Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92752 (TENR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tenascin-R

Short name=TN-R
Alternative name(s):
Janusin
Restrictin
Gene names
Name:TNR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These 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 mediate 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.

Subunit structure

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

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Brain specific. 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 By similarity.

Post-translational modification

Contains N-linked oligosaccharides, O-linked sialylated structures and O-linked chondroitin sulfate glycosaminoglycans. Contains N-linked oligosaccharides with a sulfated carbohydrate structure By similarity. O-glycosylated on Thr-36 or Thr-37 with a core 1 or possibly core 8 glycan.

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 processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
EGF-like domain
Repeat
Signal
   LigandSialic acid
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processassociative learning

Inferred from electronic annotation. Source: Ensembl

axon guidance

Non-traceable author statement PubMed 8940128. Source: ProtInc

cell adhesion

Non-traceable author statement PubMed 8940128. Source: ProtInc

extracellular matrix organization

Traceable author statement. Source: Reactome

locomotory exploration behavior

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of axon extension involved in regeneration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic transmission

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

neuron cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of transmission of nerve impulse

Inferred from electronic annotation. Source: Ensembl

synapse organization

Inferred from electronic annotation. Source: Ensembl

telencephalon cell migration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

extracellular region

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

perineuronal net

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92752-1)

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: Q92752-2)

The sequence of this isoform differs from the canonical sequence as follows:
     773-862: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 13581327Tenascin-R
PRO_0000007747

Regions

Domain188 – 19912EGF-like 1
Domain219 – 23012EGF-like 2
Domain250 – 26112EGF-like 3
Domain281 – 29212EGF-like 4
Domain312 – 32312EGF-like 5
Domain328 – 42093Fibronectin type-III 1
Domain421 – 50585Fibronectin type-III 2
Domain506 – 59590Fibronectin type-III 3
Domain596 – 68792Fibronectin type-III 4
Domain688 – 77790Fibronectin type-III 5
Domain778 – 86588Fibronectin type-III 6
Domain866 – 95590Fibronectin type-III 7
Domain956 – 104287Fibronectin type-III 8
Domain1043 – 113088Fibronectin type-III 9
Domain1129 – 1344216Fibrinogen C-terminal
Coiled coil127 – 15731 Potential
Compositional bias155 – 314160Cys-rich

Amino acid modifications

Glycosylation361O-linked (GalNAc...) Probable
Glycosylation371O-linked (GalNAc...) Probable
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Potential
Glycosylation5811N-linked (GlcNAc...) Potential
Glycosylation7911N-linked (GlcNAc...) Potential
Glycosylation8741N-linked (GlcNAc...) Potential
Glycosylation10361N-linked (GlcNAc...) Potential
Glycosylation10461N-linked (GlcNAc...) Potential
Glycosylation12611N-linked (GlcNAc...) Potential
Disulfide bond292 ↔ 301 By similarity
Disulfide bond297 ↔ 312 By similarity
Disulfide bond314 ↔ 323 By similarity

Natural variations

Alternative sequence773 – 86290Missing in isoform 2.
VSP_012993
Natural variant171I → V. Ref.1 Ref.2
Corresponds to variant rs859398 [ dbSNP | Ensembl ].
VAR_021479
Natural variant1281A → S.
Corresponds to variant rs2239819 [ dbSNP | Ensembl ].
VAR_021906
Natural variant2931G → S.
Corresponds to variant rs3752516 [ dbSNP | Ensembl ].
VAR_021907
Natural variant3021S → N.
Corresponds to variant rs35736986 [ dbSNP | Ensembl ].
VAR_055780
Natural variant6431R → K.
Corresponds to variant rs859427 [ dbSNP | Ensembl ].
VAR_030737

Experimental info

Sequence conflict6291S → I in CAA66709. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: E4DE356B44D117E7

FASTA1,358149,562
        10         20         30         40         50         60 
MGADGETVVL KNMLIGINLI LLGSMIKPSE CQLEVTTERV QRQSVEEEGG IANYNTSSKE 

        70         80         90        100        110        120 
QPVVFNHVYN INVPLDNLCS SGLEASAEQE VSAEDETLAE YMGQTSDHES QVTFTHRINF 

       130        140        150        160        170        180 
PKKACPCASS AQVLQELLSR IEMLEREVSV LRDQCNANCC QESAATGQLD YIPHCSGHGN 

       190        200        210        220        230        240 
FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS 

       250        260        270        280        290        300 
SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGRCANGT CLCEEGYVGE DCGQRQCLNA 

       310        320        330        340        350        360 
CSGRGQCEEG LCVCEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ 

       370        380        390        400        410        420 
PTALGGLQLQ QRVPGDWSGV TITELEPGLT YNISVYAVIS NILSLPITAK VATHLSTPQG 

       430        440        450        460        470        480 
LQFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QVPSDVTSFN QTGLKPGEEY 

       490        500        510        520        530        540 
IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWIPPRAK VDFILLKYGL 

       550        560        570        580        590        600 
VGGEGGRTTF RLQPPLSQYS VQALRPGSRY EVSVSAVRGT NESDSATTQF TTEIDAPKNL 

