GenomeNet

Database: UniProt
Entry: P10039
LinkDB: P10039
Original site: P10039 
ID   TENA_CHICK              Reviewed;        1808 AA.
AC   P10039; O73584; O73585; P13132;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 2.
DT   13-FEB-2019, entry version 163.
DE   RecName: Full=Tenascin;
DE            Short=TN;
DE   AltName: Full=Cytotactin;
DE   AltName: Full=GMEM;
DE   AltName: Full=GP 150-225;
DE   AltName: Full=Glioma-associated-extracellular matrix antigen;
DE   AltName: Full=Hexabrachion;
DE   AltName: Full=JI;
DE   AltName: Full=Myotendinous antigen;
DE   AltName: Full=Neuronectin;
DE   AltName: Full=Tenascin-C;
DE            Short=TN-C;
DE   Flags: Precursor;
GN   Name=TNC;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Embryo;
RX   PubMed=2478295; DOI=10.1016/0092-8674(89)90294-8;
RA   Spring J., Beck K., Chiquet-Ehrismann R.;
RT   "Two contrary functions of tenascin: dissection of the active sites by
RT   recombinant tenascin fragments.";
RL   Cell 59:325-334(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-722 (ISOFORMS 1/2/3), AND PROTEIN
RP   SEQUENCE OF 79-96.
RC   TISSUE=Fibroblast;
RX   PubMed=2460335;
RA   Pearson C.A., Pearson D., Shibahara S., Hofsteenge J.,
RA   Chiquet-Ehrismann R.;
RT   "Tenascin: cDNA cloning and induction by TGF-beta.";
RL   EMBO J. 7:2977-2982(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 464-1018 AND 1412-1661 (ISOFORMS 1/2/3),
RP   AND PROTEIN SEQUENCE OF 852-868.
RC   TISSUE=Embryo;
RX   PubMed=2451243; DOI=10.1073/pnas.85.7.2186;
RA   Jones F.S., Burgoon M.P., Hoffman S., Crossin K.L., Cunningham B.A.,
RA   Edelman G.M.;
RT   "A cDNA clone for cytotactin contains sequences similar to epidermal
RT   growth factor-like repeats and segments of fibronectin and
RT   fibrinogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:2186-2190(1988).
RN   [4]
RP   INTERACTION WITH CSPG5.
RX   PubMed=9049254; DOI=10.1083/jcb.136.4.895;
RA   Schumacher S., Volkmer H., Buck F., Otto A., Tarnok A., Roth S.,
RA   Rathjen F.G.;
RT   "Chicken acidic leucine-rich EGF-like domain containing brain protein
RT   (CALEB), a neural member of the EGF family of differentiation factors,
RT   is implicated in neurite formation.";
RL   J. Cell Biol. 136:895-906(1997).
RN   [5]
RP   INTERACTION WITH CSPG5, AND DOMAIN.
RX   PubMed=11069908; DOI=10.1074/jbc.M007234200;
RA   Schumacher S., Jung M., Noerenberg U., Dorner A.,
RA   Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.;
RT   "CALEB binds via its acidic stretch to the fibrinogen-like domain of
RT   tenascin-C or tenascin-R and its expression is dynamically regulated
RT   after optic nerve lesion.";
RL   J. Biol. Chem. 276:7337-7345(2001).
CC   -!- FUNCTION: Extracellular matrix protein implicated in guidance of
CC       migrating neurons as well as axons during development, synaptic
CC       plasticity as well as neuronal regeneration. Ligand for integrins
CC       alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.
