ID TM216_DANRE Reviewed; 160 AA. AC E7EYQ9; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 08-MAR-2011, sequence version 1. DT 13-NOV-2013, entry version 18. DE RecName: Full=Transmembrane protein 216; GN Name=tmem216; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; 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., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA 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., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] RP DISRUPTION PHENOTYPE. RX PubMed=22282472; DOI=10.1126/science.1213506; RA Lee J.H., Silhavy J.L., Lee J.E., Al-Gazali L., Thomas S., Davis E.E., RA Bielas S.L., Hill K.J., Iannicelli M., Brancati F., Gabriel S.B., RA Russ C., Logan C.V., Sharif S.M., Bennett C.P., Abe M., RA Hildebrandt F., Diplas B.H., Attie-Bitach T., Katsanis N., Rajab A., RA Koul R., Sztriha L., Waters E.R., Ferro-Novick S., Woods G.C., RA Johnson C.A., Valente E.M., Zaki M.S., Gleeson J.G.; RT "Evolutionarily assembled cis-regulatory module at a human ciliopathy RT locus."; RL Science 335:966-969(2012). CC -!- FUNCTION: Part of the tectonic-like complex which is required for CC tissue-specific ciliogenesis and may regulate ciliary membrane CC composition (By similarity). CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex) CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). Cytoplasm, cytoskeleton, cilium basal body (By CC similarity). Note=Localizes at the transition zone, a region CC between the basal body and the ciliary axoneme (By similarity). CC -!- DISRUPTION PHENOTYPE: Ciliary phenotypes such as pericardial CC effusion, hydrocephalic brain, curved or kinked tail, gastrulation CC defects and other severe defects in left/right axis. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL645792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR IPI; IPI00900846; -. DR Ensembl; ENSDART00000131027; ENSDARP00000111752; ENSDARG00000091576. DR GeneTree; ENSGT00390000002170; -. DR OMA; LMFIYKG; -. DR OrthoDB; EOG7SV0XB; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005932; C:microtubule basal body; IEA:UniProtKB-SubCell. DR GO; GO:0042384; P:cilium assembly; IMP:UniProtKB. DR InterPro; IPR019184; Uncharacterised_TM-17. DR Pfam; PF09799; Transmemb_17; 1. PE 3: Inferred from homology; KW Cell projection; Cilium biogenesis/degradation; Complete proteome; KW Cytoplasm; Cytoskeleton; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 160 Transmembrane protein 216. FT /FTId=PRO_0000416297. FT TRANSMEM 41 61 Helical; (Potential). FT TRANSMEM 68 88 Helical; (Potential). FT TRANSMEM 101 121 Helical; (Potential). FT TRANSMEM 134 154 Helical; (Potential). SQ SEQUENCE 160 AA; 18216 MW; 86DF135F2268FCEF CRC64; MADVCLRLQY ACPWQSNMAA HGRQPVLSST PLQILFHLNG WYFAAFFVAE ILMFIYKGVI LPYPQDNLIL DVVLLLLFSG LETLRLFYGW KGNLCQRSLA LFVSVAILVP CAVLSVYYLL LQTFVLRLEF VLNAVLLCFY GFELVLGVMT ISIFSRANIY //