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Protein

Tenascin-R

Gene

Tnr

Organism
Mus musculus (Mouse)
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 similarity4 Publications

GO - Molecular functioni

  • sphingolipid binding Source: MGI

GO - Biological processi

  • associative learning Source: MGI
  • extracellular matrix organization Source: MGI
  • locomotory exploration behavior Source: MGI
  • long-term synaptic potentiation Source: MGI
  • modulation of synaptic transmission Source: MGI
  • negative regulation of axon extension Source: MGI
  • negative regulation of axon extension involved in regeneration Source: MGI
  • negative regulation of cell-cell adhesion Source: MGI
  • negative regulation of neuron projection development Source: MGI
  • negative regulation of synaptic transmission Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • neuron cell-cell adhesion Source: MGI
  • positive regulation of synaptic transmission, glutamatergic Source: MGI
  • positive regulation of transmission of nerve impulse Source: MGI
  • synapse organization Source: MGI
  • telencephalon cell migration Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiR-MMU-3000178. ECM proteoglycans.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:99516. Tnr.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • membrane raft Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • perineuronal net Source: MGI
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence analysisAdd
BLAST
Chaini32 – 13581327Tenascin-RPRO_0000007748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence analysis
Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence analysis
Disulfide bondi297 ↔ 307PROSITE-ProRule annotation
Disulfide bondi314 ↔ 323PROSITE-ProRule annotation
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence analysis
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence analysis
Glycosylationi581 – 5811N-linked (GlcNAc...)Sequence analysis
Modified residuei724 – 7241PhosphoserineBy similarity
Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence analysis
Glycosylationi869 – 8691N-linked (GlcNAc...)Sequence analysis
Glycosylationi874 – 8741N-linked (GlcNAc...)Sequence analysis
Glycosylationi1036 – 10361N-linked (GlcNAc...)Sequence analysis
Glycosylationi1046 – 10461N-linked (GlcNAc...)Sequence analysis
Glycosylationi1261 – 12611N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Contains N-linked oligosaccharides with a sulfated carbohydrate structures (By similarity). Contains N-linked oligosaccharides, O-linked sialylated structures and O-linked chondroitin sulfate glycosaminoglycans.By similarity2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

MaxQBiQ8BYI9.
PaxDbiQ8BYI9.
PRIDEiQ8BYI9.

PTM databases

iPTMnetiQ8BYI9.
PhosphoSiteiQ8BYI9.
SwissPalmiQ8BYI9.
UniCarbKBiQ8BYI9.

Expressioni

Tissue specificityi

Brain-specific.1 Publication

Developmental stagei

Isoform 1 is barely detectable at E17 embryo and increases in intensity until postnatal day 15, when it reaches adult levels. Isoform 2 is detectable from postnatal day 5 and reaches adult levels also at postnatal day 15.1 Publication

Gene expression databases

BgeeiQ8BYI9.
CleanExiMM_TNR.
ExpressionAtlasiQ8BYI9. baseline and differential.
GenevisibleiQ8BYI9. MM.

Interactioni

Subunit structurei

Interacts with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B, PTPRZ1, and CSPG3 (By similarity). Forms oligomers. Isoforms 1 and 2 form respectively trimeric (tribrachion) and dimeric kink-armed rodlike structures, which are linked by disulfide bridges. Interacts with CNTN1, TNC and FN1.By similarity2 Publications

Protein-protein interaction databases

IntActiQ8BYI9. 4 interactions.
MINTiMINT-4113482.
STRINGi10090.ENSMUSP00000107298.

Structurei

3D structure databases

ProteinModelPortaliQ8BYI9.
SMRiQ8BYI9. Positions 503-771.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini188 – 19912EGF-like 1Add
BLAST
Domaini219 – 23012EGF-like 2Add
BLAST
Domaini250 – 26112EGF-like 3Add
BLAST
Domaini281 – 29212EGF-like 4Add
BLAST
Domaini312 – 32312EGF-like 5Add
BLAST
Domaini328 – 42093Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini421 – 50585Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini506 – 59792Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini598 – 68790Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini688 – 77790Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini778 – 86588Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini866 – 95590Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini956 – 104287Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1043 – 113189Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1129 – 1344216Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili127 – 15731Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 314160Cys-richAdd
BLAST

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 (By similarity).By similarity

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

eggNOGiKOG1225. Eukaryota.
KOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ8BYI9.
KOiK06252.
OMAiKACPCAS.
OrthoDBiEOG7X9G60.
TreeFamiTF329915.