       610        620        630        640        650        660 
RVGSRTATSL DLEWDNSEAE VQEYKVVYST LAGEQYHEVL VPRGIGPTTR ATLTDLVPGT 

       670        680        690        700        710        720 
EYGVGISAVM NSQQSVPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF 

       730        740        750        760        770        780 
TPSSGIASEV TVPKDRTSYT LTDLEPGAEY IISVTAERGR QQSLESTVDA FTGFRPISHL 

       790        800        810        820        830        840 
HFSHVTSSSV NITWSDPSPP ADRLILNYSP RDEEEEMMEV SLDATKRHAV LMGLQPATEY 

       850        860        870        880        890        900 
IVNLVAVHGT VTSEPIVGSI TTGIDPPKDI TISNVTKDSV MVSWSPPVAS FDYYRVSYRP 

       910        920        930        940        950        960 
TQVGRLDSSV VPNTVTEFTI TRLNPATEYE ISLNSVRGRE ESERICTLVH TAMDNPVDLI 

       970        980        990       1000       1010       1020 
ATNITPTEAL LQWKAPVGEV ENYVIVLTHF AVAGETILVD GVSEEFRLVD LLPSTHYTAT 

      1030       1040       1050       1060       1070       1080 
MYATNGPLTS GTISTNFSTL LDPPANLTAS EVTRQSALIS WQPPRAEIEN YVLTYKSTDG 

      1090       1100       1110       1120       1130       1140 
SRKELIVDAE DTWIRLEGLL ENTDYTVLLQ AAQDTTWSSI TSTAFTTGGR VFPHPQDCAQ 

      1150       1160       1170       1180       1190       1200 
HLMNGDTLSG VYPIFLNGEL SQKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG 

      1210       1220       1230       1240       1250       1260 
FGNVEDEFWL GLDNIHRITS QGRYELRVDM RDGQEAAFAS YDRFSVEDSR NLYKLRIGSY 

      1270       1280       1290       1300       1310       1320 
NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY KNCHRTNLNG KYGESRHSQG 

      1330       1340       1350 
INWYHWKGHE FSIPFVEMKM RPYNHRLMAG RKRQSLQF 

« Hide

Isoform 2 [UniParc].

Checksum: E4EB4095284A4E29
Show »

FASTA1,268139,695

References

« Hide 'large scale' references
[1]"Human tenascin-R: complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24."
Carnemolla B., Leprini A., Borsi L., Querze G., Urbini S., Zardi L.
J. Biol. Chem. 271:8157-8160(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANT VAL-17.
Tissue: Brain.
[2]"Isolation of the gene for neural cell adhesion molecule tenascin-R and fine mapping relative to loci in 1q25-31."
Williams H., Schachner M., Wang B., Goodfellow P., Kenwrick S.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-17.
Tissue: Brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND THR-37, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z67996 mRNA. Translation: CAA91947.1.
X98085 mRNA. Translation: CAA66709.1.
AL021919 Genomic DNA. No translation available.
AL023285 Genomic DNA. No translation available.
AL136530 Genomic DNA. No translation available.
Z94057, Z94055 Genomic DNA. Translation: CAI21650.1.
Z94055, Z94057 Genomic DNA. Translation: CAI19943.1.
CCDSCCDS1318.1. [Q92752-1]
RefSeqNP_003276.3. NM_003285.2. [Q92752-1]
UniGeneHs.659864.

3D structure databases

ProteinModelPortalQ92752.
SMRQ92752. Positions 503-771.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112997. 3 interactions.
IntActQ92752. 1 interaction.
STRING9606.ENSP00000263525.

PTM databases

PhosphoSiteQ92752.

Polymorphism databases

DMDM311033534.

Proteomic databases

PaxDbQ92752.
PRIDEQ92752.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263525; ENSP00000263525; ENSG00000116147. [Q92752-1]
ENST00000367674; ENSP00000356646; ENSG00000116147. [Q92752-1]
GeneID7143.
KEGGhsa:7143.
UCSCuc001gkp.1. human. [Q92752-1]

Organism-specific databases

CTD7143.
GeneCardsGC01M175291.
H-InvDBHIX0028854.
HGNCHGNC:11953. TNR.
HPACAB022343.
HPA027134.
HPA027150.
HPA029859.
MIM601995. gene.
neXtProtNX_Q92752.
PharmGKBPA36642.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311251.
HOGENOMHOG000234355.
HOVERGENHBG008949.
InParanoidQ92752.
KOK06252.
OMAKACPCAS.
OrthoDBEOG7X9G60.
PhylomeDBQ92752.
TreeFamTF329915.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ92752.
BgeeQ92752.
CleanExHS_TNR.
GenevestigatorQ92752.

Family and domain databases

Gene3D2.60.40.10. 9 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR013032. EGF-like_CS.
IPR013111. EGF_extracell.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF07974. EGF_2. 2 hits.
PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 9 hits.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
SM00060. FN3. 9 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 4 hits.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTenascin-R.
GenomeRNAi7143.
NextBio27961.
PROQ92752.
SOURCESearch...

Entry information

Entry nameTENR_HUMAN
AccessionPrimary (citable) accession number: Q92752
Secondary accession number(s): C9J563, Q15568, Q5R3G0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM