Reviewed, UniProtKB/Swiss-Prot Q05546 (TENR_RAT)

Names and origin

Protein names

Recommended name:
    Tenascin-R
      Short name=TN-R
Alternative name(s):
    Restrictin
    Janusin
    Neural recognition molecule J1-160/180

Gene names

Name:

Tnr

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1356 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 (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. Ref.4 Ref.6 Ref.8
Subunit structure	Forms oligomers. Interacts with TNC and FN1 By similarity. Interacts with BCAN and AGC1 in a calcium -dependent manner. Interacts with CNTN1, SCN2B, PTPRZ1, and CSPG3. Ref.4 Ref.2 Ref.3 Ref.5 Ref.9
Subcellular location	Secreted › extracellular space › extracellular matrix.
Tissue specificity	Brain-specific. Expressed in oligodendrocytes and small subsets of neurons (mainly interneurons and motoneurons) of the cerebellum, hippocampus and olfactory bulb. Ref.1
Developmental stage	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. Ref.8 Ref.1
Domain	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.
Post-translational modification	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.
Sequence similarities	Belongs to the tenascin family. Contains 5 EGF-like domains. Contains 1 fibrinogen C-terminal domain. Contains 9 fibronectin type-III domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing
Domain	Coiled coil EGF-like domain Repeat Signal
Ligand	Sialic acid
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell adhesion Inferred from direct assay. Source: RGD nervous system development Traceable author statement. Source: RGD signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	proteinaceous extracellular matrix Inferred from direct assay. Source: RGD
Molecular function	receptor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Acan	P07897	1	EBI-1039732,EBI-1039762

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q05546-1)

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.

Isoform 2 (identifier: Q05546-2)

Also known as: TN-R 160; 160 kDa form;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Potential

Chain

32 – 1356

1325

Tenascin-R

PRO_0000007749

Regions

Domain

188 – 199

12

EGF-like 1

Domain

204 – 230

27

EGF-like 2

Domain

235 – 261

27

EGF-like 3

Domain

281 – 292

12

EGF-like 4

Domain

293 – 324

32

EGF-like 5

Domain

325 – 412

88

Fibronectin type-III 1

Domain

413 – 501

89

Fibronectin type-III 2

Domain

502 – 591

90

Fibronectin type-III 3

Domain

592 – 683

92

Fibronectin type-III 4

Domain

684 – 771

88

Fibronectin type-III 5

Domain

772 – 861

90

Fibronectin type-III 6

Domain

862 – 949

88

Fibronectin type-III 7

Domain

950 – 1037

88

Fibronectin type-III 8

Domain

1038 – 1125

88

Fibronectin type-III 9

Domain

1127 – 1342

216

Fibrinogen C-terminal

Coiled coil

127 – 157

31

Potential

Compositional bias

155 – 314

160

Cys-rich

Amino acid modifications

Modified residue

723

1

Phosphoserine By similarity

Glycosylation

55

1

N-linked (GlcNAc...) Potential

Glycosylation

180

1

N-linked (GlcNAc...) Potential

Glycosylation

198

1

N-linked (GlcNAc...) Potential

Glycosylation

278

1

N-linked (GlcNAc...) Potential

Glycosylation

391

1

N-linked (GlcNAc...) Potential

Glycosylation

469

1

N-linked (GlcNAc...) Potential

Glycosylation

580

1

N-linked (GlcNAc...) Potential

Glycosylation

790

1

N-linked (GlcNAc...) Potential

Glycosylation

868

1

N-linked (GlcNAc...) Potential

Glycosylation

873

1

N-linked (GlcNAc...) Potential

Glycosylation

1034

1

N-linked (GlcNAc...) Potential

Glycosylation

1044

1

N-linked (GlcNAc...) Potential

Glycosylation

1259

1

N-linked (GlcNAc...) Potential

Disulfide bond

297 ↔ 307

By similarity

Disulfide bond

314 ↔ 323

By similarity

Natural variations

Alternative sequence

772 – 861

90

Missing in isoform 2.

VSP_012995

Secondary structure

1

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1356

Helix Strand Turn

Details...

