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Protein

Tenascin-R

Gene

Tnr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. Theses interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediates inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity).By similarity3 Publications

GO - Molecular functioni

  • integrin binding Source: RGD

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • negative regulation of cell adhesion Source: RGD
  • nervous system development Source: RGD
  • regulation of neurogenesis Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Sialic acid

Names & Taxonomyi

Protein namesi
Recommended name:
Tenascin-R
Short name:
TN-R
Alternative name(s):
Janusin
Neural recognition molecule J1-160/180
Restrictin
Gene namesi
Name:Tnr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3886. Tnr.

Subcellular locationi

GO - Cellular componenti

  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000000774932 – 1356Tenascin-RAdd BLAST1325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi55N-linked (GlcNAc...)Sequence analysis1
Glycosylationi180N-linked (GlcNAc...)Sequence analysis1
Glycosylationi198N-linked (GlcNAc...)Sequence analysis1
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi297 ↔ 307PROSITE-ProRule annotation
Disulfide bondi314 ↔ 323PROSITE-ProRule annotation
Glycosylationi391N-linked (GlcNAc...)Sequence analysis1
Glycosylationi469N-linked (GlcNAc...)Sequence analysis1
Glycosylationi580N-linked (GlcNAc...)Sequence analysis1
Modified residuei723PhosphoserineCombined sources1
Glycosylationi790N-linked (GlcNAc...)Sequence analysis1
Glycosylationi868N-linked (GlcNAc...)Sequence analysis1
Glycosylationi873N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1034N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1044N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1259N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Contains N-linked oligosaccharides, O-linked sialylated structures (By similarity). Contains O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked oligosaccharides with a sulfated carbohydrate structure type GalNAc-4-SO4 or HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc). The levels of HNK-1 rise and fall in parallel to those of TNR during postnatal development of the cerebellum. In contrast, levels of GalNAc-4-SO4 are regulated independently from those of TNR, rising late in cerebellar development and continuing into adulthood. Early in postnatal development, GalNAc-4-SO4 is found predominantly on isoform 1, whereas in the adult it is predominantly on isoform 2.By similarity3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

PRIDEiQ05546.

PTM databases

iPTMnetiQ05546.
PhosphoSitePlusiQ05546.
UniCarbKBiQ05546.

Expressioni

Tissue specificityi

Brain-specific. Expressed in oligodendrocytes and small subsets of neurons (mainly interneurons and motoneurons) of the cerebellum, hippocampus and olfactory bulb.1 Publication

Developmental stagei

Expression in oligodendrocytes is highest between the second and third postnatal week and low in the adult. In contrast the expression in neurons increases from birth to third postnatal week and is continuous from late development to adulthood. Isoform 1 is the dominant form early in development. Isoform 2 is more prominent later in development and in adulthood.2 Publications

Interactioni

Subunit structurei

Forms oligomers. Interacts with TNC and FN1 (By similarity). Interacts with BCAN and ACAN in a calcium -dependent manner. Interacts with CNTN1, SCN2B, PTPRZ1, and CSPG3.By similarity5 Publications

GO - Molecular functioni

  • integrin binding Source: RGD

Protein-protein interaction databases

BioGridi247598. 1 interactor.
IntActiQ05546. 1 interactor.

Structurei

Secondary structure

11356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi507 – 514Combined sources8
Beta strandi519 – 524Combined sources6
Beta strandi531 – 543Combined sources13
Beta strandi547 – 551Combined sources5
Beta strandi556 – 560Combined sources5
Beta strandi568 – 577Combined sources10
Beta strandi585 – 590Combined sources6
Beta strandi597 – 604Combined sources8
Beta strandi609 – 614Combined sources6
Beta strandi621 – 629Combined sources9
Beta strandi636 – 641Combined sources6
Beta strandi644 – 652Combined sources9
Beta strandi660 – 669Combined sources10
Beta strandi677 – 682Combined sources6
Beta strandi689 – 696Combined sources8
Beta strandi701 – 706Combined sources6
Beta strandi713 – 720Combined sources8
Beta strandi722 – 724Combined sources3
Beta strandi727 – 734Combined sources8
Beta strandi736 – 740Combined sources5
Beta strandi749 – 757Combined sources9
Beta strandi765 – 769Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TDQX-ray2.60A502-771[»]
ProteinModelPortaliQ05546.
SMRiQ05546.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05546.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini188 – 199EGF-like 1Add BLAST12
Domaini204 – 230EGF-like 2Add BLAST27
Domaini235 – 261EGF-like 3Add BLAST27
Domaini281 – 292EGF-like 4Add BLAST12
Domaini293 – 324EGF-like 5Add BLAST32
Domaini328 – 419Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST92
Domaini420 – 504Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST85
Domaini505 – 596Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini597 – 686Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST90
Domaini687 – 776Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST90
Domaini777 – 864Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST88
Domaini865 – 953Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST89
Domaini954 – 1040Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST87
Domaini1041 – 1129Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST89
Domaini1127 – 1342Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST216

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili127 – 157Sequence analysisAdd BLAST31

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi155 – 314Cys-richAdd BLAST160

Domaini

The EGF-like domains mediate interaction with CNTN1. The fibronectin type-III domains 3-5 mediate interaction with BCAN. The fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B.

Sequence similaritiesi

Belongs to the tenascin family.Curated
Contains 5 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

HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ05546.
KOiK06252.
PhylomeDBiQ05546.

