TECTB_MOUSE
ID TECTB_MOUSE Reviewed; 329 AA.
AC O08524;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Beta-tectorin;
DE Flags: Precursor;
GN Name=Tectb;
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].
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 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 alpha-tectorin (Probable).
CC Interacts with CEACAM16 (PubMed:25080593).
CC {ECO:0000269|PubMed:25080593, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted,
CC extracellular space, extracellular matrix. Note=Found in the non-
CC collagenous matrix of the tectorial membrane. {ECO:0000250}.
CC -!- DOMAIN: Zona pellucida domain may enable to form filaments.
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.
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; X99806; CAA68139.2; -; mRNA.
DR CCDS; CCDS29907.1; -.
DR RefSeq; NP_033374.2; NM_009348.3.
DR RefSeq; XP_006526966.1; XM_006526903.1.
DR AlphaFoldDB; O08524; -.
DR SMR; O08524; -.
DR STRING; 10090.ENSMUSP00000025936; -.
DR GlyGen; O08524; 4 sites.
DR PaxDb; O08524; -.
DR PRIDE; O08524; -.
DR Antibodypedia; 53513; 91 antibodies from 12 providers.
DR DNASU; 21684; -.
DR Ensembl; ENSMUST00000025936; ENSMUSP00000025936; ENSMUSG00000024979.
DR GeneID; 21684; -.
DR KEGG; mmu:21684; -.
DR UCSC; uc008hxm.1; mouse.
DR CTD; 6975; -.
DR MGI; MGI:109574; Tectb.
DR VEuPathDB; HostDB:ENSMUSG00000024979; -.
DR eggNOG; ENOG502RGQ6; Eukaryota.
DR GeneTree; ENSGT00940000159064; -.
DR InParanoid; O08524; -.
DR OMA; TNRATFQ; -.
DR OrthoDB; 880252at2759; -.
DR PhylomeDB; O08524; -.
DR TreeFam; TF330284; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 21684; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Tectb; mouse.
DR PRO; PR:O08524; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O08524; protein.
DR Bgee; ENSMUSG00000024979; Expressed in epithelium of cochlear duct and 15 other tissues.
DR ExpressionAtlas; O08524; baseline and differential.
DR Genevisible; O08524; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
DR GO; GO:0007605; P:sensory perception of sound; TAS:MGI.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Extracellular matrix; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..305
FT /note="Beta-tectorin"
FT /id="PRO_0000041743"
FT PROPEP 306..329
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041744"
FT DOMAIN 19..283
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT LIPID 305
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 204..264
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 36986 MW; CC69A33EBC270AB3 CRC64;
MVVRAFVLLA LFAEASAKSC TPNKADVILV FCYPKTIITK IPECPYGWEV HQLALGGLCY
NGVHEGGYYQ FVIPDLSPKN KSYCGTQSEY KPPIYHFYSH IVSNDSTVIV KNQPVNYSFS
CTYHSTYLVN QAAFDQRVAT VHVKNGSMGT FESQLSLNFY TNAKFSTKKE APFVLETSEI
GSDLFAGVEA KGLSVRFKVV LNSCWATPSA DFMYPLQWQL INKGCPTDET VLVHENGKDH
RATFQFNAFR FQNIPKLSKV WLHCETFICD SEKLSCPVNC DKRKRMLRDQ TGGVLVVELS
LRSRAFSGLC DFSDVLLHLI LMLGTWAVL
