TECT2_MOUSE
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 03-AUG-2022, entry version 103.
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 GlyGen; Q2MV57; 5 sites.
DR iPTMnet; Q2MV57; -.
DR PhosphoSitePlus; Q2MV57; -.
DR MaxQB; Q2MV57; -.
DR PaxDb; Q2MV57; -.
DR PRIDE; Q2MV57; -.
DR ProteomicsDB; 263154; -. [Q2MV57-1]
DR ProteomicsDB; 263155; -. [Q2MV57-2]
DR Antibodypedia; 45731; 167 antibodies from 31 providers.
DR DNASU; 67978; -.
DR Ensembl; ENSMUST00000239501; ENSMUSP00000159383; ENSMUSG00000118662. [Q2MV57-1]
DR GeneID; 67978; -.
DR KEGG; mmu:67978; -.
DR UCSC; uc008zqg.2; mouse. [Q2MV57-1]
DR CTD; 79867; -.
DR MGI; MGI:1915228; Tctn2.
DR GeneTree; ENSGT00570000079101; -.
DR InParanoid; Q2MV57; -.
DR OMA; WVEIIRL; -.
DR OrthoDB; 446525at2759; -.
DR PhylomeDB; Q2MV57; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 67978; 2 hits in 19 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: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; IPR040354; Tectonic.
DR InterPro; IPR011677; Tectonic_dom.
DR PANTHER; PTHR14611; PTHR14611; 1.
DR Pfam; PF07773; 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
