TENN_MOUSE
ID TENN_MOUSE Reviewed; 1560 AA.
AC Q80Z71; B9EHR3; Q70HX0;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Tenascin-N {ECO:0000312|MGI:MGI:2665790};
DE Short=TN-N;
DE AltName: Full=Tenascin-W {ECO:0000303|PubMed:14709716};
DE Short=TN-W {ECO:0000303|PubMed:14709716};
DE Flags: Precursor;
GN Name=Tnn {ECO:0000312|MGI:MGI:2665790};
GN Synonyms=Tnw {ECO:0000303|PubMed:14709716};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAO63807.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO63807.1};
RX PubMed=12812753; DOI=10.1016/s1044-7431(03)00012-5;
RA Neidhardt J., Fehr S., Kutsche M., Loehler J., Schachner M.;
RT "Tenascin-N: characterization of a novel member of the tenascin family that
RT mediates neurite repulsion from hippocampal explants.";
RL Mol. Cell. Neurosci. 23:193-209(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=14709716; DOI=10.1242/jcs.00867;
RA Scherberich A., Tucker R.P., Samandari E., Brown-Luedi M., Martin D.,
RA Chiquet-Ehrismann R.;
RT "Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at
RT sites of bone and smooth muscle development.";
RL J. Cell Sci. 117:571-581(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 1524-1535, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15592496; DOI=10.1038/sj.onc.1208342;
RA Scherberich A., Tucker R.P., Degen M., Brown-Luedi M., Andres A.C.,
RA Chiquet-Ehrismann R.;
RT "Tenascin-W is found in malignant mammary tumors, promotes alpha8 integrin-
RT dependent motility and requires p38MAPK activity for BMP-2 and TNF-alpha
RT induced expression in vitro.";
RL Oncogene 24:1525-1532(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17395156; DOI=10.1016/j.bbrc.2007.03.071;
RA Kimura H., Akiyama H., Nakamura T., de Crombrugghe B.;
RT "Tenascin-W inhibits proliferation and differentiation of preosteoblasts
RT during endochondral bone formation.";
RL Biochem. Biophys. Res. Commun. 356:935-941(2007).
RN [7]
RP FUNCTION.
RX PubMed=22211116; DOI=10.7150/ijbs.8.187;
RA Brellier F., Martina E., Chiquet M., Ferralli J., van der Heyden M.,
RA Orend G., Schittny J.C., Chiquet-Ehrismann R., Tucker R.P.;
RT "The adhesion modulating properties of tenascin-W.";
RL Int. J. Biol. Sci. 8:187-194(2012).
CC -!- FUNCTION: Extracellular matrix protein that seems to be a ligand for
CC ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1 (By similarity)
CC (PubMed:14709716). Involved in neurite outgrowth and cell migration in
CC hippocampal explants (PubMed:12812753). During endochondral bone
CC formation, inhibits proliferation and differentiation of proteoblasts
CC mediated by canonical WNT signaling (PubMed:17395156). In tumors,
CC stimulates angiogenesis by elongation, migration and sprouting of
CC endothelial cells (By similarity). Expressed in most mammary tumors,
CC may facilitate tumorigenesis by supporting the migratory behavior of
CC breast cancer cells (PubMed:15592496). {ECO:0000250|UniProtKB:Q9UQP3,
CC ECO:0000269|PubMed:12812753, ECO:0000269|PubMed:14709716,
CC ECO:0000269|PubMed:15592496, ECO:0000269|PubMed:17395156}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:14709716}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:15592496}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.
CC {ECO:0000269|PubMed:12812753};
CC Name=1;
CC IsoId=Q80Z71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80Z71-2; Sequence=VSP_058850;
CC -!- TISSUE SPECIFICITY: Highest expression in kidney followed by spleen and
CC brain. In brain, highest expression is found in hippocampus, cerebellum
CC and olfactory bulb. Expressed in aortic valve, corneal limbus
CC (PubMed:14709716). Expressed in ribs periosteum. During a fracture
CC repair process, expression increases in cells of newly formed
CC perichondrium/peristeum surrounding the cartalaginous callus
CC (PubMed:14709716, PubMed:17395156). {ECO:0000269|PubMed:12812753,
CC ECO:0000269|PubMed:14709716, ECO:0000269|PubMed:17395156}.
CC -!- DEVELOPMENTAL STAGE: Hardly detectable at embryonic day (E) 14, then
CC increases until postnatal day 17 and remains detectable in the adult
CC (PubMed:12812753). Expressed as early as 11.5 dpc in the maxillary
CC process until 16.5 dpc when is expressed in the newly formed mandible.
