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O08524 (TECTB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-tectorin
Gene names
Name:Tectb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

One of the major non-collagenous components of the tectorial membrane By similarity. The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals.

Subunit structure

May form homomeric filament after self-association or heteromeric filament after association with alpha-tectorin.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor; Extracellular side Probable. Secretedextracellular spaceextracellular matrix. Note: Found in the non-collagenous matrix of the tectorial membrane By similarity.

Domain

Zona pellucida domain may enable to form filaments.

Post-translational modification

The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment.

Sequence similarities

Contains 1 ZP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 305288Beta-tectorin
PRO_0000041743
Propeptide306 – 32924Removed in mature form Potential
PRO_0000041744

Regions

Domain19 – 283265ZP

Amino acid modifications

Lipidation3051GPI-anchor amidated alanine Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Disulfide bond204 ↔ 264 By similarity

Sequences

Sequence LengthMass (Da)Tools
O08524 [UniParc].

Last modified October 1, 2000. Version 2.
Checksum: CC69A33EBC270AB3

FASTA32936,986
        10         20         30         40         50         60 
MVVRAFVLLA LFAEASAKSC TPNKADVILV FCYPKTIITK IPECPYGWEV HQLALGGLCY 

        70         80         90        100        110        120 
NGVHEGGYYQ FVIPDLSPKN KSYCGTQSEY KPPIYHFYSH IVSNDSTVIV KNQPVNYSFS 

       130        140        150        160        170        180 
CTYHSTYLVN QAAFDQRVAT VHVKNGSMGT FESQLSLNFY TNAKFSTKKE APFVLETSEI 

       190        200        210        220        230        240 
GSDLFAGVEA KGLSVRFKVV LNSCWATPSA DFMYPLQWQL INKGCPTDET VLVHENGKDH 

       250        260        270        280        290        300 
RATFQFNAFR FQNIPKLSKV WLHCETFICD SEKLSCPVNC DKRKRMLRDQ TGGVLVVELS 

       310        320 
LRSRAFSGLC DFSDVLLHLI LMLGTWAVL 

« Hide

References

[1]"The mouse tectorins. Modular matrix proteins of the inner ear homologous to components of the sperm-egg adhesion system."
Legan P.K., Rau A., Keene J.N., Richardson G.P.
J. Biol. Chem. 272:8791-8801(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
Tissue: Cochlea.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99806 mRNA. Translation: CAA68139.2.
CCDSCCDS29907.1.
RefSeqNP_033374.2. NM_009348.3.
XP_006526966.1. XM_006526903.1.
UniGeneMm.42139.

3D structure databases

ProteinModelPortalO08524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000113805.

Proteomic databases

PRIDEO08524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025936; ENSMUSP00000025936; ENSMUSG00000024979.
GeneID21684.
KEGGmmu:21684.
UCSCuc008hxm.1. mouse.

Organism-specific databases

CTD6975.
MGIMGI:109574. Tectb.

Phylogenomic databases

eggNOGNOG44475.
HOGENOMHOG000124070.
HOVERGENHBG056825.
PhylomeDBO08524.
TreeFamTF330284.

Gene expression databases

BgeeO08524.
CleanExMM_TECTB.
GenevestigatorO08524.

Family and domain databases

InterProIPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamPF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSPR00023. ZPELLUCIDA.
SMARTSM00241. ZP. 1 hit.
[Graphical view]
PROSITEPS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301000.
PROO08524.
SOURCESearch...

Entry information

Entry nameTECTB_MOUSE
AccessionPrimary (citable) accession number: O08524
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot