TECTB_HUMAN
ID TECTB_HUMAN Reviewed; 329 AA.
AC Q96PL2; Q5VW53;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Beta-tectorin;
DE Flags: Precursor;
GN Name=TECTB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Xia J.H., Zhang H.L., Deng H., Lu C.Y., Pang Q.;
RT "Cloning and identification of human TECTB.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By similarity). {ECO:0000250|UniProtKB:O08524,
CC 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; AF312827; AAL12829.1; -; mRNA.
DR EMBL; AL391986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113497; AAI13498.1; -; mRNA.
DR EMBL; BC113499; AAI13500.1; -; mRNA.
DR CCDS; CCDS7571.1; -.
DR RefSeq; NP_478129.1; NM_058222.2.
DR AlphaFoldDB; Q96PL2; -.
DR SMR; Q96PL2; -.
DR BioGRID; 112835; 42.
DR STRING; 9606.ENSP00000358430; -.
DR GlyGen; Q96PL2; 4 sites.
DR BioMuta; TECTB; -.
DR DMDM; 48428669; -.
DR PaxDb; Q96PL2; -.
DR PRIDE; Q96PL2; -.
DR Antibodypedia; 53513; 91 antibodies from 12 providers.
DR DNASU; 6975; -.
DR Ensembl; ENST00000369422.4; ENSP00000358430.3; ENSG00000119913.6.
DR Ensembl; ENST00000646139.2; ENSP00000494896.1; ENSG00000119913.6.
DR GeneID; 6975; -.
DR KEGG; hsa:6975; -.
DR MANE-Select; ENST00000646139.2; ENSP00000494896.1; NM_058222.3; NP_478129.1.
DR UCSC; uc001kzr.3; human.
DR CTD; 6975; -.
DR GeneCards; TECTB; -.
DR HGNC; HGNC:11721; TECTB.
DR HPA; ENSG00000119913; Not detected.
DR MIM; 602653; gene.
DR neXtProt; NX_Q96PL2; -.
DR OpenTargets; ENSG00000119913; -.
DR PharmGKB; PA36438; -.
DR VEuPathDB; HostDB:ENSG00000119913; -.
DR eggNOG; ENOG502RGQ6; Eukaryota.
DR GeneTree; ENSGT00940000159064; -.
DR HOGENOM; CLU_073084_0_0_1; -.
DR InParanoid; Q96PL2; -.
DR OMA; TNRATFQ; -.
DR OrthoDB; 880252at2759; -.
DR PhylomeDB; Q96PL2; -.
DR TreeFam; TF330284; -.
DR PathwayCommons; Q96PL2; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 6975; 8 hits in 1060 CRISPR screens.
DR ChiTaRS; TECTB; human.
DR GeneWiki; TECTB; -.
DR GenomeRNAi; 6975; -.
DR Pharos; Q96PL2; Tbio.
DR PRO; PR:Q96PL2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96PL2; protein.
DR Bgee; ENSG00000119913; Expressed in pigmented layer of retina and 15 other tissues.
DR ExpressionAtlas; Q96PL2; baseline and differential.
DR Genevisible; Q96PL2; HS.
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:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
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 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..305
FT /note="Beta-tectorin"
FT /id="PRO_0000041741"
FT PROPEP 306..329
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041742"
FT DOMAIN 19..283
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT LIPID 305
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; 36956 MW; 0B4D379624F488D0 CRC64;
MVTKAFVLLA IFAEASAKSC APNKADVILV FCYPKTIITK IPECPYGWEV HQLALGGLCY
NGVHEGGYYQ FVIPDLSPKN KSYCGTQSEY KPPIYHFYSH IVSNDTTVIV KNQPVNYSFS
CTYHSTYLVN QAAFDQRVAT VHVKNGSMGT FESQLSLNFY TNAKFSIKKE APFVLEASEI
GSDLFAGVEA KGLSIRFKVV LNSCWATPSA DFMYPLQWQL INKGCPTDET VLVHENGRDH
RATFQFNAFR FQNIPKLSKV WLHCETFICD SEKLSCPVTC DKRKRLLRDQ TGGVLVVELS
LRSRGFSSLY SFSDVLHHLI MMLGICAVL
