ID TECTA_MOUSE Reviewed; 2155 AA.
AC O08523; E9QNR3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 24-JAN-2024, entry version 173.
DE RecName: Full=Alpha-tectorin;
DE Flags: Precursor;
GN Name=Tecta;
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] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 25-34,
RP SUBUNIT, SUBCELLULAR LOCATION, POST-TRANSLATIONAL MODIFICATIONS, AND TISSUE
RP SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Cochlea;
RX PubMed=9079715; DOI=10.1074/jbc.272.13.8791;
RA Legan P.K., Rau A., Keene J.N., Richardson G.P.;
RT "The mouse tectorins. Modular matrix proteins of the inner ear homologous
RT to components of the sperm-egg adhesion system.";
RL J. Biol. Chem. 272:8791-8801(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=9590290; DOI=10.1038/ng0598-60;
RA Verhoeven K., Van Laer L., Kirschhofer K., Legan P.K., Hughes D.C.,
RA Schatteman I., Verstreken M., Van Hauwe P., Coucke P., Chen A.,
RA Smith R.J.H., Somers T., Offeciers F.E., Van de Heyning P.,
RA Richardson G.P., Wachtler F., Kimberling W.J., Willems P.J., Govaerts P.J.,
RA Van Camp G.;
RT "Mutations in the human alpha-tectorin gene cause autosomal dominant non-
RT syndromic hearing impairment.";
RL Nat. Genet. 19:60-62(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INTERACTION WITH CEACAM16.
RX PubMed=25080593; DOI=10.1523/jneurosci.1256-14.2014;
RA Cheatham M.A., Goodyear R.J., Homma K., Legan P.K., Korchagina J.,
RA Naskar S., Siegel J.H., Dallos P., Zheng J., Richardson G.P.;
RT "Loss of the tectorial membrane protein CEACAM16 enhances spontaneous,
RT stimulus-frequency, and transiently evoked otoacoustic emissions.";
RL J. Neurosci. 34:10325-10338(2014).
CC -!- FUNCTION: One of the major non-collagenous components of the tectorial
CC membrane (By similarity). The tectorial membrane is an extracellular
CC matrix of the inner ear that covers the neuroepithelium of the cochlea
CC and contacts the stereocilia bundles of specialized sensory hair cells.
CC Sound induces movement of these hair cells relative to the tectorial
CC membrane, deflects the stereocilia and leads to fluctuations in hair-
CC cell membrane potential, transducing sound into electrical signals.
CC {ECO:0000250}.
CC -!- SUBUNIT: May form homomeric filament after self-association or
CC heteromeric filament after association with beta-tectorin (Probable).
CC Interacts with CEACAM16 (PubMed:25080593).
CC {ECO:0000269|PubMed:25080593, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9079715};
CC Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:9079715}; Extracellular
CC side {ECO:0000305|PubMed:9079715}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:9079715}. Note=Found in the
CC non-collagenous matrix of the tectorial membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08523-2; Sequence=VSP_010557;
CC -!- TISSUE SPECIFICITY: Cochlea-specific. {ECO:0000269|PubMed:9079715}.
CC -!- DOMAIN: Zona pellucida domain may enable to form filaments.
CC -!- PTM: 3 products of tectorin seem to exist: HMM, MMM and LMM. They may
CC be generated by active processing or the result of proteolysis
CC occurring between intrachain disulfide bonds.
CC -!- PTM: The presence of a hydrophobic C-terminus preceded by a potential
CC cleavage site strongly suggests that tectorins are synthesized as
CC glycosylphosphatidylinositol-linked, membrane-bound precursors.
CC Tectorins are targeted to the apical surface of the inner ear epithelia
CC by the lipid and proteolytically released into the extracellular
CC compartment.
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DR EMBL; X99805; CAA68138.1; -; mRNA.
DR EMBL; AC156631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23087.1; -. [O08523-1]
DR CCDS; CCDS85660.1; -. [O08523-2]
DR PIR; T30197; T30197.
DR RefSeq; NP_001311477.1; NM_001324548.1. [O08523-2]
DR RefSeq; NP_033373.2; NM_009347.3. [O08523-1]
DR RefSeq; XP_017168765.1; XM_017313276.1.
DR AlphaFoldDB; O08523; -.
DR SMR; O08523; -.
DR STRING; 10090.ENSMUSP00000040262; -.
DR GlyCosmos; O08523; 31 sites, No reported glycans.
DR GlyGen; O08523; 31 sites.
DR PhosphoSitePlus; O08523; -.
DR MaxQB; O08523; -.
