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Entry version 152 (12 Aug 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Tenascin-R

Gene

Tnr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion
LigandSialic acid

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-3000178, ECM proteoglycans

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tenascin-R
Short name:
TN-R
Alternative name(s):
Janusin
Neural recognition molecule J1-160/180
Restrictin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Tnr
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3886, Tnr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 31Sequence analysisAdd BLAST31
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000774932 – 1356Tenascin-RAdd BLAST1325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi55N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi180N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi198N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi278N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi297 ↔ 307PROSITE-ProRule annotation
Disulfide bondi314 ↔ 323PROSITE-ProRule annotation
Glycosylationi391N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi469N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi580N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei723PhosphoserineCombined sources1
Glycosylationi790N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi868N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi873N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1034N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1044N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1259N-linked (GlcNAc...) asparagineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PRoteomics IDEntifications database

More...
PRIDEi
Q05546

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q05546, 13 sites, 3 N-linked glycans (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q05546

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q05546

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
Q05546

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Brain-specific (PubMed:7679676). Expressed in oligodendrocytes and small subsets of neurons (mainly interneurons and motoneurons) of the cerebellum, hippocampus and olfactory bulb (PubMed:7679676). Expressed in dorsal root ganglia (PubMed:28270793).2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Transiently increased in dorsal root ganglia 1 day post-dorsal rhizotomy, returning to comparable levels 3 days post-injury (PubMed:28270793). Increased in dorsal root ganglia in response to both sciatic nerve crush and transection injury (PubMed:28270793).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
247598, 2 interactors

Protein interaction database and analysis system

More...
IntActi
Q05546, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000068101

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q05546

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q05546

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili127 – 157Sequence analysisAdd BLAST31

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi155 – 314Cys-richAdd BLAST160

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the tenascin family.Curated

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1225, Eukaryota
KOG2579, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q05546

KEGG Orthology (KO)

More...
KOi
K06252

Database of Orthologous Groups

More...
OrthoDBi
18592at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q05546

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063, FN3, 9 hits
cd00087, FReD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 9 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR041161, EGF_Tenascin
IPR036056, Fibrinogen-like_C
IPR002181, Fibrinogen_a/b/g_C_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR013783, Ig-like_fold
IPR033079, TNR

The PANTHER Classification System

More...
PANTHERi
PTHR19143:SF254, PTHR19143:SF254, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18720, EGF_Tenascin, 4 hits
PF00147, Fibrinogen_C, 1 hit
PF00041, fn3, 9 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181, EGF, 4 hits
SM00186, FBG, 1 hit
SM00060, FN3, 9 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265, SSF49265, 5 hits
SSF56496, SSF56496, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00022, EGF_1, 5 hits
PS01186, EGF_2, 4 hits
PS51406, FIBRINOGEN_C_2, 1 hit
PS50853, FN3, 9 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A096MJE6A0A096MJE6_RAT
Tenascin R, isoform CRA_b
Tnr rCG_46283
1,358Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1LQ63F1LQ63_RAT
Tenascin-R
Tnr
1,357Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012995772 – 861Missing in isoform 2. 1 PublicationAdd BLAST90

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z18630 mRNA Translation: CAA79229.1

Protein sequence database of the Protein Information Resource

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PIRi
A45445

NCBI Reference Sequences

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RefSeqi
NP_037177.1, NM_013045.1 [Q05546-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
25567

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25567

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TDQX-ray2.60A502-771[»]
SMRiQ05546
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi247598, 2 interactors
IntActiQ05546, 1 interactor
STRINGi10116.ENSRNOP00000068101

PTM databases

GlyGeniQ05546, 13 sites, 3 N-linked glycans (1 site)
iPTMnetiQ05546
PhosphoSitePlusiQ05546
UniCarbKBiQ05546

Proteomic databases

PRIDEiQ05546

Genome annotation databases

GeneIDi25567
KEGGirno:25567

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7143
RGDi3886, Tnr

Phylogenomic databases

eggNOGiKOG1225, Eukaryota
KOG2579, Eukaryota
InParanoidiQ05546
KOiK06252
OrthoDBi18592at2759
PhylomeDBiQ05546

Enzyme and pathway databases

ReactomeiR-RNO-3000178, ECM proteoglycans

Miscellaneous databases

EvolutionaryTraceiQ05546

Protein Ontology

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PROi
PR:Q05546

Family and domain databases

CDDicd00063, FN3, 9 hits
cd00087, FReD, 1 hit
Gene3Di2.60.40.10, 9 hits
InterProiView protein in InterPro
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR041161, EGF_Tenascin
IPR036056, Fibrinogen-like_C
IPR002181, Fibrinogen_a/b/g_C_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR013783, Ig-like_fold
IPR033079, TNR
PANTHERiPTHR19143:SF254, PTHR19143:SF254, 1 hit
PfamiView protein in Pfam
PF18720, EGF_Tenascin, 4 hits
PF00147, Fibrinogen_C, 1 hit
PF00041, fn3, 9 hits
SMARTiView protein in SMART
SM00181, EGF, 4 hits
SM00186, FBG, 1 hit
SM00060, FN3, 9 hits
SUPFAMiSSF49265, SSF49265, 5 hits
SSF56496, SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS00022, EGF_1, 5 hits
PS01186, EGF_2, 4 hits
PS51406, FIBRINOGEN_C_2, 1 hit
PS50853, FN3, 9 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTENR_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q05546
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1996
Last modified: August 12, 2020
This is version 152 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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