TENN_HUMAN
ID TENN_HUMAN Reviewed; 1299 AA.
AC Q9UQP3; A0A0A6YY94; B9EGP3; Q5R360;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Tenascin-N {ECO:0000312|HGNC:HGNC:22942};
DE Short=TN-N;
DE AltName: Full=Tenascin-W {ECO:0000303|PubMed:17909022};
DE Short=TN-W;
DE Flags: Precursor;
GN Name=TNN {ECO:0000312|HGNC:HGNC:22942};
GN Synonyms=TNW {ECO:0000303|PubMed:17909022};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:CAB41260.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1299.
RA Rhodes S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1149.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17909022; DOI=10.1158/0008-5472.can-07-0666;
RA Degen M., Brellier F., Kain R., Ruiz C., Terracciano L., Orend G.,
RA Chiquet-Ehrismann R.;
RT "Tenascin-W is a novel marker for activated tumor stroma in low-grade human
RT breast cancer and influences cell behavior.";
RL Cancer Res. 67:9169-9179(2007).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19884327; DOI=10.1096/fj.09-140491;
RA Martina E., Degen M., Rueegg C., Merlo A., Lino M.M., Chiquet-Ehrismann R.,
RA Brellier F.;
RT "Tenascin-W is a specific marker of glioma-associated blood vessels and
RT stimulates angiogenesis in vitro.";
RL FASEB J. 24:778-787(2010).
CC -!- FUNCTION: Extracellular matrix protein that seems to be a ligand for
CC ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1 (By similarity)
CC (PubMed:17909022). Involved in neurite outgrowth and cell migration in
CC hippocampal explants (By similarity). During endochondral bone
CC formation, inhibits proliferation and differentiation of proteoblasts
CC mediated by canonical WNT signaling (By similarity). In tumors,
CC stimulates angiogenesis by elongation, migration and sprouting of
CC endothelial cells (PubMed:19884327). Expressed in most mammary tumors,
CC may facilitate tumorigenesis by supporting the migratory behavior of
CC breast cancer cells (PubMed:17909022). {ECO:0000250|UniProtKB:Q80YX1,
CC ECO:0000250|UniProtKB:Q80Z71, ECO:0000269|PubMed:17909022,
CC ECO:0000269|PubMed:19884327}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q80Z71}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:19884327}.
CC -!- TISSUE SPECIFICITY: Not detected in normal adult mammary tissues or
CC brain but expressed in most breast tumors and brain tumors, such as
CC glioblastomas, astrocytomas and oligodendrogliomas, tested
CC (PubMed:17909022, PubMed:19884327). In brain tumors, detected around
CC the endothelial cell layer of the clood vessels (PubMed:19884327).
CC {ECO:0000269|PubMed:17909022, ECO:0000269|PubMed:19884327}.
CC -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TNNID44209ch1q25.html";
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DR EMBL; Z99297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136619; AAI36620.1; -; mRNA.
DR EMBL; AL049689; CAB41260.1; -; mRNA.
DR CCDS; CCDS30943.1; -.
DR RefSeq; NP_071376.1; NM_022093.1.
DR AlphaFoldDB; Q9UQP3; -.
DR SMR; Q9UQP3; -.
DR BioGRID; 121992; 5.
DR ComplexPortal; CPX-1012; Tenascin-W complex.
DR IntAct; Q9UQP3; 1.
DR STRING; 9606.ENSP00000239462; -.
DR GlyConnect; 1793; 11 N-Linked glycans (3 sites).
DR GlyGen; Q9UQP3; 4 sites, 12 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9UQP3; -.
DR PhosphoSitePlus; Q9UQP3; -.
DR BioMuta; TNN; -.
DR DMDM; 81175198; -.
DR EPD; Q9UQP3; -.
DR jPOST; Q9UQP3; -.
DR MassIVE; Q9UQP3; -.
DR PaxDb; Q9UQP3; -.
DR PeptideAtlas; Q9UQP3; -.
DR PRIDE; Q9UQP3; -.
DR ProteomicsDB; 85562; -.
DR ABCD; Q9UQP3; 3 sequenced antibodies.
DR Antibodypedia; 4397; 115 antibodies from 27 providers.
DR DNASU; 63923; -.
DR Ensembl; ENST00000239462.9; ENSP00000239462.4; ENSG00000120332.17.
DR GeneID; 63923; -.
DR KEGG; hsa:63923; -.
DR MANE-Select; ENST00000239462.9; ENSP00000239462.4; NM_022093.2; NP_071376.1.
DR UCSC; uc001gkl.1; human.
DR CTD; 63923; -.
DR DisGeNET; 63923; -.
DR GeneCards; TNN; -.
DR HGNC; HGNC:22942; TNN.
DR HPA; ENSG00000120332; Tissue enhanced (adipose tissue, breast).
DR MIM; 617472; gene.
DR neXtProt; NX_Q9UQP3; -.
DR OpenTargets; ENSG00000120332; -.
DR PharmGKB; PA134973710; -.
DR VEuPathDB; HostDB:ENSG00000120332; -.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000160553; -.
DR InParanoid; Q9UQP3; -.
DR OMA; KGDRQSR; -.
DR OrthoDB; 18592at2759; -.
DR PhylomeDB; Q9UQP3; -.
DR TreeFam; TF329915; -.
DR PathwayCommons; Q9UQP3; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR SignaLink; Q9UQP3; -.
DR BioGRID-ORCS; 63923; 7 hits in 1070 CRISPR screens.
DR ChiTaRS; TNN; human.
DR GenomeRNAi; 63923; -.