Beta strand

507 – 514

8

Beta strand

519 – 524

6

Beta strand

531 – 543

13

Beta strand

547 – 551

5

Beta strand

556 – 560

5

Beta strand

568 – 577

10

Beta strand

585 – 590

6

Beta strand

597 – 604

8

Beta strand

609 – 614

6

Beta strand

621 – 629

9

Beta strand

636 – 641

6

Beta strand

644 – 652

9

Beta strand

660 – 669

10

Beta strand

677 – 682

6

Beta strand

689 – 696

8

Beta strand

701 – 706

6

Beta strand

713 – 720

8

Beta strand

722 – 724

3

Beta strand

727 – 734

8

Beta strand

736 – 740

5

Beta strand

749 – 757

9

Beta strand

765 – 769

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TN-R 180) (180 kDa form) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9BFE2BF7AD4CA781	FASTA	1,356	149,371
	10 20 30 40 50 60 MGIEGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERV QRQTVEEEGG ASSYNTSSKE 70 80 90 100 110 120 QPMVFNHVYN INVPLESLCS SGLEASAEQD VSAEDDTLAE YTGQTSDHES QVTFTHKINL 130 140 150 160 170 180 PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNTNCC QESAATGQLD YVPHCSGHGN 190 200 210 220 230 240 FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS 250 260 270 280 290 300 SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGQCANGT CLCQEGYAGE DCSQRRCLNA 310 320 330 340 350 360 CSGRGHCQEG LCICEEGYQG PDCSAVTPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ 370 380 390 400 410 420 PSLGGLQLQQ RVPGDWSGVT ITELEPGLTY NISVYAVISN ILSLPITAKV ATHLSTPQGL 430 440 450 460 470 480 QFKTITETTV EVQWEPFSFS FDGWEISFTP KNNEGGVIAQ LPSDVTSFNQ TGLKPGEEYI 490 500 510 520 530 540 VNVVALKEQA RGPPTSASVS TVIDGPTQIL VRDVSDTVAF VEWTPPRAKV DFILLKYGLV 550 560 570 580 590 600 GGEGGKTTFR LQPPLSQYSV QALRPGSRYE VSISAVRGTN ESDASSTQFT TEIDAPKNLR 610 620 630 640 650 660 VGSRTATSLD LEWDNSEAEA QEYKVVYSTL AGEQYHEVLV PKGIGPTTKT TLTDLVPGTE 670 680 690 700 710 720 YGVGISAVMN SKQSIPATMN ARTELDSPRD LMVTASSETS ISLIWTKASG PIDHYRITFT 730 740 750 760 770 780 PSSGISSEVT VPRDRTSYTL TDLEPGAEYI ISITAERGRQ QSLESTVDAF TGFRPISHLH 790 800 810 820 830 840 FSHVTSSSVN ITWSDPSPPA DRLILNYSPR DEEEEMMEVL LDATKRHAVL MGLQPATEYI 850 860 870 880 890 900 VNLVAVHGTV TSEPIVGSIT TGIDPPKNIT ISNVTKDSLT VSWSPPVAPF DYYEYPIDHP 910 920 930 940 950 960 SGRLDSSVVP NTVTEFTITR LYPASQYEIS LNSVRGREES ERICTLVHTA MDSPMDLIAT 970 980 990 1000 1010 1020 NITPTEALLQ WKAPMGEVEN YVIVLTHFAM AGETILVDGV SEEFQLVDLL PRTHYTVTMY 1030 1040 1050 1060 1070 1080 ATSGPLVSGT IATNFSTLLD PPANLTASEV TRQSALISWQ PPRAAIENYV LTYKSTDGSR 1090 1100 1110 1120 1130 1140 