CC At 14.5 dpc is detected in smooth muscle cells of the stomach and
CC intestine and at 15.5, in the periosteum of the ribs. At 16.5 dpc the
CC expression is restricted to mandible, palate and teeth
CC (PubMed:14709716). During endochondral bone formation, first expressed
CC at 13.5 dpc in the perichondrium. At E 16.5, detected in perichondrium
CC and periosteum (PubMed:17395156). {ECO:0000269|PubMed:12812753,
CC ECO:0000269|PubMed:14709716, ECO:0000269|PubMed:17395156}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
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DR EMBL; AF455756; AAO63807.1; -; mRNA.
DR EMBL; AJ580920; CAE45651.1; -; mRNA.
DR EMBL; BC138335; AAI38336.1; -; mRNA.
DR EMBL; BC138336; AAI38337.1; -; mRNA.
DR CCDS; CCDS15404.1; -. [Q80Z71-1]
DR RefSeq; NP_808507.2; NM_177839.3. [Q80Z71-1]
DR AlphaFoldDB; Q80Z71; -.
DR SMR; Q80Z71; -.
DR ComplexPortal; CPX-1013; Tenascin-W complex.
DR STRING; 10090.ENSMUSP00000039452; -.
DR GlyGen; Q80Z71; 1 site.
DR iPTMnet; Q80Z71; -.
DR PhosphoSitePlus; Q80Z71; -.
DR MaxQB; Q80Z71; -.
DR PaxDb; Q80Z71; -.
DR PRIDE; Q80Z71; -.
DR ProteomicsDB; 263273; -. [Q80Z71-1]
DR ProteomicsDB; 263274; -. [Q80Z71-2]
DR ABCD; Q80Z71; 2 sequenced antibodies.
DR Antibodypedia; 4397; 115 antibodies from 27 providers.
DR DNASU; 329278; -.
DR Ensembl; ENSMUST00000039178; ENSMUSP00000039452; ENSMUSG00000026725. [Q80Z71-1]
DR GeneID; 329278; -.
DR KEGG; mmu:329278; -.
DR UCSC; uc007dee.2; mouse. [Q80Z71-1]
DR CTD; 63923; -.
DR MGI; MGI:2665790; Tnn.
DR VEuPathDB; HostDB:ENSMUSG00000026725; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000160553; -.
DR InParanoid; Q80Z71; -.
DR OMA; KGDRQSR; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q80Z71; -.
DR TreeFam; TF329915; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 329278; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q80Z71; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80Z71; protein.
DR Bgee; ENSMUSG00000026725; Expressed in diaphysis of femur and 35 other tissues.
DR ExpressionAtlas; Q80Z71; baseline and differential.
DR Genevisible; Q80Z71; MM.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990026; C:hippocampal mossy fiber expansion; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0090733; C:tenascin complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IDA:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR GO; GO:0070593; P:dendrite self-avoidance; IDA:UniProtKB.
DR GO; GO:1905240; P:negative regulation of canonical Wnt signaling pathway involved in osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:2001223; P:negative regulation of neuron migration; IDA:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IDA:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IDA:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; IDA:UniProtKB.
DR GO; GO:0002076; P:osteoblast development; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ComplexPortal.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:1903010; P:regulation of bone development; IDA:ComplexPortal.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:ComplexPortal.
DR GO; GO:0030334; P:regulation of cell migration; IDA:ComplexPortal.
DR GO; GO:1905899; P:regulation of smooth muscle tissue development; IDA:ComplexPortal.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00063; FN3; 12.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 12.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR041161; EGF_Tenascin.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF18720; EGF_Tenascin; 2.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 12.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 12.
