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Protein

Tenascin-R

Gene

TNR

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. Involved in cell attachment and neurite formation. Interaction with CNTN1 enhances the neurite outgrowth.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Tenascin-R
Short name:
TN-R
Alternative name(s):
Restrictin
Gene namesi
Name:TNR
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence analysisAdd
BLAST
Chaini34 – 13531320Tenascin-RPRO_0000007750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi296 ↔ 306PROSITE-ProRule annotation
Disulfide bondi313 ↔ 322PROSITE-ProRule annotation
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence analysis
Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence analysis
Glycosylationi580 – 5801N-linked (GlcNAc...)Sequence analysis
Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence analysis
Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence analysis
Glycosylationi872 – 8721N-linked (GlcNAc...)Sequence analysis
Glycosylationi1031 – 10311N-linked (GlcNAc...)Sequence analysis
Glycosylationi1041 – 10411N-linked (GlcNAc...)Sequence analysis
Glycosylationi1256 – 12561N-linked (GlcNAc...)Sequence analysis
Glycosylationi1342 – 13421N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ00546.

Expressioni

Tissue specificityi

Brain specific.1 Publication

Developmental stagei

Expression weakly detectable at E6 embryo, reaches a maximum at E16 and declines in the adult.1 Publication

Interactioni

Subunit structurei

Forms homodimers and homotrimers. Interacts with CNTN1, NFASC and CSPG5.5 Publications

Protein-protein interaction databases

STRINGi9031.ENSGALP00000007195.

Structurei

3D structure databases

ProteinModelPortaliQ00546.
SMRiQ00546. Positions 502-770.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini187 – 19812EGF-like 1Add
BLAST
Domaini234 – 26027EGF-like 2Add
BLAST
Domaini265 – 29127EGF-like 3Add
BLAST
Domaini292 – 32332EGF-like 4Add
BLAST
Domaini327 – 41993Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini420 – 50485Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini505 – 59490Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini595 – 68692Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini687 – 77690Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini777 – 86387Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini864 – 95289Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini953 – 103785Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1038 – 112689Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1124 – 1339216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili132 – 15625Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi154 – 313160Cys-richAdd
BLAST

Domaini

The N-terminus cysteine-rich segment may mediate the formation of oligomers. The fibronectin type-III 2-3 mediate the binding to contactin 1. The fibronectin type-III 9 mediates the cell attachment. The fibronectin type-III 2-5 mediate NFASC binding. The fibrinogen C-terminal domain mediates interaction with CSPG5.1 Publication

Sequence similaritiesi

Belongs to the tenascin family.Curated
Contains 4 EGF-like domains.Curated
Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation
Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ00546.
KOiK06252.
PhylomeDBiQ00546.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR033079. TNR.
[Graphical view]
PANTHERiPTHR19143:SF254. PTHR19143:SF254. 2 hits.
PfamiPF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 9 hits.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 9 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 4 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 9 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q00546-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGTDSENPVL RNVLISFNLL LLGAVLKPFE CRLEVTTEPA ERPAVDEEGG
60 70 80 90 100
LANCSPPVKE QPMVFHHIYN INVPVDSCCS SMLRSSAEEV SSEDDRLAEY
110 120 130 140 150
TEQTSDSESQ VTFTHRINLP KQACKCSTSL PSLQELLSRI EMLEREVSML
160 170 180 190 200
RDQCNSNCCQ ENAATGRLDY TLPCSGHGNF SLESCRCICS EGWAGSNCSE
210 220 230 240 250
PRCPRGCSSR GVCLEGQCVC DNDYGGEDCS QLRCPAGCGS RGLCVDGECI
260 270 280 290 300
CEEGFGGEDC SQPRCPRDCS GRGHCDNGTC VCAEGYAGED CGWLRCPNAC
310 320 330 340 350
SGRGVCQDGL CICEDGYGGQ DCSAVAPPEN LRVTGISDGS IELAWDSLGA
360 370 380 390 400
ATEYVVSYQP AGPGGSQLQQ RVPGDWSTIT ITELEPGVAY NVSIYAVISD
410 420 430 440 450
VLSSPVTTKV TTNLATPQGL KFKTITETTV EVQWEPFSFP FDGWEISFIP
460 470 480 490 500
KNNEGGVIAQ LPSTVTTFNQ TGLKPGEEYT VTVVALKDQA RSPPASDSIS
510 520 530 540 550
TLIDGPTQIL VRDVSDTVAF VEWTPPRARV DAILLKYGLA DGEGGRTTFR
560 570 580 590 600
LQPPLSQYSL QALRPGARYH LAVSALRGAN ESQPALAQFT TEIDAPKNLR
610 620 630 640 650
VGSRTPASLE LTWDNSEAEA HSYRVVYSTL AGEHYHEVLV PRDTGPTTRA
660 670 680 690 700
TLADLVPGTE YGIGISAVMD SQQSVPATMN ARTELDSPRD LLVTASTETS
710 720 730 740 750
ISLSWTKAMG PIDHYRVTFT PASGMASEVT VSRNESQLTL SELEPGTEYT
760 770 780 790 800
ISIIAERGRQ QSLEATVDAF TGVRPITQLH FSQLTSSSVN ITWSDPSPPA
810 820 830 840 850
DRLVLTYSPR DEEAPQQLAL DGTRRHASLT GLRPSTEYLV SLVAVHGAVS
860 870 880 890 900
SEPVTGSITT GMDAPKDLRV GNITQDSMVI YWSPPVAPFD HYRISYRAAE
910 920 930 940 950
GRTDSTAIGN DATEYIMRLL QPATKYEIGV KSVRGREESE VASITTYTAM
960 970 980 990 1000
DAPLGVTATN ITPTEALLQW NPPLMDVESY VLVLTRHTGE TILVDGINQE
1010 1020 1030 1040 1050
YQLTNLQPST TYTVAMYATN GPLTSQTIST NFTTLLDPPT NLTASEVTRR
1060 1070 1080 1090 1100
SALLSWVPPV GDIENYILTY RSTDGSRKEL IVDAEDTWIR LEGLSETTQY
1110 1120 1130 1140 1150
TVRLQAAQNA MRSGFISTTF TTGGRVFANP QDCAQHLMNG DTLSGVYTIS
1160 1170 1180 1190 1200
INGDLSQRVQ VFCDMSTDGG GWIVFQRRQN GLTDFFRKWA DYRVGFGNLE
1210 1220 1230 1240 1250
DEFWLGLDNI HKITSQGRYE LRIDMRDGQE AAYAYYDKFS VGDSRSLYKL
1260 1270 1280 1290 1300
RIGDYNGTSG DSLTYHQGRP FSTKDRDNDV AVTNCAMSYK GAWWYKNCHR
1310 1320 1330 1340 1350
TNLNGKYGES RHSQGINWYH WKGHEFSIPF VEMKMRPYNH RNISGRKRRS

LQL
Length:1,353
Mass (Da):148,280
Last modified:November 1, 1996 - v1
Checksum:iCD8393C4203171D9
GO
Isoform 2 (identifier: Q00546-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-134: Missing.

Show »
Length:1,308
Mass (Da):143,266
Checksum:i8EF2E57806262A09
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 13445Missing in isoform 2. 1 PublicationVSP_012996Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64649 mRNA. Translation: CAA45920.1.
PIRiJH0675.
RefSeqiNP_990607.2. NM_205276.3.
UniGeneiGga.711.

Genome annotation databases

GeneIDi396213.
KEGGigga:396213.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64649 mRNA. Translation: CAA45920.1.
PIRiJH0675.
RefSeqiNP_990607.2. NM_205276.3.
UniGeneiGga.711.

3D structure databases

ProteinModelPortaliQ00546.
SMRiQ00546. Positions 502-770.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000007195.

Proteomic databases

PaxDbiQ00546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396213.
KEGGigga:396213.

Organism-specific databases

CTDi7143.

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ00546.
KOiK06252.
PhylomeDBiQ00546.

Miscellaneous databases

NextBioi20816265.
PROiQ00546.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR033079. TNR.
[Graphical view]
PANTHERiPTHR19143:SF254. PTHR19143:SF254. 2 hits.
PfamiPF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 9 hits.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 9 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 4 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs."
    Noerenberg U., Wille H., Wolff J.M., Frank R., Rathjen F.G.
    Neuron 8:849-863(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 579-586 AND 827-840, DEVELOPMENTAL STAGE, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R."
    Noerenberg U., Hubert M., Bruemmendorf T., Tarnok A., Rathjen F.G.
    J. Cell Biol. 130:473-484(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNTN1, FUNCTION, CELL ATTACHMENT SITE.
  3. "Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells."
    Volkmer H., Zacharias U., Noerenberg U., Rathjen F.G.
    J. Cell Biol. 142:1083-1093(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFASC.
  4. "Chicken acidic leucine-rich EGF-like domain containing brain protein (CALEB), a neural member of the EGF family of differentiation factors, is implicated in neurite formation."
    Schumacher S., Volkmer H., Buck F., Otto A., Tarnok A., Roth S., Rathjen F.G.
    J. Cell Biol. 136:895-906(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG5.
  5. "CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesion."
    Schumacher S., Jung M., Noerenberg U., Dorner A., Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.
    J. Biol. Chem. 276:7337-7345(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG5, DOMAIN.

Entry informationi

Entry nameiTENR_CHICK
AccessioniPrimary (citable) accession number: Q00546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 110 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.