD ENAIAQVPRP GTSLKLPGTN QTGGPTQAVR PITQAGRPIT
GFLRPSTQSG RPGTMEQAIR TPRTAYTARP ITSSSGRFVR LGTASMLTSP DGPFINLSRL
NLTKYSQKPK LAKALFEYIL HHENDVKMAL DLASLSTEYS QYKDWWWKVQ IGKCYYRLGM
YREAEKQFKS ALKQQEMVDT FLYLAKVYII LDQPVTALNL FKQGLDKFPG EVTLLCGIAR
IYEEMNNSSS AAEYYKEVLK QDNTHVEAIA CIGSNHFYSD QPEVALRFYR RLLQMGVYNC
QLFNNLGLCC FYAQQYDMTL TSFERALSLA ENEEEAADVW YNLGHIAVGI GDTNLAHQCF
RLALVHNNHH AEAYNNLAVL EMRKGHVEQA RALLQTASSL APHMYEPHFN FATVSDKIGD
LQRSYVAAQK SEVAFPEHVD TQHLIKQLKQ HFAML