KELIVDAEDT WIRLEGLSEN TDYTVLLQAA QEATRSSLTS TIFTTGGRVF SHPQDCAQHL 1150 1160 1170 1180 1190 1200 MNGDTLSGVY TIFLNGELSH KLQVYCDMTT DGGGWIVFQR RQNGQTDFFR KWADYRVGFG 1210 1220 1230 1240 1250 1260 NLEDEFWLGL DNYHRITAQG RYELRVDMRD GQEAVFAYYD KFAVEDSRSL YKLRIGGYNG 1270 1280 1290 1300 1310 1320 TAGDSLSYHQ GRPFSTEDRD NDVAVTNCAM SYKGAWWYKN CHRTNLNGKY GESRHSQGIN 1330 1340 1350 WYHWKGHEFS IPFVEMKMRP YIHRLTAGRK RRALKF
	Isoform 2 (TN-R 160) (160 kDa form). Checksum: 032688DDF3ED0158	FASTA	1,266	139,478
	10 20 30 40 50 60 MGIEGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERV QRQTVEEEGG ASSYNTSSKE 70 80 90 100 110 120 QPMVFNHVYN INVPLESLCS SGLEASAEQD VSAEDDTLAE YTGQTSDHES QVTFTHKINL 130 140 150 160 170 180 PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNTNCC QESAATGQLD YVPHCSGHGN 190 200 210 220 230 240 FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS 250 260 270 280 290 300 SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGQCANGT CLCQEGYAGE DCSQRRCLNA 310 320 330 340 350 360 CSGRGHCQEG LCICEEGYQG PDCSAVTPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ 370 380 390 400 410 420 PSLGGLQLQQ RVPGDWSGVT ITELEPGLTY NISVYAVISN ILSLPITAKV ATHLSTPQGL 430 440 450 460 470 480 QFKTITETTV EVQWEPFSFS FDGWEISFTP KNNEGGVIAQ LPSDVTSFNQ TGLKPGEEYI 490 500 510 520 530 540 VNVVALKEQA RGPPTSASVS TVIDGPTQIL VRDVSDTVAF VEWTPPRAKV DFILLKYGLV 550 560 570 580 590 600 GGEGGKTTFR LQPPLSQYSV QALRPGSRYE VSISAVRGTN ESDASSTQFT TEIDAPKNLR 610 620 630 640 650 660 VGSRTATSLD LEWDNSEAEA QEYKVVYSTL AGEQYHEVLV PKGIGPTTKT TLTDLVPGTE 670 680 690 700 710 720 YGVGISAVMN SKQSIPATMN ARTELDSPRD LMVTASSETS ISLIWTKASG PIDHYRITFT 730 740 750 760 770 780 PSSGISSEVT VPRDRTSYTL TDLEPGAEYI ISITAERGRQ QSLESTVDAF TGIDPPKNIT 790 800 810 820 830 840 ISNVTKDSLT VSWSPPVAPF DYYEYPIDHP SGRLDSSVVP NTVTEFTITR LYPASQYEIS 850 860 870 880 890 900 LNSVRGREES ERICTLVHTA MDSPMDLIAT NITPTEALLQ WKAPMGEVEN YVIVLTHFAM 910 920 930 940 950 960 AGETILVDGV SEEFQLVDLL PRTHYTVTMY ATSGPLVSGT IATNFSTLLD PPANLTASEV 970 980 990 1000 1010 1020 TRQSALISWQ PPRAAIENYV LTYKSTDGSR KELIVDAEDT WIRLEGLSEN TDYTVLLQAA 1030 1040 1050 1060 1070 1080 QEATRSSLTS TIFTTGGRVF SHPQDCAQHL MNGDTLSGVY TIFLNGELSH KLQVYCDMTT 1090 1100 1110 1120 1130 1140 DGGGWIVFQR RQNGQTDFFR KWADYRVGFG NLEDEFWLGL DNYHRITAQG RYELRVDMRD 1150 1160 1170 1180 1190 1200 GQEAVFAYYD KFAVEDSRSL YKLRIGGYNG TAGDSLSYHQ GRPFSTEDRD NDVAVTNCAM 1210 1220 1230 1240 1250 1260 SYKGAWWYKN CHRTNLNGKY GESRHSQGIN WYHWKGHEFS IPFVEMKMRP YIHRLTAGRK RRALKF

