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Q9YH85 (TECTA_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Alpha-tectorin
Gene names
Name:TECTA
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length2120 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the major non-collagenous components of the tectorial membrane. 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. Ref.3

Subunit structure

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

Tissue specificity

Expressed in the inner ear. Ref.1

Developmental stage

Apically located within the epithelium of the developing basilar papilla at days E5.5 to E8. As development proceeds, expression becomes restricted to the basal layer. In the utricle, alpha-tectorin is first expressed at E4.5. Ref.1

Domain

Zona pellucida domain may enable to form filaments.

Post-translational modification

At least 3 products of tectorin seem to exist: HMM, MMM and LMM. They may be generated by active processing or the result of proteolysis occurring between intrachain disulfide bonds.

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 NIDO domain.

Contains 3 TIL (trypsin inhibitory-like) domains.

Contains 1 VWFC domain.

Contains 4 VWFD domains.

Contains 1 ZP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2
Chain25 – 20582034Alpha-tectorin
PRO_0000041739
Propeptide2059 – 212062Removed in mature form Potential
PRO_0000041740

Regions

Domain98 – 252155NIDO
Domain260 – 31253VWFC
Domain318 – 520203VWFD 1
Domain578 – 62043TIL 1
Domain691 – 908218VWFD 2
Domain963 – 101351TIL 2
Domain1067 – 1289223VWFD 3
Domain1345 – 139854TIL 3
Domain1459 – 1674216VWFD 4
Domain1772 – 2026255ZP
Compositional bias2091 – 20944Poly-Ser

Amino acid modifications

Lipidation20581GPI-anchor amidated asparagine Potential
Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation4961N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation7921N-linked (GlcNAc...) Potential
Glycosylation8221N-linked (GlcNAc...) Potential
Glycosylation8341N-linked (GlcNAc...) Potential
Glycosylation8771N-linked (GlcNAc...) Potential
Glycosylation8991N-linked (GlcNAc...) Potential
Glycosylation9071N-linked (GlcNAc...) Potential
Glycosylation9281N-linked (GlcNAc...) Potential
Glycosylation10251N-linked (GlcNAc...) Potential
Glycosylation10411N-linked (GlcNAc...) Potential
Glycosylation12071N-linked (GlcNAc...) Potential
Glycosylation13371N-linked (GlcNAc...) Potential
Glycosylation15111N-linked (GlcNAc...) Potential
Glycosylation15371N-linked (GlcNAc...) Potential
Glycosylation17231N-linked (GlcNAc...) Potential
Glycosylation17391N-linked (GlcNAc...) Potential
Glycosylation17611N-linked (GlcNAc...) Potential
Glycosylation18181N-linked (GlcNAc...) Potential
Glycosylation18311N-linked (GlcNAc...) Potential
Glycosylation18471N-linked (GlcNAc...) Potential
Glycosylation18871N-linked (GlcNAc...) Potential
Glycosylation19061N-linked (GlcNAc...) Potential
Disulfide bond1947 ↔ 2007 By similarity

Experimental info

Sequence conflict1114 – 11152Missing AA sequence Ref.2
Sequence conflict11231Missing AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9YH85 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E93F69EA18B51A4C

FASTA2,120233,965
        10         20         30         40         50         60 
MNTRSLLSAW AALLVVTVRH RAHAMASLYP FWPNDTKTPK VDDGSSSEIK LSVPFIFFRS 

        70         80         90        100        110        120 
PYRTVYVNNN GVISFNSLVS QFTPEAFPLA DGRAFVAPFC GDVANGIRGE IYYRESTNPE 

       130        140        150        160        170        180 
LLGESSKDIR KYFKDMASFS ASWVFIVTWE EVQFYGGSST TPVNTFQAVL ITDGVSSFAI 

       190        200        210        220        230        240 
FNYQEISWTT GTASGGDPLT GLGGVMAQAG FNGGNISNFF SIPGSRTPDI VNIEQTTNVN 