Family and domain databases

CDDicd00063. FN3. 9 hits.
cd00087. FReD. 1 hit.
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: Q05546-1) [UniParc]FASTAAdd to basket
Also known as: TN-R 180, 180 kDa form

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
MGIEGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERV QRQTVEEEGG
60 70 80 90 100
ASSYNTSSKE QPMVFNHVYN INVPLESLCS SGLEASAEQD VSAEDDTLAE
110 120 130 140 150
YTGQTSDHES QVTFTHKINL PKKACPCASS AQVLQELLSR IEMLEREVSV
160 170 180 190 200
LRDQCNTNCC QESAATGQLD YVPHCSGHGN FSFESCGCIC NEGWFGKNCS
210 220 230 240 250
EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS SRGLCVDGEC
260 270 280 290 300
VCEEPYTGED CRELRCPGDC SGKGQCANGT CLCQEGYAGE DCSQRRCLNA
310 320 330 340 350
CSGRGHCQEG LCICEEGYQG PDCSAVTPPE DLRVAGISDR SIELEWDGPM
360 370 380 390 400
AVTEYVISYQ PSLGGLQLQQ RVPGDWSGVT ITELEPGLTY NISVYAVISN
410 420 430 440 450
ILSLPITAKV ATHLSTPQGL QFKTITETTV EVQWEPFSFS FDGWEISFTP
460 470 480 490 500
KNNEGGVIAQ LPSDVTSFNQ TGLKPGEEYI VNVVALKEQA RGPPTSASVS
510 520 530 540 550
TVIDGPTQIL VRDVSDTVAF VEWTPPRAKV DFILLKYGLV GGEGGKTTFR
560 570 580 590 600
LQPPLSQYSV QALRPGSRYE VSISAVRGTN ESDASSTQFT TEIDAPKNLR
610 620 630 640 650
VGSRTATSLD LEWDNSEAEA QEYKVVYSTL AGEQYHEVLV PKGIGPTTKT
660 670 680 690 700
TLTDLVPGTE YGVGISAVMN SKQSIPATMN ARTELDSPRD LMVTASSETS
710 720 730 740 750
ISLIWTKASG PIDHYRITFT PSSGISSEVT VPRDRTSYTL TDLEPGAEYI
760 770 780 790 800
ISITAERGRQ QSLESTVDAF TGFRPISHLH FSHVTSSSVN ITWSDPSPPA
810 820 830 840 850
DRLILNYSPR DEEEEMMEVL LDATKRHAVL MGLQPATEYI VNLVAVHGTV
860 870 880 890 900
TSEPIVGSIT TGIDPPKNIT ISNVTKDSLT VSWSPPVAPF DYYEYPIDHP
910 920 930 940 950
SGRLDSSVVP NTVTEFTITR LYPASQYEIS LNSVRGREES ERICTLVHTA
960 970 980 990 1000
MDSPMDLIAT NITPTEALLQ WKAPMGEVEN YVIVLTHFAM AGETILVDGV
1010 1020 1030 1040 1050
SEEFQLVDLL PRTHYTVTMY ATSGPLVSGT IATNFSTLLD PPANLTASEV
1060 1070 1080 1090 1100
TRQSALISWQ PPRAAIENYV LTYKSTDGSR KELIVDAEDT WIRLEGLSEN
1110 1120 1130 1140 1150
TDYTVLLQAA QEATRSSLTS TIFTTGGRVF SHPQDCAQHL MNGDTLSGVY
1160 1170 1180 1190 1200
TIFLNGELSH KLQVYCDMTT DGGGWIVFQR RQNGQTDFFR KWADYRVGFG
1210 1220 1230 1240 1250
NLEDEFWLGL DNYHRITAQG RYELRVDMRD GQEAVFAYYD KFAVEDSRSL
1260 1270 1280 1290 1300
YKLRIGGYNG TAGDSLSYHQ GRPFSTEDRD NDVAVTNCAM SYKGAWWYKN
1310 1320 1330 1340 1350
CHRTNLNGKY GESRHSQGIN WYHWKGHEFS IPFVEMKMRP YIHRLTAGRK

RRALKF
Length:1,356
Mass (Da):149,371
Last modified:November 1, 1996 - v1
Checksum:i9BFE2BF7AD4CA781
GO
Isoform 2 (identifier: Q05546-2) [UniParc]FASTAAdd to basket
Also known as: TN-R 160, 160 kDa form

The sequence of this isoform differs from the canonical sequence as follows:
     772-861: Missing.

Show »
Length:1,266
Mass (Da):139,478
Checksum:i032688DDF3ED0158
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012995772 – 861Missing in isoform 2. 1 PublicationAdd BLAST90

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18630 mRNA. Translation: CAA79229.1.
PIRiA45445.
RefSeqiNP_037177.1. NM_013045.1. [Q05546-1]
UniGeneiRn.11028.
Rn.131578.

Genome annotation databases

GeneIDi25567.
KEGGirno:25567.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18630 mRNA. Translation: CAA79229.1.
PIRiA45445.
RefSeqiNP_037177.1. NM_013045.1. [Q05546-1]
UniGeneiRn.11028.
Rn.131578.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TDQX-ray2.60A502-771[»]
ProteinModelPortaliQ05546.
SMRiQ05546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247598. 1 interactor.
IntActiQ05546. 1 interactor.

PTM databases

iPTMnetiQ05546.
PhosphoSitePlusiQ05546.
UniCarbKBiQ05546.

Proteomic databases

PRIDEiQ05546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25567.
KEGGirno:25567.

Organism-specific databases

CTDi7143.
RGDi3886. Tnr.

Phylogenomic databases

HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ05546.
KOiK06252.
PhylomeDBiQ05546.

Miscellaneous databases

EvolutionaryTraceiQ05546.
PROiQ05546.

Family and domain databases

CDDicd00063. FN3. 9 hits.
cd00087. FReD. 1 hit.
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...

Entry informationi

Entry nameiTENR_RAT
AccessioniPrimary (citable) accession number: Q05546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 132 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.