DR SUPFAM; SSF49265; SSF49265; 7.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1560
FT /note="Tenascin-N"
FT /id="PRO_0000007746"
FT DOMAIN 167..198
FT /note="EGF-like 1"
FT DOMAIN 199..229
FT /note="EGF-like 2"
FT DOMAIN 230..260
FT /note="EGF-like 3"
FT DOMAIN 264..353
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 354..444
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 445..532
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 533..622
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 623..706
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 709..798
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 799..882
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 885..970
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 973..1062
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1063..1144
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1149..1238
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1239..1325
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1323..1540
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 868..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 171..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 175..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 188..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 202..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 206..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 219..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 233..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 237..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 250..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 832..1095
FT /note="Missing (in isoform 2)"
FT /id="VSP_058850"
FT CONFLICT 354
FT /note="V -> L (in Ref. 2; CAE45651)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="T -> A (in Ref. 2; CAE45651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1199
FT /note="S -> N (in Ref. 2; CAE45651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1221
FT /note="A -> P (in Ref. 1; AAO63807)"
FT /evidence="ECO:0000305"
FT CONFLICT 1278
FT /note="E -> G (in Ref. 2; CAE45651)"
FT /evidence="ECO:0000305"
FT CONFLICT 1479
FT /note="N -> S (in Ref. 2; CAE45651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1560 AA; 173090 MW; 672FBADBC2DAFCB2 CRC64;
MGLWGMLAFP LGFLLASVLL VASAPATPES PGCSNKEQQV TVSHTYKIDV PKSALVQVET
DPQSLSDDGT SLLAPGEDGE EQNIIFRHNI RLQTPQKNCD LADSVQDLLA RMKKLEEEMA
ELKEQCNTNR CCQGAADLSR HCSGHGTFLP ETCSCHCDQG WEGADCDQPT CPGACNGHGR
CVDGQCVCDA PYVGVDCAYA ACPQDCSGHG VCVQGVCQCH EDFTAEDCSE QRCPGDCSGN
GFCDTGECYC EMGFTGPDCS QVVAPQGLQL LKSTENSLLV SWEPSSEVDY YLLSYYPLGK
EQATKQVRVP KEQHTYDITG LLPGTKYIVT LRNVKKDISS SPQHLLATTD LAVVGTAWVN
EETETSLDVE WENPLTEVDY YKLRYGPLTG QEVTEVTVPK SRDPKSRYDI TGLQPGTEYK
ITVVPIRGDL EGKPILLNGR TEIDGPTNVV TNQVTEDTAS VSWDPVRADI DKYVVRYIAP
DGETKEKAVP KDQSSTVLTG LKPGEAYKVF VWAERGNQGS KKADTKALTE IDSPENLVTD
RVTENSLSVS WDPVEADIDR YVVSYTSVDG ETKQVPVKKD QRSTVLTGLS PGVEYKVYVW
AEKGDRESKK ANTKAPTDID SPKNLVTDQV TENTLSVSWD PVQANIDRYM VSYTSADGET
REVPVPKEKS STVLTGLRPG VEYKVHVWAQ KGTQESRKAN TKAPTDIDGP KNLVTDQVTE
TTLSVSWDPV EADIDRYMVR YTSPDGETKE VPVSKDKSST VLRGLRPGVE YKVDVWAQKG
AQDSRKANTK APTDIDSPKN LVTEQVTEST ATVSWDPVEA DIDRYVVRYT SVDGETREFL
VGKDQTSTVL TGMRPGVEYQ VDVWAQKGTQ ESRKTSTKAP TDIDGPKNLV TDQVTETTLS
VSWDPVEADI DRYMVRYTSP DGETKEVPVS KDKSSTVLRG LRPGVEYKVD VWAQKGAQDS
RKANTKAPTD IDSPKNLAID QVTETTLSVS WDPVQADIDR YVVRYTSADG ESKEFLIGKE
QRSTVLTGLR PGVEYKVEVW AQKGARESKK ANTEGHTDID SPKNLVTNQV TENTATISWD
PVQADIDRYM VRYTSADGET REIPVRKEKS STVLTGLRPG VEYTVQVWAQ KGARESKKAK
TKAPTEIDSP KNLVTNRVTE NTATISWDPV RANIDRYMVR YTSADGETKE IPVSKDQSST
ILTGLKPGME YTIHVWAQKG ARESKKADTK ALTEIDPPRN LRPFGVTHSG GVLTWLPPSA
QIDGYILTYQ FPNGTVKEVE LPRGQQRFEL QDLEQGVTYP VSLVAFKGNQ RSRTVSTTLS
TVDARFPHPS DCSQVQQNTN AASGLYTIYL NGDASRPMQV YCDMDTDGGG WIVFQRRNTG
QLDFFKRWRS YVEGFGDPMK EFWLGLDKLH NLTTGTTTRY EVRADLQTFN ESAYAVYDFF
QVASSKERYK LSVGKYRGTA GDALTYHNGW KFTTFDRDND IALSNCALTH HGGWWYKNCH
LANPNGKYGE TKHSEGVNWE PWKGHEFSIP YVELKIRPFG YSRDRFSGRK KRSIGKARMF