       250        260        270        280        290        300 
IPGRWAFKID GREIDPANLS LRGQFLHQGE IFWENSNCST KCRCLDFNNE IFCQEMLAPF 

       310        320        330        340        350        360 
ETVEPKIKFF QCVPVETACV VFGDPHYHTF DGFLFHFQGS CSYLLARQCW PGSQLPYFNV 

       370        380        390        400        410        420 
EAKNERGGSS VSWAEDIFVE VYRHKIVLPK GGFGKAKVDD LVVSLGAIKV YQSGLSTALE 

       430        440        450        460        470        480 
TDFGLLVTYD GQHYASVSVP GTYINGTCGL CGNYNKDPED DALRSDGRLA SSVPELGESW 

       490        500        510        520        530        540 
RVPHPERKCS PGCVENCSVC DASRILYSPI CGFSQECGAW SVLVATAFVH SCVYDLCSAR 

       550        560        570        580        590        600 
RTHRLCQAIQ VTLRCCQGLG IRWENGVPDG MRGGLAVPGH SHYSGCASGC PATCSDLTAP 

       610        620        630        640        650        660 
LRCTAPCPEG CECDDGHVLS ARPLHSLCRS GCVVDGRSRC REVFWATADC TAECQCEDGG 

       670        680        690        700        710        720 
EAKCFNTSCP EGEVCTIEDG YRGCYPKREG LCSVGQNQVL RTFDGVTFPY PLEHSYTLLK 

       730        740        750        760        770        780 
TCMEKPDFIE VDISQKKPDT LPMAGRVVRI QVVGQEVKVG GASLSEVKVN GYDVDLPYFH 

       790        800        810        820        830        840 
PSGHLEIYRT DNGTVTESEG LLSIGYYDSG LLEIRLSTAY FNCTGGLCGF FNGNDSDEFC 

       850        860        870        880        890        900 
TPKAKCTDNL ELFLESWTTF DEICNGECGD LLKACNNDSE LLKTYRSRSN CAIINDPTNS 

       910        920        930        940        950        960 
SFLECHNVSI VSAYYRTCLF RLCQSGGNQS ELCSAVARYA SACKNSEVDV GQWRSHSFCP 

       970        980        990       1000       1010       1020 
LACPENSHFE ECMSCVETCE TLATGCCMDT CTEGCQCDEG FALRSPCVPR GECGCNFEGH 

      1030       1040       1050       1060       1070       1080 
ELATNQTFWM DISCHLLCYC NGSDNSVYCE NVLQDDEYYC HVRTDASCIV SGYGHYLTFD 

      1090       1100       1110       1120       1130       1140 
GFSFDFQSSC ALVLCTTIHG ACERSDTFPT FTVTVTAKNE DRDTSLACVV KQVEVEVFNY 

      1150       1160       1170       1180       1190       1200 
YIVIHRAYKY TVMINNERLY LPLKLGQGKV NIFAFGFHIV VETDFGLKVV YDWKTFLSVT 

      1210       1220       1230       1240       1250       1260 
IPRSFQNLTY GLCGRYNGNP DDDLVAAGGT PRFGVTDFVQ SWAKRDTFCR VGSGDRCPAC 

      1270       1280       1290       1300       1310       1320 
GKVEGFWKPQ QLCSLIPSQS GVFAKCHSKI NPSYFYKNCL FDTVVDGGAM ARRVADWLQN 

      1330       1340       1350       1360       1370       1380 
YASTCQTQGI AIIGWRNFTS CSVSCPPNSH YESCVSLCQP RCAAIRLKSD CGHYCVEGCQ 

      1390       1400       1410       1420       1430       1440 
CDPGYVLNGK SCILPQNCGC YSDGKYYEPK QLFWNGDCTR RCARFRRNLI QCDPRHCKSD 

      1450       1460       1470       1480       1490       1500 
EECASRNGVR GCFSTRSSFC LAAGGGVFRT FDGAFLRFPA NCAFVLSTIC QRLADFSFQL 