CC   -!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed
CC       in the triple coiled-coil region and may be stabilized by
CC       disulfide rings at both ends. Two of such half-hexabrachions may
CC       be disulfide linked within the central globule. Interacts with
CC       CSPG4. {ECO:0000269|PubMed:11069908, ECO:0000269|PubMed:9049254}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Isoforms are produced in a tissue- and time-specific
CC         manner during development.;
CC       Name=1; Synonyms=230 kDa;
CC         IsoId=P10039-1; Sequence=Displayed;
CC       Name=2; Synonyms=200 kDa;
CC         IsoId=P10039-2; Sequence=VSP_001410;
CC       Name=3; Synonyms=190 kDa;
CC         IsoId=P10039-3; Sequence=VSP_001411;
CC   -!- INDUCTION: By TGF-beta.
CC   -!- DOMAIN: The fibrinogen C-terminal domain mediates interaction with
CC       CSPG5. {ECO:0000269|PubMed:11069908}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
DR   EMBL; M23121; AAA49086.1; -; mRNA.
DR   EMBL; X08031; CAB40811.1; -; mRNA.
DR   EMBL; X08030; CAA30824.1; ALT_TERM; mRNA.
DR   EMBL; J03641; AAA48748.1; ALT_SEQ; mRNA.
DR   EMBL; M20816; AAA48749.1; ALT_SEQ; mRNA.
DR   PIR; A31930; A31930.
DR   UniGene; Gga.3818; -.
DR   UniGene; Gga.51524; -.
DR   PDB; 1QR4; X-ray; 2.55 A; A/B=950-1042, A/B=1316-1408.
DR   PDBsum; 1QR4; -.
DR   ProteinModelPortal; P10039; -.
DR   SMR; P10039; -.
DR   IntAct; P10039; 1.
DR   STRING; 9031.ENSGALP00000011509; -.
DR   PaxDb; P10039; -.
DR   PRIDE; P10039; -.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG2579; Eukaryota.
DR   eggNOG; ENOG4111MDJ; LUCA.
DR   HOVERGEN; HBG008949; -.
DR   InParanoid; P10039; -.
DR   OrthoDB; 18592at2759; -.
DR   EvolutionaryTrace; P10039; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR   CDD; cd00063; FN3; 11.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 2.60.40.10; -; 11.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR033078; TNC.
DR   PANTHER; PTHR19143:SF38; PTHR19143:SF38; 5.
DR   Pfam; PF07974; EGF_2; 3.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 11.
DR   SMART; SM00181; EGF; 13.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 11.
DR   SUPFAM; SSF49265; SSF49265; 8.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS00022; EGF_1; 14.
DR   PROSITE; PS01186; EGF_2; 14.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 11.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion;
KW   Cleavage on pair of basic residues; Coiled coil; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     22
FT   PROPEP       23     33
FT                                /FTId=PRO_0000007743.
FT   CHAIN        34   1808       Tenascin.
FT                                /FTId=PRO_0000007744.
FT   DOMAIN      176    188       EGF-like 1; incomplete.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      188    219       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      219    250       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      250    281       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      281    312       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      312    343       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      343    374       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      374    405       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      405    436       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      436    467       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      467    498       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      498    529       EGF-like 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      529    560       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      560    591       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      595    685       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      686    775       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      776    866       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      867    957       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      958   1046       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1047   1138       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1139   1228       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1229   1318       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1319   1408       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1409   1495       Fibronectin type-III 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1496   1584       Fibronectin type-III 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1582   1797       Fibrinogen C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   COILED      118    142       {ECO:0000255}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    168    168       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    186    186       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    328    328       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    603    603       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    643    643       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    751    751       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    759    759       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1050   1050       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1090   1090       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1101   1101       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1112   1112       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1153   1153       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1183   1183       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1416   1416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1736   1736       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1769   1769       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     64     64       Interchain. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00739}.
FT   DISULFID    192    202       {ECO:0000250}.
FT   DISULFID    196    207       {ECO:0000250}.
FT   DISULFID    209    218       {ECO:0000250}.
FT   DISULFID    223    233       {ECO:0000250}.
FT   DISULFID    227    238       {ECO:0000250}.
FT   DISULFID    240    249       {ECO:0000250}.
FT   DISULFID    254    264       {ECO:0000250}.
