TECT1_MOUSE
ID TECT1_MOUSE Reviewed; 593 AA.
AC Q8BZ64; Q3UMP0; Q8BUE2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tectonic-1;
DE Flags: Precursor;
GN Name=Tctn1; Synonyms=Tect1;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone, Lung, and Mammary gland;
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 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 [4]
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 [5]
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).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-486, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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. Regulator of Hedgehog (Hh), required for both
CC activation and inhibition of the Hh pathway in the patterning of the
CC neural tube. During neural tube development, it is required for
CC formation of the most ventral cell types and for full Hh pathway
CC activation. Functions in Hh signal transduction to fully activate the
CC pathway in the presence of high Hh levels and to repress the pathway in
CC the absence of Hh signals. Modulates Hh signal transduction downstream
CC of SMO and RAB23. {ECO:0000269|PubMed:16357211,
CC ECO:0000269|PubMed:21725307, 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: Cytoplasm, cytoskeleton, cilium basal body.
CC Secreted. Note=Localizes at the transition zone, a region between the
CC basal body and the ciliary axoneme. Despite the presence of a signal
CC sequence, the full-length protein might not be secreted
CC (PubMed:16357211). {ECO:0000269|PubMed:16357211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZ64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZ64-2; Sequence=VSP_017764, VSP_017765;
CC -!- DEVELOPMENTAL STAGE: During embryonic development, it is expressed in
CC regions that participate in Hedgehog signaling. First expressed during
CC gastrulation stages in the ventral node. At 9.5 dpc, expressed in the
CC gut endoderm, limb buds, notochord, somites, neural tube and
CC floorplate. {ECO:0000269|PubMed:16357211}.
CC -!- DISRUPTION PHENOTYPE: Null animals show disruption of nodal flow,
CC laterality defects, and neural tube dorsalization. Basal bodies dock to
CC the cellular plasma membrane, but fail to extend axonemes. However,
CC cilia are present in the notochord, early gut epithelium, and
CC mesenchymal cells surrounding the neural tube and in the limb bud. Null
CC embryos develop an extra preaxial digit on 1 or both hindlimbs.
CC Although sonic hedgehog (Shh) expression is normal, downstream
CC signaling is disturbed, suggesting that Tctn1 is required for cilium-
CC dependent Shh signal transduction. {ECO:0000269|PubMed:21725307}.
CC -!- MISCELLANEOUS: Was named 'Tectonic' after the Greek word for builder.
CC -!- SIMILARITY: Belongs to the tectonic family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE26058.1; Type=Frameshift; Evidence={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; DQ278867; ABB90559.1; -; mRNA.
DR EMBL; AK036568; BAC29481.1; -; mRNA.
DR EMBL; AK085676; BAC39502.1; -; mRNA.
DR EMBL; AK144772; BAE26058.1; ALT_FRAME; mRNA.
DR CCDS; CCDS39254.1; -. [Q8BZ64-1]
DR RefSeq; NP_001034242.2; NM_001039153.3. [Q8BZ64-1]
DR AlphaFoldDB; Q8BZ64; -.
DR BioGRID; 576601; 2.
DR CORUM; Q8BZ64; -.
DR IntAct; Q8BZ64; 5.
DR STRING; 10090.ENSMUSP00000107367; -.
DR GlyGen; Q8BZ64; 3 sites.
DR iPTMnet; Q8BZ64; -.
DR PhosphoSitePlus; Q8BZ64; -.
DR MaxQB; Q8BZ64; -.
DR PaxDb; Q8BZ64; -.
DR PRIDE; Q8BZ64; -.
DR ProteomicsDB; 259372; -. [Q8BZ64-1]
DR ProteomicsDB; 259373; -. [Q8BZ64-2]
DR Antibodypedia; 45260; 93 antibodies from 26 providers.
DR DNASU; 654470; -.
DR Ensembl; ENSMUST00000111738; ENSMUSP00000107367; ENSMUSG00000038593. [Q8BZ64-1]
DR GeneID; 654470; -.
DR KEGG; mmu:654470; -.
DR UCSC; uc012ecz.1; mouse. [Q8BZ64-2]
DR UCSC; uc033ilv.2; mouse. [Q8BZ64-1]
DR CTD; 79600; -.
DR MGI; MGI:3603820; Tctn1.
DR VEuPathDB; HostDB:ENSMUSG00000038593; -.
DR eggNOG; ENOG502QUK6; Eukaryota.
DR GeneTree; ENSGT00570000079101; -.
DR HOGENOM; CLU_016974_0_1_1; -.
DR InParanoid; Q8BZ64; -.
DR OMA; AWPTINI; -.
DR OrthoDB; 446525at2759; -.
DR PhylomeDB; Q8BZ64; -.
DR TreeFam; TF329169; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 654470; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tctn1; mouse.
DR PRO; PR:Q8BZ64; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BZ64; protein.
DR Bgee; ENSMUSG00000038593; Expressed in spermatocyte and 204 other tissues.
DR ExpressionAtlas; Q8BZ64; baseline and differential.
DR Genevisible; Q8BZ64; MM.
DR GO; GO:0035869; C:ciliary transition zone; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
DR GO; GO:0021956; P:central nervous system interneuron axonogenesis; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR GO; GO:1904491; P:protein localization to ciliary transition zone; IMP:WormBase.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0021523; P:somatic motor neuron differentiation; IMP:MGI.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
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; Developmental protein; Glycoprotein; Methylation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..593
FT /note="Tectonic-1"
FT /id="PRO_0000229797"
FT REGION 37..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 486
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 162..195
FT /note="YKPALSFANPEVPDENNFDRLMQTSGGFTLSAES -> LWSPSADCRSIFRV
FT ISETALASHVISVCRSEPRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017764"
FT VAR_SEQ 196..593
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017765"
SQ SEQUENCE 593 AA; 63447 MW; 9DC347D81DE2B641 CRC64;
MGSRGLPPLL LVLLNCYTSS STQVIAIPAA ATPAVTKEDL NSTKATPTTL QPSLSPRTPG
TPRAPERSGP RPTPVTDVAA LCVCDLLPAQ CDVNCCCDPD CSPADFSIFS ACSVPVVTGD
RQFCSQKAAF YSMNLTADPP HRDFKLIDQI NPSVFCIHIS NYKPALSFAN PEVPDENNFD
RLMQTSGGFT LSAESAVPST AASDGPQPTK YEYGAPLQTA GASSGSFLKL PSPLTSSLCA
DQNPAAFLVS QAFECSRRVD IEQCEGMEAL SMAHYSSPAI LRVPNSMTQV SIKIQSVMYR
SLNHTLTQLE GHGVLRPSLV STGQDRLCSN VVLQVKYSLL YTATGQIHEA GLSLVLGTLS
SAVSLLQQKF EIHFIQHGTK PVPLSGNPGY RVGLPLAAGF QPQKGSGIIQ TTNRQGQFTI
LRSTSQQDCL ASEGLRTPVL FGYNVQSGCQ LRLTGTIPCG LLAQKVQDLL RGQAFPDYVA
AFGNSRAQDV QDWVPVHFVT YSSNMKGSCQ LPVALAIEVK WTKYGSLLNP QARIVNVTAQ
LVSVPEPLPG PERTVVISTA VTFVDVSAPA EAGFRAPPTI NARLPFSFFF PFV