      1510       1520       1530       1540       1550       1560 
IINFDKWSSP NLTIISVYIY INEEQILISD RSTVKVNGSL VSIPFVTGLS TKIYSQEGFL 

      1570       1580       1590       1600       1610       1620 
VIDSGPDIHI RYNGFNVIKI TIGDRLQNKV CGLCGNFNGD PADDYATLRG KPVVSSVVLA 

      1630       1640       1650       1660       1670       1680 
QSWKTNGMQK SCNELQYSQY AASCDNVQIQ KLQSDSYCLK LTDMKGFFQP CYGLLDPLPF 

      1690       1700       1710       1720       1730       1740 
YESCFLDGCY NRKQVQLCGS LAAYGEACRT FGILGTEWIE KENCSGVVED PCAGADCPNR 

      1750       1760       1770       1780       1790       1800 
TCELDDGGEL CGCIEPPPYG NTTHDIIDAE VTCKAAQMEV SISKCKLFQL GFEREGVRVN 

      1810       1820       1830       1840       1850       1860 
DRHCPGIEGE DFISFQINNT KGNCGNLVQS NSTHIVYKNT VWIESANNTG NIITRDRTIN 

      1870       1880       1890       1900       1910       1920 
VEVFCAYELD IKISLDSVVR PMLSVINLTV PTQEGSFTTK MALYKNSSYK HPYRQGEVVL 

      1930       1940       1950       1960       1970       1980 
TTRDVLYVGV FVVGADSNHL ILMLNKCYAT PSRDSNDKLR YFIIEGGCQN LKDNTIGIEE 

      1990       2000       2010       2020       2030       2040 
NGVSLTCRFH VTVFKFIGDY DEVHLHCAVS LCDSEKYSCK INCPQHRRSA SAFAQEAHEQ 

      2050       2060       2070       2080       2090       2100 
ILSVGPIRRK RSDWCEDNGG CEQICTSQAD GPLCSCVTGT LQGDGKSCMA SSSSADIRAQ 

      2110       2120 
ASLLVAAQLW LWAALHDPTS 

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References

[1]"Chick alpha-tectorin: molecular cloning and expression during embryogenesis."
Coutinho P., Goodyear R., Legan P.K., Richardson G.P.
Hear. Res. 130:62-74(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Cochlear duct.
[2]"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: PROTEIN SEQUENCE OF 25-33; 325-334 AND 1105-1124.
[3]"The protein composition of the avian tectorial membrane."
Killick R., Malenczak C., Richardson G.P.
Hear. Res. 64:21-38(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ012287 mRNA. Translation: CAA09979.1.
PIRT30243.
RefSeqNP_990204.1. NM_204873.1.
UniGeneGga.399.

3D structure databases

ProteinModelPortalQ9YH85.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000010663.

Proteomic databases

PaxDbQ9YH85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395686.
KEGGgga:395686.

Organism-specific databases

CTD7007.

Phylogenomic databases

eggNOGNOG317991.
HOVERGENHBG079244.
KOK18273.
PhylomeDBQ9YH85.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16938.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR003886. Nidogen_extracell_dom.
IPR002919. TIL_dom.
IPR025615. TILa_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR006552. VWC_out.
IPR001846. VWF_type-D.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamPF08742. C8. 3 hits.
PF06119. NIDO. 1 hit.
PF01826. TIL. 3 hits.
PF12714. TILa. 2 hits.
PF00094. VWD. 4 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
SMARTSM00832. C8. 3 hits.
SM00181. EGF. 1 hit.
SM00539. NIDO. 1 hit.
SM00215. VWC_out. 1 hit.
SM00216. VWD. 4 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMSSF57567. SSF57567. 3 hits.
PROSITEPS51220. NIDO. 1 hit.
PS51233. VWFD. 4 hits.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20815758.
PROQ9YH85.

Entry information

Entry nameTECTA_CHICK
AccessionPrimary (citable) accession number: Q9YH85
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 90 of the entry and version 1 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