FT   DISULFID    258    269       {ECO:0000250}.
FT   DISULFID    271    280       {ECO:0000250}.
FT   DISULFID    285    295       {ECO:0000250}.
FT   DISULFID    289    300       {ECO:0000250}.
FT   DISULFID    302    311       {ECO:0000250}.
FT   DISULFID    316    326       {ECO:0000250}.
FT   DISULFID    320    331       {ECO:0000250}.
FT   DISULFID    333    342       {ECO:0000250}.
FT   DISULFID    347    357       {ECO:0000250}.
FT   DISULFID    351    362       {ECO:0000250}.
FT   DISULFID    364    373       {ECO:0000250}.
FT   DISULFID    378    388       {ECO:0000250}.
FT   DISULFID    382    393       {ECO:0000250}.
FT   DISULFID    395    404       {ECO:0000250}.
FT   DISULFID    409    419       {ECO:0000250}.
FT   DISULFID    413    424       {ECO:0000250}.
FT   DISULFID    426    435       {ECO:0000250}.
FT   DISULFID    440    450       {ECO:0000250}.
FT   DISULFID    444    455       {ECO:0000250}.
FT   DISULFID    457    466       {ECO:0000250}.
FT   DISULFID    471    481       {ECO:0000250}.
FT   DISULFID    475    486       {ECO:0000250}.
FT   DISULFID    488    497       {ECO:0000250}.
FT   DISULFID    502    512       {ECO:0000250}.
FT   DISULFID    506    517       {ECO:0000250}.
FT   DISULFID    519    528       {ECO:0000250}.
FT   DISULFID    533    543       {ECO:0000250}.
FT   DISULFID    537    548       {ECO:0000250}.
FT   DISULFID    550    559       {ECO:0000250}.
FT   DISULFID    564    574       {ECO:0000250}.
FT   DISULFID    568    579       {ECO:0000250}.
FT   DISULFID    581    590       {ECO:0000250}.
FT   VAR_SEQ    1043   1315       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:2478295}.
FT                                /FTId=VSP_001411.
FT   VAR_SEQ    1043   1224       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:2478295}.
FT                                /FTId=VSP_001410.
FT   CONFLICT    182    182       W -> R (in Ref. 2; CAA30824).
FT                                {ECO:0000305}.
FT   CONFLICT    563    571       SCPNDCNNV -> PAPMTATTW (in Ref. 3;
FT                                AAA48748). {ECO:0000305}.
FT   CONFLICT    598    598       E -> G (in Ref. 3; AAA48748).
FT                                {ECO:0000305}.
FT   CONFLICT    838    838       T -> TEY (in Ref. 3; AAA48748).
FT                                {ECO:0000305}.
FT   CONFLICT    886    886       N -> F (in Ref. 3; AAA48748).
FT                                {ECO:0000305}.
FT   STRAND     1233   1237       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1240   1248       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1255   1262       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1268   1272       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1280   1286       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1292   1303       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1309   1314       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1323   1327       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1333   1337       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1345   1353       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1360   1365       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1370   1373       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1381   1390       {ECO:0000244|PDB:1QR4}.
FT   STRAND     1398   1403       {ECO:0000244|PDB:1QR4}.