DR PaxDb; 10090-ENSMUSP00000040262; -.
DR Antibodypedia; 18890; 33 antibodies from 15 providers.
DR DNASU; 21683; -.
DR Ensembl; ENSMUST00000042190.14; ENSMUSP00000040262.8; ENSMUSG00000037705.14. [O08523-1]
DR Ensembl; ENSMUST00000160940.2; ENSMUSP00000125370.2; ENSMUSG00000037705.14. [O08523-2]
DR GeneID; 21683; -.
DR KEGG; mmu:21683; -.
DR UCSC; uc009pau.1; mouse. [O08523-1]
DR UCSC; uc012grn.1; mouse. [O08523-2]
DR AGR; MGI:109575; -.
DR CTD; 7007; -.
DR MGI; MGI:109575; Tecta.
DR VEuPathDB; HostDB:ENSMUSG00000037705; -.
DR eggNOG; KOG1216; Eukaryota.
DR eggNOG; KOG4291; Eukaryota.
DR GeneTree; ENSGT00950000183155; -.
DR HOGENOM; CLU_001423_0_0_1; -.
DR InParanoid; O08523; -.
DR OMA; RVQTGCV; -.
DR OrthoDB; 2872912at2759; -.
DR PhylomeDB; O08523; -.
DR TreeFam; TF300299; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 21683; 2 hits in 76 CRISPR screens.
DR PRO; PR:O08523; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O08523; Protein.
DR Bgee; ENSMUSG00000037705; Expressed in epithelium of cochlear duct and 28 other cell types or tissues.
DR Genevisible; O08523; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IGI:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0007605; P:sensory perception of sound; TAS:MGI.
DR CDD; cd19941; TIL; 3.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR025615; TILa_dom.
DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR46160:SF3; ALPHA-TECTORIN; 1.
DR PANTHER; PTHR46160; ALPHA-TECTORIN-RELATED; 1.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF01826; TIL; 3.
DR Pfam; PF12714; TILa; 2.
DR Pfam; PF00094; VWD; 4.
DR Pfam; PF00100; Zona_pellucida; 1.
DR SMART; SM00832; C8; 4.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00215; VWC_out; 3.
DR SMART; SM00216; VWD; 4.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57567; Serine protease inhibitors; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS51233; VWFD; 4.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Glycoprotein; GPI-anchor; Hearing;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:9079715"
FT CHAIN 25..2091
FT /note="Alpha-tectorin"
FT /id="PRO_0000041737"
FT PROPEP 2092..2155
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041738"
FT DOMAIN 98..252
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 260..314
FT /note="VWFC"
FT DOMAIN 320..500
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 597..650
FT /note="TIL 1"
FT DOMAIN 711..886
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 984..1036
FT /note="TIL 2"
FT DOMAIN 1098..1278
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1372..1425
FT /note="TIL 3"
FT DOMAIN 1485..1666
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1805..2059
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT LIPID 2091
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 322..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 344..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 713..849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1100..1241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1122..1277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1487..1622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1509..1665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1717..1775
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1741..1784
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1786..1818
