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Protein

Alpha-tectorin

Gene

TECTA

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hearing

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-tectorin
Gene namesi
Name:TECTA
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000004173925 – 2058Alpha-tectorinAdd BLAST2034
PropeptideiPRO_00000417402059 – 2120Removed in mature formSequence analysisAdd BLAST62

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34N-linked (GlcNAc...)Sequence analysis1
Glycosylationi215N-linked (GlcNAc...)Sequence analysis1
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Glycosylationi277N-linked (GlcNAc...)Sequence analysis1
Glycosylationi445N-linked (GlcNAc...)Sequence analysis1
Glycosylationi496N-linked (GlcNAc...)Sequence analysis1
Glycosylationi666N-linked (GlcNAc...)Sequence analysis1
Glycosylationi792N-linked (GlcNAc...)Sequence analysis1
Glycosylationi822N-linked (GlcNAc...)Sequence analysis1
Glycosylationi834N-linked (GlcNAc...)Sequence analysis1
Glycosylationi877N-linked (GlcNAc...)Sequence analysis1
Glycosylationi899N-linked (GlcNAc...)Sequence analysis1
Glycosylationi907N-linked (GlcNAc...)Sequence analysis1
Glycosylationi928N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1025N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1041N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1207N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1337N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1511N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1537N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1684 ↔ 1742By similarity
Disulfide bondi1708 ↔ 1751By similarity
Glycosylationi1723N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1739N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1753 ↔ 1785By similarity
Glycosylationi1761N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1773 ↔ 1865By similarity
Disulfide bondi1804 ↔ 1824By similarity
Glycosylationi1818N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1831N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1847N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1887N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1906N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1947 ↔ 2007PROSITE-ProRule annotation
Disulfide bondi1968 ↔ 2023By similarity
Disulfide bondi2012 ↔ 2019By similarity
Lipidationi2058GPI-anchor amidated asparagineSequence analysis1

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Tissue specificityi

Expressed in the inner ear.1 Publication

Developmental stagei

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 E4.5.1 Publication

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ9YH85.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 252NIDOPROSITE-ProRule annotationAdd BLAST155
Domaini260 – 312VWFCAdd BLAST53
Domaini318 – 520VWFD 1PROSITE-ProRule annotationAdd BLAST203
Domaini578 – 620TIL 1Add BLAST43
Domaini691 – 908VWFD 2PROSITE-ProRule annotationAdd BLAST218
Domaini963 – 1013TIL 2Add BLAST51
Domaini1067 – 1289VWFD 3PROSITE-ProRule annotationAdd BLAST223
Domaini1345 – 1398TIL 3Add BLAST54
Domaini1459 – 1674VWFD 4PROSITE-ProRule annotationAdd BLAST216
Domaini1772 – 2026ZPPROSITE-ProRule annotationAdd BLAST255

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2091 – 2094Poly-Ser4

Domaini

Zona pellucida domain may enable to form filaments.

Sequence similaritiesi

Contains 1 NIDO domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.Curated
Contains 4 VWFD domains.PROSITE-ProRule annotation
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG079244.
InParanoidiQ9YH85.
PhylomeDBiQ9YH85.