DR Pharos; Q9UQP3; Tbio.
DR PRO; PR:Q9UQP3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UQP3; protein.
DR Bgee; ENSG00000120332; Expressed in periodontal ligament and 81 other tissues.
DR ExpressionAtlas; Q9UQP3; baseline and differential.
DR Genevisible; Q9UQP3; HS.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990026; C:hippocampal mossy fiber expansion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0090733; C:tenascin complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; ISA:UniProtKB.
DR GO; GO:1905240; P:negative regulation of canonical Wnt signaling pathway involved in osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISA:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; IBA:GO_Central.
DR GO; GO:0002076; P:osteoblast development; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:ComplexPortal.
DR GO; GO:1903010; P:regulation of bone development; IEA:Ensembl.
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; IEA:Ensembl.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00063; FN3; 9.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.60.40.10; -; 9.
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; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 9.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 9.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 9.
PE 1: Evidence at protein level;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1299
FT /note="Tenascin-N"
FT /id="PRO_0000007745"
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..352
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 353..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..623
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 624..709
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 710..800
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 801..886
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 887..976
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 977..1063
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1061..1278
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 605..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
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 VARIANT 79
FT /note="R -> G (in dbSNP:rs2072032)"
FT /id="VAR_049007"
FT VARIANT 289
FT /note="D -> N (in dbSNP:rs16847812)"
FT /id="VAR_033832"
FT VARIANT 440
FT /note="R -> S (in dbSNP:rs6664276)"
FT /id="VAR_049008"
FT VARIANT 499
FT /note="T -> M (in dbSNP:rs17374761)"
FT /id="VAR_033833"
FT VARIANT 807
FT /note="W -> R (in dbSNP:rs6696455)"
FT /id="VAR_033834"
FT VARIANT 859
FT /note="M -> V (in dbSNP:rs6694078)"
FT /id="VAR_059275"
FT VARIANT 930
FT /note="P -> L (in dbSNP:rs2285215)"
FT /id="VAR_024269"
FT VARIANT 941
FT /note="T -> M (in dbSNP:rs10798333)"
FT /id="VAR_033835"
FT VARIANT 1135
FT /note="D -> E (in dbSNP:rs10158841)"
FT /id="VAR_049009"
FT VARIANT 1156
FT /note="A -> V (in dbSNP:rs2072036)"
FT /id="VAR_049010"
SQ SEQUENCE 1299 AA; 144034 MW; CC4BBD5CE47ADBED CRC64;
MSLQEMFRFP MGLLLGSVLL VASAPATLEP PGCSNKEQQV TVSHTYKIDV PKSALVQVDA
DPQPLSDDGA SLLALGEARE EQNIIFRHNI RLQTPQKDCE LAGSVQDLLA RVKKLEEEMV
EMKEQCSAQR CCQGVTDLSR HCSGHGTFSL ETCSCHCEEG REGPACERLA CPGACSGHGR
CVDGRCLCHE PYVGADCGYP ACPENCSGHG ECVRGVCQCH EDFMSEDCSE KRCPGDCSGH
GFCDTGECYC EEGFTGLDCA QVVTPQGLQL LKNTEDSLLV SWEPSSQVDH YLLSYYPLGK
ELSGKQIQVP KEQHSYEILG LLPGTKYIVT LRNVKNEVSS SPQHLLATTD LAVLGTAWVT
DETENSLDVE WENPSTEVDY YKLRYGPMTG QEVAEVTVPK SSDPKSRYDI TGLHPGTEYK
ITVVPMRGEL EGKPILLNGR TEIDSPTNVV TDRVTEDTAT VSWDPVQAVI DKYVVRYTSA
DGDTKEMAVH KDESSTVLTG LKPGEAYKVY VWAERGNQGS KKADTNALTE IDSPANLVTD
RVTENTATIS WDPVQATIDK YVVRYTSADD QETREVLVGK EQSSTVLTGL RPGVEYTVHV
WAQKGDRESK KADTNAPTDI DSPKNLVTDR VTENMATVSW DPVQAAIDKY VVRYTSAGGE
TREVPVGKEQ SSTVLTGLRP GMEYMVHVWA QKGDQESKKA DTKAQTDIDS PQNLVTDRVT
ENMATVSWDP VRATIDRYVV RYTSAKDGET REVPVGKEQS STVLTGLRPG VEYTVHVWAQ
KGAQESKKAD TKAQTDIDSP QNLVTDWVTE NTATVSWDPV QATIDRYVVH YTSANGETRE
VPVGKEQSST VLTGLRPGME YTVHVWAQKG NQESKKADTK AQTEIDGPKN LVTDWVTENM
ATVSWDPVQA TIDKYMVRYT SADGETREVP VGKEHSSTVL TGLRPGMEYM VHVWAQKGAQ
ESKKADTKAQ TELDPPRNLR PSAVTQSGGI LTWTPPSAQI HGYILTYQFP DGTVKEMQLG
REDQRFALQG LEQGATYPVS LVAFKGGRRS RNVSTTLSTV GARFPHPSDC SQVQQNSNAA
SGLYTIYLHG DASRPLQVYC DMETDGGGWI VFQRRNTGQL DFFKRWRSYV EGFGDPMKEF
WLGLDKLHNL TTGTPARYEV RVDLQTANES AYAIYDFFQV ASSKERYKLT VGKYRGTAGD
ALTYHNGWKF TTFDRDNDIA LSNCALTHHG GWWYKNCHLA NPNGRYGETK HSEGVNWEPW
KGHEFSIPYV ELKIRPHGYS REPVLGRKKR TLRGRLRTF