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: Q8BYI9-1) [UniParc]FASTAAdd to basket

Also known as: J1-180, TN-R 180

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
MGIDGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERA QRQTVEEEGG
60 70 80 90 100
ASSYNTSSKE QPMVFNHVYN INVPLESLCS SGLEASAEQD MSAEDDTLAE
110 120 130 140 150
YIGQTSDHES QVTFTHKINL PKKACPCASS SQVLQELLSR IEMLEREVSL
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 PDCSAVAPPE DLRVAGISDR SIELEWDGPM
360 370 380 390 400
AVTEYVISYQ PTALGGLQLQ QRVPGDWSGV TIMELEPGLT YNISVYAVIS
410 420 430 440 450
NILSLPITAK VATHLSTPQG LQFKTITETT VEVQWEPFSF SFDGWEISFI
460 470 480 490 500
PKNNEGGVIA QLPSDVTSFN QTGLKPGEEY IVNVVALKEQ ARSPPTSASV
510 520 530 540 550
STVIDGPTQI LVRDVSDTVA FVEWTPPRAK VDFILLKYGL VGGEGGKTTF
560 570 580 590 600
RLQPPLSQYS VQALRPGSRY EVSISAVRGT NESEASSTQF TTEIDAPKNL
610 620 630 640 650
RVGSRTATSL DLEWDNSEAE AQEYKVVYST LAGEQYHEVL VPKGIGPTTK
660 670 680 690 700
TTLTDLVPGT EYGVGISAVM NSKQSIPATM NARTELDSPR DLMVTASSET
710 720 730 740 750
SISLIWTKAS GPIDHYRITF TPSSGISSEV TVPRDRTSYT LTDLEPGAEY
760 770 780 790 800
IISITAERGR QQSLESTVDA FTGFRPISHL HFSHVTSSSV NITWSDPSPP
810 820 830 840 850
ADRLILNYSP RDKEEDMLEV LLDATKRHAV LMGLQPATEY IVNLVAVHGT
860 870 880 890 900
VTSEPIVGSI TTGIDPPKNI TISNVTKDSL TVSWSSPVAP FDYYRVSYRP
910 920 930 940 950
TQVGRLDSSV VPNTVTEFAI TRLYPATEYE ISLNSVRGRE ESERICTLVH
960 970 980 990 1000
TAMDSPMDLI ATNITPTEAL LQWKAPMGEV ENYVIVLTHF AIAGETILVD
1010 1020 1030 1040 1050
GVSEEFQLVD LLPSTHYTVT MYATSGPLMS GTIATNFSTL LDPPDNLTAS
1060 1070 1080 1090 1100
EVTRQSALIS WQPPRAAIEN YVLTYKSTDG SRKELIVDAE DTWIRLEGLS
1110 1120 1130 1140 1150
ENTDYTVLLQ AAQEATRSSL TSTVFTTGGR VFSHPQDCAQ HLMNGDTLSG
1160 1170 1180 1190 1200
VYTIFLNGEL SHKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG
1210 1220 1230 1240 1250
FGNLEDEFWL GLDNIHRITA QGRYELRVDM RDGQEAVFAY YDKFAVEDSR
1260 1270 1280 1290 1300
SLYKIRIGSY NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY
1310 1320 1330 1340 1350
KNCHRTNLNG KYGESRHSQG INWYHWKGHE FSIPFVEMKM RPYIHRLTAG

RKRRALKF
Length:1,358
Mass (Da):149,589
Last modified:July 27, 2011 - v2
Checksum:i354D2E71AB356952
GO
Isoform 2 (identifier: Q8BYI9-2) [UniParc]FASTAAdd to basket

Also known as: J1-160, TN-R 160

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

Show »
Length:1,268
Mass (Da):139,729
Checksum:iD6131FA460948A41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541Y → H in BAC30335 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei773 – 86290Missing in isoform 2. CuratedVSP_012994Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039390 mRNA. Translation: BAC30335.1.
BC132392 mRNA. Translation: AAI32393.1.
BC138043 mRNA. Translation: AAI38044.1.
AJ005844 mRNA. Translation: CAA06739.1.
CCDSiCCDS15403.1. [Q8BYI9-1]
RefSeqiNP_071707.2. NM_022312.3. [Q8BYI9-1]
XP_006496805.1. XM_006496742.2. [Q8BYI9-1]
XP_006496806.1. XM_006496743.1. [Q8BYI9-1]
XP_006496807.1. XM_006496744.2. [Q8BYI9-1]
UniGeneiMm.44701.
Mm.483249.