Family and domain databases

InterProiIPR003886. NIDO_dom.
IPR033026. TECTA.
IPR002919. TIL_dom.
IPR025615. TILa_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PANTHERiPTHR11339:SF235. PTHR11339:SF235. 2 hits.
PfamiPF08742. C8. 3 hits.
PF06119. NIDO. 1 hit.
PF01826. TIL. 3 hits.
PF12714. TILa. 1 hit.
PF00094. VWD. 4 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
SMARTiSM00832. C8. 3 hits.
SM00539. NIDO. 1 hit.
SM00215. VWC_out. 2 hits.
SM00216. VWD. 4 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF57567. SSF57567. 3 hits.
PROSITEiPS51220. NIDO. 1 hit.
PS51233. VWFD. 4 hits.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9YH85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTRSLLSAW AALLVVTVRH RAHAMASLYP FWPNDTKTPK VDDGSSSEIK
60 70 80 90 100
LSVPFIFFRS PYRTVYVNNN GVISFNSLVS QFTPEAFPLA DGRAFVAPFC
110 120 130 140 150
GDVANGIRGE IYYRESTNPE LLGESSKDIR KYFKDMASFS ASWVFIVTWE
160 170 180 190 200
EVQFYGGSST TPVNTFQAVL ITDGVSSFAI FNYQEISWTT GTASGGDPLT
210 220 230 240 250
GLGGVMAQAG FNGGNISNFF SIPGSRTPDI VNIEQTTNVN IPGRWAFKID
260 270 280 290 300
GREIDPANLS LRGQFLHQGE IFWENSNCST KCRCLDFNNE IFCQEMLAPF
310 320 330 340 350
ETVEPKIKFF QCVPVETACV VFGDPHYHTF DGFLFHFQGS CSYLLARQCW
360 370 380 390 400
PGSQLPYFNV EAKNERGGSS VSWAEDIFVE VYRHKIVLPK GGFGKAKVDD
410 420 430 440 450
LVVSLGAIKV YQSGLSTALE TDFGLLVTYD GQHYASVSVP GTYINGTCGL
460 470 480 490 500
CGNYNKDPED DALRSDGRLA SSVPELGESW RVPHPERKCS PGCVENCSVC
510 520 530 540 550
DASRILYSPI CGFSQECGAW SVLVATAFVH SCVYDLCSAR RTHRLCQAIQ
560 570 580 590 600
VTLRCCQGLG IRWENGVPDG MRGGLAVPGH SHYSGCASGC PATCSDLTAP
610 620 630 640 650
LRCTAPCPEG CECDDGHVLS ARPLHSLCRS GCVVDGRSRC REVFWATADC
660 670 680 690 700
TAECQCEDGG EAKCFNTSCP EGEVCTIEDG YRGCYPKREG LCSVGQNQVL
710 720 730 740 750
RTFDGVTFPY PLEHSYTLLK TCMEKPDFIE VDISQKKPDT LPMAGRVVRI
760 770 780 790 800
QVVGQEVKVG GASLSEVKVN GYDVDLPYFH PSGHLEIYRT DNGTVTESEG
810 820 830 840 850
LLSIGYYDSG LLEIRLSTAY FNCTGGLCGF FNGNDSDEFC TPKAKCTDNL
860 870 880 890 900
ELFLESWTTF DEICNGECGD LLKACNNDSE LLKTYRSRSN CAIINDPTNS
910 920 930 940 950
SFLECHNVSI VSAYYRTCLF RLCQSGGNQS ELCSAVARYA SACKNSEVDV
960 970 980 990 1000
GQWRSHSFCP LACPENSHFE ECMSCVETCE TLATGCCMDT CTEGCQCDEG
1010 1020 1030 1040 1050
FALRSPCVPR GECGCNFEGH ELATNQTFWM DISCHLLCYC NGSDNSVYCE
1060 1070 1080 1090 1100
NVLQDDEYYC HVRTDASCIV SGYGHYLTFD GFSFDFQSSC ALVLCTTIHG
1110 1120 1130 1140 1150
ACERSDTFPT FTVTVTAKNE DRDTSLACVV KQVEVEVFNY YIVIHRAYKY
1160 1170 1180 1190 1200
TVMINNERLY LPLKLGQGKV NIFAFGFHIV VETDFGLKVV YDWKTFLSVT
1210 1220 1230 1240 1250
IPRSFQNLTY GLCGRYNGNP DDDLVAAGGT PRFGVTDFVQ SWAKRDTFCR
1260 1270 1280 1290 1300
VGSGDRCPAC GKVEGFWKPQ QLCSLIPSQS GVFAKCHSKI NPSYFYKNCL
1310 1320 1330 1340 1350
