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 28-MAR-2018, entry version 84. DE RecName: Full=Tectonic-2; DE Flags: Precursor; GN Name=Tctn2; Synonyms=Tect2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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- RT linked 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., RA Sfakianos M.K., Sandoval W., Bazan J.F., Kulkarni P., RA Garcia-Gonzalo F.R., Seol A.D., O'Toole J.F., Held S., Reutter H.M., RA Lane W.S., Rafiq M.A., Noor A., Ansar M., Devi A.R., Sheffield V.C., RA Slusarski D.C., Vincent J.B., Doherty D.A., Hildebrandt F., RA Reiter J.F., Jackson P.K.; RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease RT genes 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 RP IDENTIFICATION IN 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 RT ciliary membrane composition."; RL Nat. Genet. 43:776-784(2011). CC -!- FUNCTION: Component of the tectonic-like complex, a complex CC localized at the transition zone of primary cilia and acting as a CC barrier that prevents diffusion of transmembrane proteins between CC the cilia and plasma membranes. Required for hedgehog signaling CC transduction. {ECO:0000269|PubMed:21565611, CC ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:22179047}. CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 CC complex). {ECO:0000269|PubMed:21725307, CC ECO:0000269|PubMed:22179047}. CC -!- INTERACTION: CC Q5SW45:Mks1; NbExp=2; IntAct=EBI-4281008, EBI-4281059; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, cilium CC basal body {ECO:0000269|PubMed:21725307}. Note=Localizes at the CC transition zone, a region between the basal body and the ciliary CC 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 Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Significant expression is observed in brain, CC kidney and eye. {ECO:0000269|PubMed:21462283}. CC -!- DEVELOPMENTAL STAGE: At 8.5 dpc, expressed in the neural tube, CC most notably in the rhombomere of the future hindbrain. By 10.5 CC dpc, expressed throughout the brain, the length of the neural CC tube, the growing edge of the limb buds, heart, and eyes. Strong CC expression is observed in the kidney at 14.5 dpc. CC {ECO:0000269|PubMed:21462283}. CC -!- DISRUPTION PHENOTYPE: Mice have ventricular septal defects and can CC display right-sided stomach. The embryos exhibit microphthalmia, CC cleft palate and polydactyly. Embryos lack also nodal cilia. Cilia CC in neural tubes are scarce and morphologically defective, and CC failed to elongate axonemes. Basal bodies dock to the plasma CC membrane in Tctn2 null neural epithelium. No Arl13b ciliary CC staining in defective Tctn2 embryos perineural mesenchyme CC suggesting that, as in Tctn1 null mutants, defective Tctn2 cilia CC lack Arl13b. Tctn1 and Tctn2 share a common function, with both CC 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 UniGene; Mm.1158; -. DR BioGrid; 212577; 1. DR CORUM; Q2MV57; -. DR IntAct; Q2MV57; 3. DR STRING; 10090.ENSMUSP00000098272; -. DR iPTMnet; Q2MV57; -. DR PhosphoSitePlus; Q2MV57; -. DR MaxQB; Q2MV57; -. DR PaxDb; Q2MV57; -. DR PRIDE; Q2MV57; -. DR GeneID; 67978; -. DR KEGG; mmu:67978; -. DR UCSC; uc008zqg.2; mouse. [Q2MV57-1] DR CTD; 79867; -. DR MGI; MGI:1915228; Tctn2. DR eggNOG; ENOG410IJPP; Eukaryota. DR eggNOG; ENOG4111MZ0; LUCA. DR HOGENOM; HOG000013148; -. DR HOVERGEN; HBG083562; -. DR InParanoid; Q2MV57; -. DR KO; K19361; -. DR PhylomeDB; Q2MV57; -. DR ChiTaRS; Tctn2; mouse. DR PRO; PR:Q2MV57; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_TCTN2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; IPR011677; DUF1619. DR Pfam; PF07773; DUF1619; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Cilium biogenesis/degradation; KW Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 700 Tectonic-2. FT /FTId=PRO_0000229799. FT TOPO_DOM 26 665 Extracellular. {ECO:0000255}. FT TRANSMEM 666 682 Helical. {ECO:0000255}. FT TOPO_DOM 683 700 Cytoplasmic. {ECO:0000255}. FT COMPBIAS 171 190 Cys-rich. FT CARBOHYD 76 76 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 82 82 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 146 146 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 156 156 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 389 389 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19349973}. FT VAR_SEQ 1 121 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_017766. FT CONFLICT 42 42 R -> Q (in Ref. 1; ABB90561). FT {ECO:0000305}. FT CONFLICT 57 57 S -> T (in Ref. 1; ABB90561). FT {ECO:0000305}. FT CONFLICT 79 79 V -> E (in Ref. 1; ABB90561). FT {ECO:0000305}. FT CONFLICT 272 272 D -> E (in Ref. 2; BAC27569). FT {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 //