Genome annotation databases

EnsembliENSMUST00000111669; ENSMUSP00000107298; ENSMUSG00000015829. [Q8BYI9-1]
ENSMUST00000192069; ENSMUSP00000141553; ENSMUSG00000015829. [Q8BYI9-1]
GeneIDi21960.
KEGGimmu:21960.
UCSCiuc007dea.2. mouse. [Q8BYI9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039390 mRNA. Translation: BAC30335.1.
BC132392 mRNA. Translation: AAI32393.1.
BC138043 mRNA. Translation: AAI38044.1.
AJ005844 mRNA. Translation: CAA06739.1.
CCDSiCCDS15403.1. [Q8BYI9-1]
RefSeqiNP_071707.2. NM_022312.3. [Q8BYI9-1]
XP_006496805.1. XM_006496742.2. [Q8BYI9-1]
XP_006496806.1. XM_006496743.1. [Q8BYI9-1]
XP_006496807.1. XM_006496744.2. [Q8BYI9-1]
UniGeneiMm.44701.
Mm.483249.

3D structure databases

ProteinModelPortaliQ8BYI9.
SMRiQ8BYI9. Positions 503-771.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BYI9. 4 interactions.
MINTiMINT-4113482.
STRINGi10090.ENSMUSP00000107298.

PTM databases

iPTMnetiQ8BYI9.
PhosphoSiteiQ8BYI9.
SwissPalmiQ8BYI9.
UniCarbKBiQ8BYI9.

Proteomic databases

MaxQBiQ8BYI9.
PaxDbiQ8BYI9.
PRIDEiQ8BYI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111669; ENSMUSP00000107298; ENSMUSG00000015829. [Q8BYI9-1]
ENSMUST00000192069; ENSMUSP00000141553; ENSMUSG00000015829. [Q8BYI9-1]
GeneIDi21960.
KEGGimmu:21960.
UCSCiuc007dea.2. mouse. [Q8BYI9-1]

Organism-specific databases

CTDi7143.
MGIiMGI:99516. Tnr.

Phylogenomic databases

eggNOGiKOG1225. Eukaryota.
KOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000234355.
HOVERGENiHBG008949.
InParanoidiQ8BYI9.
KOiK06252.
OMAiKACPCAS.
OrthoDBiEOG7X9G60.
TreeFamiTF329915.

Enzyme and pathway databases

ReactomeiR-MMU-3000178. ECM proteoglycans.

Miscellaneous databases

ChiTaRSiTnr. mouse.
NextBioi301652.
PROiQ8BYI9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BYI9.
CleanExiMM_TNR.
ExpressionAtlasiQ8BYI9. baseline and differential.
GenevisibleiQ8BYI9. MM.

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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spinal cord.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Mice deficient for tenascin-r display alterations of the extracellular matrix and decreased axonal conduction velocities in the CNS."
    Weber P., Bartsch U., Rasband M.N., Czaniera R., Lang Y., Bluethmann H., Margolis R.U., Levinson S.R., Shrager P., Montag D.
    J. Neurosci. 19:4245-4262(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-24.
    Tissue: Brain.
  4. "J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion."
    Pesheva P., Spiess E., Schachner M.
    J. Cell Biol. 109:1765-1778(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE.
  5. "The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180."
    Pesheva P., Gennarini G., Goridis C., Schachner M.
    Neuron 10:69-82(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNTN1, FUNCTION.
  6. "Tenascin-R is an intrinsic autocrine factor for oligodendrocyte differentiation and promotes cell adhesion by a sulfatide-mediated mechanism."
    Pesheva P., Gloor S., Schachner M., Probstmeier R.
    J. Neurosci. 17:4642-4651(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING TO MEMBRANE SURFACE SULFATIDES OF OLIGODENDROCYTES.
  7. "Tenascin-R interferes with integrin-dependent oligodendrocyte precursor cell adhesion by a ganglioside-mediated signalling mechanism."
    Probstmeier R., Michels M., Franz T., Chan B.M.C., Pesheva P.
    Eur. J. Neurosci. 11:2474-2488(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING TO MEMBRANE SURFACE GANGLIOSIDES OF OLIGODENDROCYTES.
  8. "Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and 'brain-type' neutral N-glycans."
    Zamze S., Harvey D.J., Pesheva P., Mattu T.S., Schachner M., Dwek R.A., Wing D.R.
    Glycobiology 9:823-831(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  9. "Involvement of chondroitin sulfates on brain-derived tenascin-R in carbohydrate-dependent interactions with fibronectin and tenascin-C."
    Probstmeier R., Braunewell K.-H., Pesheva P.
    Brain Res. 863:42-51(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, INTERACTION WITH FN1 AND TNC, FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiTENR_MOUSE
AccessioniPrimary (citable) accession number: Q8BYI9
Secondary accession number(s): A2RT70, O88717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Knockout mice display alterations of the extracellular matrix, and decreased axonal conduction velocities in the CNS.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.