FDTVVDGGAM ARRVADWLQN YASTCQTQGI AIIGWRNFTS CSVSCPPNSH
1360 1370 1380 1390 1400
YESCVSLCQP RCAAIRLKSD CGHYCVEGCQ CDPGYVLNGK SCILPQNCGC
1410 1420 1430 1440 1450
YSDGKYYEPK QLFWNGDCTR RCARFRRNLI QCDPRHCKSD EECASRNGVR
1460 1470 1480 1490 1500
GCFSTRSSFC LAAGGGVFRT FDGAFLRFPA NCAFVLSTIC QRLADFSFQL
1510 1520 1530 1540 1550
IINFDKWSSP NLTIISVYIY INEEQILISD RSTVKVNGSL VSIPFVTGLS
1560 1570 1580 1590 1600
TKIYSQEGFL VIDSGPDIHI RYNGFNVIKI TIGDRLQNKV CGLCGNFNGD
1610 1620 1630 1640 1650
PADDYATLRG KPVVSSVVLA QSWKTNGMQK SCNELQYSQY AASCDNVQIQ
1660 1670 1680 1690 1700
KLQSDSYCLK LTDMKGFFQP CYGLLDPLPF YESCFLDGCY NRKQVQLCGS
1710 1720 1730 1740 1750
LAAYGEACRT FGILGTEWIE KENCSGVVED PCAGADCPNR TCELDDGGEL
1760 1770 1780 1790 1800
CGCIEPPPYG NTTHDIIDAE VTCKAAQMEV SISKCKLFQL GFEREGVRVN
1810 1820 1830 1840 1850
DRHCPGIEGE DFISFQINNT KGNCGNLVQS NSTHIVYKNT VWIESANNTG
1860 1870 1880 1890 1900
NIITRDRTIN VEVFCAYELD IKISLDSVVR PMLSVINLTV PTQEGSFTTK
1910 1920 1930 1940 1950
MALYKNSSYK HPYRQGEVVL TTRDVLYVGV FVVGADSNHL ILMLNKCYAT
1960 1970 1980 1990 2000
PSRDSNDKLR YFIIEGGCQN LKDNTIGIEE NGVSLTCRFH VTVFKFIGDY
2010 2020 2030 2040 2050
DEVHLHCAVS LCDSEKYSCK INCPQHRRSA SAFAQEAHEQ ILSVGPIRRK
2060 2070 2080 2090 2100
RSDWCEDNGG CEQICTSQAD GPLCSCVTGT LQGDGKSCMA SSSSADIRAQ
2110 2120
ASLLVAAQLW LWAALHDPTS
Length:2,120
Mass (Da):233,965
Last modified:May 1, 1999 - v1
Checksum:iE93F69EA18B51A4C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1114 – 1115Missing AA sequence (PubMed:9079715).Curated2
Sequence conflicti1123Missing AA sequence (PubMed:9079715).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012287 mRNA. Translation: CAA09979.1.
PIRiT30243.
UniGeneiGga.399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012287 mRNA. Translation: CAA09979.1.
PIRiT30243.
UniGeneiGga.399.

3D structure databases

ProteinModelPortaliQ9YH85.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG079244.
InParanoidiQ9YH85.
PhylomeDBiQ9YH85.

Family and domain databases

InterProiIPR003886. NIDO_dom.
IPR033026. TECTA.
IPR002919. TIL_dom.
IPR025615. TILa_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PANTHERiPTHR11339:SF235. PTHR11339:SF235. 2 hits.
PfamiPF08742. C8. 3 hits.
PF06119. NIDO. 1 hit.
PF01826. TIL. 3 hits.
PF12714. TILa. 1 hit.
PF00094. VWD. 4 hits.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
SMARTiSM00832. C8. 3 hits.
SM00539. NIDO. 1 hit.
SM00215. VWC_out. 2 hits.
SM00216. VWD. 4 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF57567. SSF57567. 3 hits.
PROSITEiPS51220. NIDO. 1 hit.
PS51233. VWFD. 4 hits.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTECTA_CHICK
AccessioniPrimary (citable) accession number: Q9YH85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.