SQ   SEQUENCE   1808 AA;  198859 MW;  B924A06CF9EFD6DE CRC64;
     MGLPSQVLAC AILGLLYQHA SGGLIKRIIR QKRETGLNVT LPEDNQPVVF NHVYNIKLPV
     GSLCSVDLDT ASGDADLKAE IEPVKNYEEH TVNEGNQIVF THRINIPRRA CGCAAAPDIK
     DLLSRLEELE GLVSSLREQC ASGAGCCPNS QTAEGRLDTA PYCSGHGNYS TEICGCVCEP
     GWKGPNCSEP ACPRNCLNRG LCVRGKCICE EGFTGEDCSQ AACPSDCNDQ GKCVDGVCVC
     FEGYTGPDCG EELCPHGCGI HGRCVGGRCV CHEGFTGEDC NEPLCPNNCH NRGRCVDNEC
     VCDEGYTGED CGELICPNDC FDRGRCINGT CFCEEGYTGE DCGELTCPNN CNGNGRCENG
     LCVCHEGFVG DDCSQKRCPK DCNNRGHCVD GRCVCHEGYL GEDCGELRCP NDCHNRGRCI
     NGQCVCDEGF IGEDCGELRC PNDCHNRGRC VNGQCECHEG FIGEDCGELR CPNDCNSHGR
     CVNGQCVCDE GYTGEDCGEL RCPNDCHNRG RCVEGRCVCD NGFMGEDCGE LSCPNDCHQH
     GRCVDGRCVC HEGFTGEDCR ERSCPNDCNN VGRCVEGRCV CEEGYMGIDC SDVSPPTELT
     VTNVTDKTVN LEWKHENLVN EYLVTYVPTS SGGLDLQFTV PGNQTSATIH ELEPGVEYFI
     RVFAILKNKK SIPVSARVAT YLPAPEGLKF KSVRETSVQV EWDPLSISFD GWELVFRNMQ
     KKDDNGDITS SLKRPETSYM QPGLAPGQQY NVSLHIVKNN TRGPGLSRVI TTKLDAPSQI
     EAKDVTDTTA LITWSKPLAE IEGIELTYGP KDVPGDRTTI DLSEDENQYS IGNLRPHTEY
     EVTLISRRGD MESDPAKEVF VTDLDAPRNL KRVSQTDNSI TLEWKNSHAN IDNYRIKFAP
     ISGGDHTELT VPKGNQATTR ATLTGLRPGT EYGIGVTAVR QDRESAPATI NAGTDLDNPK
     DLEVSDPTET TLSLRWRRPV AKFDRYRLTY VSPSGKKNEM EIPVDSTSFI LRGLDAGTEY
     TISLVAEKGR HKSKPTTIKG STEEEPELGN LSVSETGWDG FQLTWTAADG AYENFVIQVQ
     QSDNPEETWN ITVPGGQHSV NVTGLKANTP YNVTLYGVIR GYRTKPLYVE TTTGAHPEVG
     ELTVSDITPE SFNLSWTTTN GDFDAFTIEI IDSNRLLEPM EFNISGNSRT AHISGLSPST
     DFIVYLYGIS HGFRTQAISA AATTEAEPEV DNLLVSDATP DGFRLSWTAD DGVFDSFVLK
     IRDTKRKSDP LELIVPGHER THDITGLKEG TEYEIELYGV SSGRRSQPIN SVATTVVGSP
     KGISFSDITE NSATVSWTPP RSRVDSYRVS YVPITGGTPN VVTVDGSKTR TKLVKLVPGV
     DYNVNIISVK GFEESEPISG ILKTALDSPS GLVVMNITDS EALATWQPAI AAVDNYIVSY
     SSEDEPEVTQ MVSGNTVEYD LNGLRPATEY TLRVHAVKDA QKSETLSTQF TTGLDAPKDL
     SATEVQSETA VITWRPPRAP VTDYLLTYES IDGRVKEVIL DPETTSYTLT ELSPSTQYTV
     KLQALSRSMR SKMIQTVFTT TGLLYPYPKD CSQALLNGEV TSGLYTIYLN GDRTQPLQVF
     CDMAEDGGGW IVFLRRQNGK EDFYRNWKNY VAGFGDPKDE FWIGLENLHK ISSQGQYELR
     VDLRDRGETA YAVYDKFSVG DAKTRYRLRV DGYSGTAGDS MTYHNGRSFS TFDKDNDSAI
     TNCALSYKGA FWYKNCHRVN LMGRYGDNNH SQGVNWFHWK GHEYSIQFAE MKLRPSSFRN
     LEGRRKRA
//
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