ID TECT2_MOUSE Reviewed; 700 AA. AC Q2MV57; Q6PDZ5; Q8C0B3; Q9CXF5; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 22-FEB-2023, entry version 106. DE RecName: Full=Tectonic-2; DE Flags: Precursor; GN Name=Tctn2; Synonyms=Tect2; 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 [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; RX PubMed=16357211; DOI=10.1101/gad.1363606; RA Reiter J.F., Skarnes W.C.; RT "Tectonic, a novel regulator of the Hedgehog pathway required for both RT activation and inhibition."; RL Genes Dev. 20:22-27(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Liver, and Medulla oblongata; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; 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 [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-389. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [5] RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH MKS1. RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019; RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A., RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K., RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D., RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A., RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B., RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.; RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes RT and pathways."; RL Cell 145:513-528(2011). RN [6] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=21462283; DOI=10.1002/humu.21507; RA Shaheen R., Faqeih E., Seidahmed M.Z., Sunker A., Alali F.E., RA Alkuraya F.S.; RT "A TCTN2 mutation defines a novel Meckel Gruber syndrome locus."; RL Hum. Mutat. 32:573-578(2011). RN [7] RP IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX, AND FUNCTION. RX PubMed=22179047; DOI=10.1038/ncb2410; RA Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E., RA Sandoval W., Peterson A.S.; RT "A ciliopathy complex at the transition zone protects the cilia as a RT privileged membrane domain."; RL Nat. Cell Biol. 14:61-72(2012). RN [8] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND IDENTIFICATION IN RP THE TECTONIC-LIKE COMPLEX. RX PubMed=21725307; DOI=10.1038/ng.891; RA Garcia-Gonzalo F.R., Corbit K.C., Sirerol-Piquer M.S., Ramaswami G., RA Otto E.A., Noriega T.R., Seol A.D., Robinson J.F., Bennett C.L., RA Josifova D.J., Garcia-Verdugo J.M., Katsanis N., Hildebrandt F., RA Reiter J.F.; RT "A transition zone complex regulates mammalian ciliogenesis and ciliary RT membrane composition."; RL Nat. Genet. 43:776-784(2011). CC -!- FUNCTION: Component of the tectonic-like complex, a complex localized CC at the transition zone of primary cilia and acting as a barrier that CC prevents diffusion of transmembrane proteins between the cilia and CC plasma membranes. Required for hedgehog signaling transduction. CC {ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307, CC ECO:0000269|PubMed:22179047}. CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex). CC {ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000269|PubMed:21725307}. Note=Localizes at the transition CC zone, a region between the basal body and the ciliary axoneme. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q2MV57-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2MV57-2; Sequence=VSP_017766; CC -!- TISSUE SPECIFICITY: Significant expression is observed in brain, kidney CC and eye. {ECO:0000269|PubMed:21462283}. CC -!- DEVELOPMENTAL STAGE: At 8.5 dpc, expressed in the neural tube, most CC notably in the rhombomere of the future hindbrain. By 10.5 dpc, CC expressed throughout the brain, the length of the neural tube, the CC growing edge of the limb buds, heart, and eyes. Strong expression is CC observed in the kidney at 14.5 dpc. {ECO:0000269|PubMed:21462283}. CC -!