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   24-JAN-2024, entry version 145.
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.
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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   GlyCosmos; O08524; 4 sites, No reported glycans.
DR   GlyGen; O08524; 4 sites.
DR   PaxDb; 10090-ENSMUSP00000025936; -.
DR   Antibodypedia; 53513; 110 antibodies from 13 providers.
DR   DNASU; 21684; -.
DR   Ensembl; ENSMUST00000025936.12; ENSMUSP00000025936.6; ENSMUSG00000024979.14.
DR   GeneID; 21684; -.
DR   KEGG; mmu:21684; -.
DR   UCSC; uc008hxm.1; mouse.
DR   AGR; MGI:109574; -.
DR   CTD; 6975; -.
DR   MGI; MGI:109574; Tectb.
DR   VEuPathDB; HostDB:ENSMUSG00000024979; -.
DR   eggNOG; ENOG502RGQ6; Eukaryota.
DR   GeneTree; ENSGT00940000159064; -.
DR   InParanoid; O08524; -.
DR   OMA; ATDYSIL; -.
DR   OrthoDB; 5304671at2759; -.
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 77 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 16 other cell types or tissues.
DR   ExpressionAtlas; O08524; baseline and differential.
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:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; Zona pellucida, ZP-C domain; 1.
DR   InterPro; IPR042235; ZP-C.
DR   InterPro; IPR048290; ZP_chr.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   PANTHER; PTHR14002:SF13; BETA-TECTORIN; 1.
DR   PANTHER; PTHR14002; ENDOGLIN/TGF-BETA RECEPTOR TYPE III; 1.
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.
DR   Genevisible; O08524; MM.
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
//