TECTB_CHICK
ID TECTB_CHICK Reviewed; 329 AA.
AC P54097;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Beta-tectorin;
DE Flags: Precursor;
GN Name=TECTB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isa brown; TISSUE=Cochlear duct;
RX PubMed=7721949; DOI=10.1083/jcb.129.2.535;
RA Killick R., Legan P.K., Malenczak C., Richardson G.P.;
RT "Molecular cloning of chick beta-tectorin, an extracellular matrix molecule
RT of the inner ear.";
RL J. Cell Biol. 129:535-547(1995).
RN [2]
RP FUNCTION.
RX PubMed=1490898; DOI=10.1016/0378-5955(92)90165-j;
RA Killick R., Malenczak C., Richardson G.P.;
RT "The protein composition of the avian tectorial membrane.";
RL Hear. Res. 64:21-38(1992).
RN [3]
RP TISSUE SPECIFICITY.
RC STRAIN=White leghorn;
RX PubMed=9736748; DOI=10.1073/pnas.95.19.11400;
RA Heller S., Sheane C.A., Javed Z., Hudspeth A.J.;
RT "Molecular markers for cell types of the inner ear and candidate genes for
RT hearing disorders.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11400-11405(1998).
CC -!- FUNCTION: One of the major non-collagenous components of the tectorial
CC membrane. The tectorial membrane is an extracellular matrix of the
CC inner ear that covers the neuroepithelium of the cochlea and contacts
CC the stereocilia bundles of specialized sensory hair cells. Sound
CC 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:0000269|PubMed:1490898}.
CC -!- SUBUNIT: May form homomeric filament after self-association or
CC heteromeric filament after association with alpha-tectorin.
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 -!- TISSUE SPECIFICITY: Exclusively expressed in the inner ear, where it is
CC found in basilar papilla, clear cells, supporting cells, cuboidal cells
CC and the lagena macula. {ECO:0000269|PubMed:9736748}.
CC -!- DOMAIN: Zona pellucida domain may enable to form filaments.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: N-glycosylated.
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; L38519; AAA92461.1; -; mRNA.
DR PIR; A57246; A57246.
DR RefSeq; NP_990694.1; NM_205363.1.
DR AlphaFoldDB; P54097; -.
DR SMR; P54097; -.
DR BioGRID; 676576; 1.
DR IntAct; P54097; 1.
DR STRING; 9031.ENSGALP00000014293; -.
DR PaxDb; P54097; -.
DR GeneID; 396320; -.
DR KEGG; gga:396320; -.
DR CTD; 6975; -.
DR VEuPathDB; HostDB:geneid_396320; -.
DR eggNOG; ENOG502RGQ6; Eukaryota.
DR InParanoid; P54097; -.
DR OrthoDB; 880252at2759; -.
DR PhylomeDB; P54097; -.
DR PRO; PR:P54097; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 SMART; SM00241; ZP; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 2: Evidence at transcript 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..304
FT /note="Beta-tectorin"
FT /id="PRO_0000041745"
FT PROPEP 305..329
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041746"
FT DOMAIN 19..287
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT LIPID 304
FT /note="GPI-anchor amidated glycine"
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; 36899 MW; 4D66131C733C0DA2 CRC64;
MVAVTVYLMV ILAQAFAGPC TPNKADVILV YCYPRTIITK IPECPYGWEV NQLALGGICY
NGIHDSGYYQ FTIPDLSPKN KSYCGTQSEF KNPVYHFYNS IVSNDSTVIV KSQPVNYSFT
CTYNANYLVN QAAFDQRVAT IHVKNGSSGS FESQLSLNFY SNAKFSSIKE APFVVETSEI
GSDIFAGVEA KGLSDRFKVV LNNCWATPSS EYFYQVHWPL ITKGCASDFS IVVHENGKTN
RATFQFNAFR FQNIPKLSKV WLHCETHVCD SEKFSCPVTC DKRKQRMEQT GGVLVAEISV
RNKGLSRFYM LSDVIFHLLF AIGFCAILL