- DISRUPTION PHENOTYPE: Mice have ventricular septal defects and can CC display right-sided stomach. The embryos exhibit microphthalmia, cleft CC palate and polydactyly. Embryos lack also nodal cilia. Cilia in neural CC tubes are scarce and morphologically defective, and failed to elongate CC axonemes. Basal bodies dock to the plasma membrane in Tctn2 null neural CC epithelium. No Arl13b ciliary staining in defective Tctn2 embryos CC perineural mesenchyme suggesting that, as in Tctn1 null mutants, CC defective Tctn2 cilia lack Arl13b. Tctn1 and Tctn2 share a common CC function, with both affecting ciliogenesis in a tissue-specific manner. CC {ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307}. CC -!- SIMILARITY: Belongs to the tectonic family. {ECO:0000305}. 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; DQ278869; ABB90561.1; -; mRNA. DR EMBL; AK014476; BAB29379.1; -; mRNA. DR EMBL; AK031829; BAC27569.1; -; mRNA. DR EMBL; BC058375; AAH58375.1; -; mRNA. DR RefSeq; NP_080762.1; NM_026486.3. [Q2MV57-1] DR AlphaFoldDB; Q2MV57; -. DR BioGRID; 212577; 1. DR CORUM; Q2MV57; -. DR IntAct; Q2MV57; 3. DR GlyCosmos; Q2MV57; 5 sites, No reported glycans. DR GlyGen; Q2MV57; 5 sites. DR iPTMnet; Q2MV57; -. DR PhosphoSitePlus; Q2MV57; -. DR SwissPalm; Q2MV57; -. DR MaxQB; Q2MV57; -. DR PaxDb; Q2MV57; -. DR ProteomicsDB; 263154; -. [Q2MV57-1] DR ProteomicsDB; 263155; -. [Q2MV57-2] DR Antibodypedia; 45731; 168 antibodies from 31 providers. DR DNASU; 67978; -. DR Ensembl; ENSMUST00000239501.2; ENSMUSP00000159383.2; ENSMUSG00000118662.2. DR GeneID; 67978; -. DR KEGG; mmu:67978; -. DR UCSC; uc008zqg.2; mouse. [Q2MV57-1] DR AGR; MGI:1915228; -. DR CTD; 79867; -. DR MGI; MGI:1915228; Tctn2. DR GeneTree; ENSGT00570000079101; -. DR InParanoid; Q2MV57; -. DR OMA; WVEIIRL; -. DR OrthoDB; 2909954at2759; -. DR PhylomeDB; Q2MV57; -. DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane. DR BioGRID-ORCS; 67978; 2 hits in 22 CRISPR screens. DR ChiTaRS; Tctn2; mouse. DR PRO; PR:Q2MV57; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q2MV57; protein. DR GO; GO:0035869; C:ciliary transition zone; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:1904491; P:protein localization to ciliary transition zone; IMP:WormBase. DR GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB. DR InterPro; IPR040354; Tectonic. DR InterPro; IPR011677; Tectonic_dom. DR PANTHER; PTHR14611; TECTONIC FAMILY MEMBER; 1. DR PANTHER; PTHR14611:SF2; TECTONIC-2; 1. DR Pfam; PF07773; TCTN_DUF1619; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Cilium biogenesis/degradation; KW Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..700 FT /note="Tectonic-2" FT /id="PRO_0000229799" FT TOPO_DOM 26..665 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 666..682 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 683..700 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 82 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 146 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 156 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 389 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT VAR_SEQ 1..121 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017766" FT CONFLICT 42 FT /note="R -> Q (in Ref. 1; ABB90561)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="S -> T (in Ref. 1; ABB90561)" FT /evidence="ECO:0000305" FT CONFLICT 79 FT /note="V -> E (in Ref. 1; ABB90561)" FT /evidence="ECO:0000305" FT CONFLICT 272 FT /note="D -> E (in Ref. 2; BAC27569)" FT /evidence="ECO:0000305" SQ SEQUENCE 700 AA; 77111 MW; 59B1C3A973EFD581 CRC64; MGSLSPLSLL WGLLLLQGVL RPLRGDPVFI PPFIRMSSPE VRATLVGGSE DVAVSLSLLQ VEEGVLPVPT CGGRRNETVD WNVTVSPRES TLEVTIRWKR GLDWCSADET ASFSEPPCVL QMLLVSASHN ASCLAHLLIQ VEIYPNTSVT HNASENMTVI PNQVYQPLGP CPCDLTAKAC DIQCCCDQDC QPEVRELFAQ SCFSGVFGGH VSPPSHHHCA VSTTHQTPDW FPLLCVQSPP STSPFLGHFY HGATSPRHSP GFEAHLHFDL RDFADASYKQ GDPIMTTEGY FTIPQVSLAG QCLQDAPVAF LRNFDSVCTM DLEVHQGRDE IVLENMKIRT TGGPVTPTVT YEEAIDLDKF ITSPDTVLSV GSAPRNVNVE EHYVFRWQNN SISGLDITVI RAEISAQQRG MMTQRFTVKF LSHHSGGEKE FSGNPGYQLG KPVRALHTAG MNVSTLHLWQ PAGRGLCTAA ALRPILFGEN AFSGCLLEVG IKENCTQLRE NVLQRLDLLT QATHVARRGN SDYSDLSDGW LEIIRAEAPD TGADLPLSSV NGVCPEVPAR LSIRILTAEA GSVEGVAQRE ILAVETRFST VTWQYQCGLT CEDKADLLPL SASVEFINVP AQMPHPPTRF QINFTEYDCT RNELCWPQLL YPLTQYYQGE PQSQCVAKGL MLLSLLMLAI LLRHPWVRMC KARDSAAIYH //