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1806..1898
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1837..1857
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1980..2040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2001..2056
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 2045..2052
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT VAR_SEQ 1659..1663
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9079715,
FT ECO:0000303|PubMed:9590290"
FT /id="VSP_010557"
FT CONFLICT 803
FT /note="S -> T (in Ref. 1; CAA68138)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="A -> R (in Ref. 1; CAA68138)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="P -> T (in Ref. 1; CAA68138)"
FT /evidence="ECO:0000305"
FT CONFLICT 1229
FT /note="V -> I (in Ref. 1; CAA68138)"
FT /evidence="ECO:0000305"
FT CONFLICT 2148
FT /note="I -> V (in Ref. 1; CAA68138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2155 AA; 239433 MW; 1F93E76E0FFB2C23 CRC64;
MNYSSLLRIW VSFIFALVRH QAQPRELMYP FWQNDTRTPK VDDGSSSEIK LAIPVFFFGV
PYRTVYVNNN GVVSFNVLVS QFTPESFPLT DGRAFIAPFW ADVHNGIRGE IYYRETMDPA
ILRRATKDIR KYFKDMTTFS ATWVFIVTWE EVTFYGGSST TPVNTFQAVL VSDGSYTFTL
FNYYEINWTT GTASGGDPLT GLGGVMAQAG FNGGNLTNFF SLPGSRTPEI VNIQETTNVN
VPGRWAFKVD GKEIDPANGC TSRGQFLRRG EVFWDDLNCT IKCRCLDFNN EIYCQEASCS
PYEVCEPKGR FFYCSPVETS TCVVFGEPHY HTFDGFLFHF QGSCAYLLAR QCLQTSSLPF
FSVEAKNEHR GGSAVSWVKE LSVEVNGYKI LIPKGSYGKV KVNDLVTSLP VTLELGAVKI
YQSGMSTAVE TDFGLLVTFD GQHYASISIP GSYINSTCGL CGNYNKNPLD DFLRPDGRPA
MSVLDLGESW RVYHADWKCG SGCVDNCTQC DAATEALYFG SDYCGFLNKT DGPLWECGTV
VDATAFVHSC VYDLCSVRDN GTLLCQAIQA YALVCQALGI PIGDWRIQTG CVSTVRCPSF
SHYSVCTSSC PDTCSDLTAS QNCATPCTEG CECNEGFVLS TSQCVPLHKC GCDFDGHYYT
MGEFFWATAN CTVQCLCEEG GDVYCFNKTC RSGEVCAVED GYQGCFPKRE TVCLLSQNQV
LHTFDGAAYA FPSELSYTLL KTCPERPEYL EIDINKKKPD AGPAWLRGVR ILVADQEVKI
GGVGALEVKL NGQDVELPFF HPSGRLEIHR NKNSTTVESK GVVSVQYSDV GLLYIRLSTM
YFNCTGGLCG FFNANASDEF CLPNGKCTDN LAVFLESWTT FEEICNGECG DLLKACNNDS
ELLKFYRSRS RCGIINDPSN SSFLECHGVV NVTAYYRTCL FRLCQSGGNE SELCDSVARY
ASACKNADVE VGPWRTYDFC PLECPENSHF EECMTCTETC ETLALGPICV DSCSEGCQCD
EGYALQGSQC VPRSECGCNF EGHQLATNET FWVDQDCQIF CYCNGTDNSV HCETIPCRDD
EYCMEESGLY YCQPRTDASC IVSGYGHYLT FDGYPFDFQT SCPLILCTTG SRPISDSFPK
FIVTAKNEDR DPSLALWVKQ VDVNVFGYSI VIHRAYKHTV LVNNERLYLP LKLGQGKINI
FSFGFHVVVE TDFGLKVVYD WKTFLSITVP RSMQNGTYGL CGRYNGNPDD DLEMPMGLPA
LSINEFGQSW VKRDTFCQVG CGDRCPSCAK VEGFSKVQQL CSLIPNQNAG FAKCHSKVNP
TFFYKNCLFD SCIDGGAVQT ACSWLQNYAS TCQTQGIAVT GWRNYTSCSV TCPPNSHYES
CVSVCQPRCA AIRLKSDCNH YCVEGCQCDA GYVLNGKSCI LPHNCGCYSD GKYYEPKQLF
WNGDCTRRCR CFRRNLIQCD PRQCKSDEEC ALRSGVRGCF STKTSYCLAA GGGVFRTFDG
AFLRFPANCA FVLSTICQKL PDISFQLIIN FDKWSSPNLT IISPVYFYIN EEQILINDRN
TVKVNGTQVN VPFITGLATK IYSSEGFLVI DTSPDIQIYY NGFNVIKISI SERLQNKVCG
LCGNFNGDMT DDYVTLRGKP VVSSVVLAQS WKTNGMQKRP LAPSCNELQF SQYAATCDNV
HIQAMQGDGY CLKLTDMKGF FQPCYGLLDP LPFYESCYLD GCYNHKKFQL CGSLAAYGEA
CRSFGILSTE WIEKENCSGV VEDPCVGADC PNRTCELDNG GELCGCIEPP PYGNNSHDII
DAEVTCKAAQ MEVSISKCKL FQLGFEREGV RINDRQCSGI EGEDFISFQI NNTKGNCGNI
VQSNGTHIMY KNTIWIESAN NTGNIITRDR TINVEFSCAY ELDIKISLDS VVKPMLSVIN
LTVPTQEGSF TTKMALYKNA SYKHPYRQGE VVLTTRDVLY VGVFVVGADS THLILTLNKC
YATPSRDSND KLRYFIIEGG CQNIKDNTIG IEENGVSLTC RFHVTVFKFI GDYDEVHLHC
AVSLCDSEKY SCKINCPQNS RIATDYSKEH KEQIISVGPI RRKRLDWCED NGGCEQICTS
RVDGPLCSCV TGSLQEDGRS CRASNSSVEL QVWTLLLIMT QISLWHLIYK SGATS
//