References

[1]	"Molecular characterization and in situ mRNA localization of the neural recognition molecule J1-160/180: a modular structure similar to tenascin." Fuss B., Wintergerst E.-S., Bartsch U., Schachner M. J. Cell Biol. 120:1237-1249(1993) [PubMed: 7679676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[2]	"Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11." Xiao Z.-C., Taylor J., Montag D., Rougon G., Schachner M. Eur. J. Neurosci. 8:766-782(1996) [PubMed: 9081628] [Abstract] Cited for: INTERACTION WITH CNTN1.
[3]	"The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety." Aspberg A., Miura R., Bourdoulous S., Shimonaka M., Heinegard D., Schachner M., Ruoslahti E., Yamaguchi Y. Proc. Natl. Acad. Sci. U.S.A. 94:10116-10121(1997) [PubMed: 9294172] [Abstract] Cited for: INTERACTION WITH BCAN.
[4]	"Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R." Srinivasan J., Schachner M., Catterall W.A. Proc. Natl. Acad. Sci. U.S.A. 95:15753-15757(1998) [PubMed: 9861042] [Abstract] Cited for: INTERACTION WITH SCN2B, FUNCTION.
[5]	"High affinity binding and overlapping localization of neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule." Milev P., Chiba A., Haring M., Rauvala H., Schachner M., Ranscht B., Margolis R.K., Margolis R.U. J. Biol. Chem. 273:6998-7005(1998) [PubMed: 9507007] [Abstract] Cited for: INTERACTION WITH PTPRZ1 AND CSPG3.
[6]	"Chondroitin sulfates expressed on oligodendrocyte-derived tenascin-R are involved in neural cell recognition. Functional implications during CNS development and regeneration." Probstmeier R., Stichel C.C., Muller H.W., Asou H., Pesheva P. J. Neurosci. Res. 60:21-36(2000) [PubMed: 10723065] [Abstract] Cited for: GLYCOSYLATION, FUNCTION.
[7]	"Spatial and temporal regulation of tenascin-R glycosylation in the cerebellum." Woodworth A., Fiete D., Baenziger J.U. J. Biol. Chem. 277:50941-50947(2002) [PubMed: 12393878] [Abstract] Cited for: GLYCOSYLATION.
[8]	"Neuronal-specific synthesis and glycosylation of tenascin-R." Woodworth A., Pesheva P., Fiete D., Baenziger J.U. J. Biol. Chem. 279:10413-10421(2004) [PubMed: 14681222] [Abstract] Cited for: GLYCOSYLATION, DEVELOPMENTAL STAGE, FUNCTION.
[9]	"Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins." Lundell A., Olin A.I., Morgelin M., al-Karadaghi S., Aspberg A., Logan D.T. Structure 12:1495-1506(2004) [PubMed: 15296743] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 489-771, INTERACTION WITH AGC1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z18630 mRNA. Translation: CAA79229.1.

IPI

IPI00190669.
IPI00554031.

PIR

A45445.

RefSeq

NP_037177.1.

UniGene

Rn.11028
Rn.131578

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TDQ	X-ray	2.60	A	502-771	[»]

SMR

Q05546. Positions 687-942, 863-1111, 1132-1340.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q05546. 1 interaction.

STRING

Q05546.

PTM databases

PhosphoSite

Q05546.

Genome annotation databases

Ensembl

ENSRNOT00000003407; ENSRNOP00000003407; ENSRNOG00000002468; Rattus norvegicus. [Genome view]

GeneID

25567.

KEGG

rno:25567.

UCSC

NM_013045. rat.

Organism-specific databases

CTD

25567.

RGD

3886. Tnr.

Phylogenomic databases

eggNOG

maNOG04403.

HOVERGEN

Q05546.

InParanoid

Q05546.

Gene expression databases

Genevestigator

Q05546.

GermOnline

ENSRNOG00000002468. Rattus norvegicus.

Family and domain databases

InterPro

IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR002181. Fibrinogen_a/b/g_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
[Graphical view]

Gene3D

G3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit.
G3DSA:2.60.40.30. FN_III-like. 9 hits.

Pfam

PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 9 hits.
[Graphical view]

SMART

SM00181. EGF. 1 hit.
SM00186. FBG. 1 hit.
SM00060. FN3. 9 hits.
[Graphical view]

PROSITE

PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. False negative.
PS00514. FIBRINOGEN_C_1. False negative.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 9 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

607175.

Entry information

Entry name

TENR_RAT

Accession

Primary (citable) accession number: Q05546

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)