ID   E9PC84_HUMAN            Unreviewed;      1928 AA.
AC   E9PC84;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   13-FEB-2019, entry version 67.
DE   SubName: Full=Tenascin {ECO:0000313|Ensembl:ENSP00000411406};
GN   Name=TNC {ECO:0000313|Ensembl:ENSP00000411406};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000411406, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000411406, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [2] {ECO:0000213|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [3] {ECO:0000313|Ensembl:ENSP00000411406}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [4] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; AL162425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; E9PC84; -.
DR   SwissPalm; E9PC84; -.
DR   jPOST; E9PC84; -.
DR   MaxQB; E9PC84; -.
DR   PeptideAtlas; E9PC84; -.
DR   PRIDE; E9PC84; -.
DR   Ensembl; ENST00000423613; ENSP00000411406; ENSG00000041982.
DR   UCSC; uc010mvf.5; human.
DR   EuPathDB; HostDB:ENSG00000041982.15; -.
DR   HGNC; HGNC:5318; TNC.
DR   OpenTargets; ENSG00000041982; -.
DR   GeneTree; ENSGT00940000155188; -.
DR   OrthoDB; 18592at2759; -.
DR   ChiTaRS; TNC; human.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000041982; Expressed in 213 organ(s), highest expression level in layer of synovial tissue.
DR   ExpressionAtlas; E9PC84; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR   CDD; cd00063; FN3; 12.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 2.60.40.10; -; 12.
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; 6.
DR   Pfam; PF07974; EGF_2; 4.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 12.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 12.
DR   SUPFAM; SSF49265; SSF49265; 9.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 12.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Proteomics identification {ECO:0000213|EPD:E9PC84,
KW   ECO:0000213|MaxQB:E9PC84, ECO:0000213|PeptideAtlas:E9PC84};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1928       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003244016.
FT   DOMAIN      186    217       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      280    311       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      373    404       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      466    497       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      559    590       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      625    715       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      716    804       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      805    894       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      895    990       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      991   1075       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1076   1165       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1167   1256       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1258   1350       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1351   1438       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1439   1528       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1529   1615       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1616   1704       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN     1702   1917       Fibrinogen C-terminal.
FT                                {ECO:0000259|PROSITE:PS51406}.
FT   COILED      119    139       {ECO:0000256|SAM:Coils}.
FT   DISULFID    190    200       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    207    216       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    284    294       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    301    310       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    377    387       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    394    403       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    470    480       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    487    496       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    563    573       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    580    589       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   1928 AA;  210854 MW;  141AD591043D1CB4 CRC64;
     MGAMTQLLAG VFLAFLALAT EGGVLKKVIR HKRQSGVNAT LPEENQPVVF NHVYNIKLPV
     GSQCSVDLES ASGEKDLAPP SEPSESFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK
     ELLSRLEELE NLVSSLREQC TAGAGCCLQP ATGRLDTRPF CSGRGNFSTE GCGCVCEPGW
     KGPNCSEPEC PGNCHLRGRC IDGQCICDDG FTGEDCSQLA CPSDCNDQGK CVNGVCICFE
     GYAGADCSRE ICPVPCSEEH GTCVDGLCVC HDGFAGDDCN KPLCLNNCYN RGRCVENECV
     CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGKPTCPHAC HTQGRCEEGQ
     CVCDEGFAGV DCSEKRCPAD CHNRGRCVDG RCECDDGFTG ADCGELKCPN GCSGHGRCVN
     GQCVCDEGYT GEDCSQLRCP NDCHSRGRCV EGKCVCEQGF KGYDCSDMSC PNDCHQHGRC
     VNGMCVCDDG YTGEDCRDRQ CPRDCSNRGL CVDGQCVCED GFTGPDCAEL SCPNDCHGQG
     RCVNGQCVCH EGFMGKDCKE QRCPSDCHGQ GRCVDGQCIC HEGFTGLDCG QHSCPSDCNN
     LGQCVSGRCI CNEGYSGEDC SEVSPPKDLV VTEVTEETVN LAWDNEMRVT EYLVVYTPTH
     EGGLEMQFRV PGDQTSTIIQ ELEPGVEYFI RVFAILENKK SIPVSARVAT YLPAPEGLKF
     KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYRQ TGLAPGQEYE
     ISLHIVKNNT RGPGLKRVTT TRLDAPSQIE VKDVTDTTAL ITWFKPLAEI DGIELTYGIK
     DVPGDRTTID LTEDENQYSI GNLKPDTEYE VSLISRRGDM SSNPAKETFT TGLDAPRNLR
     RVSQTDNSIT LEWRNGKAAI DSYRIKYAPI SGGDHAEVDV PKSQQATTKT TLTGLRPGTE
     YGIGVSAVKE DKESNPATIN AATELDTPKD LQVSETAETS LTLLWKTPLA KFDRYRLNYS
     LPTGQWVGVQ LPRNTTSYVL RGLEPGQEYN VLLTAEKGRH KSKPARVKAS TEQAPELENL
     TVTEVGWDGL RLNWTAADQA YEHFIIQVQE ANKVEAARNL TVPGSLRAVD IPGLKAATPY
     TVSIYGVIQG YRTPVLSAEA STGETPNLGE VVVAEVGWDA LKLNWTAPEG AYEYFFIQVQ
     EADTVEAAQN LTVPGGLRST DLPGLKAATH YTITIRGVTQ DFSTTPLSVE VLTEEVPDMG
     NLTVTEVSWD ALRLNWTTPD GTYDQFTIQV QEADQVEEAH NLTVPGSLRS MEIPGLRAGT
     PYTVTLHGEV RGHSTRPLAV EVVTEDLPQL GDLAVSEVGW DGLRLNWTAA DNAYEHFVIQ
     VQEVNKVEAA QNLTLPGSLR AVDIPGLEAA TPYRVSIYGV IRGYRTPVLS AEASTAMGSP
     KEVIFSDITE NSATVSWRAP TAQVESFRIT YVPITGGTPS MVTVDGTKTQ TRLVKLIPGV
     EYLVSIIAMK GFEESEPVSG SFTTALDGPS GLVTANITDS EALARWQPAI ATVDSYVISY
     TGEKVPEITR TVSGNTVEYA LTDLEPATEY TLRIFAEKGP QKSSTITAKF TTDLDSPRDL
     TATEVQSETA LLTWRPPRAS VTGYLLVYES VDGTVKEVIV GPDTTSYSLA DLSPSTHYTA
     KIQALNGPLR SNMIQTIFTT IGLLYPFPKD CSQAMLNGDT TSGLYTIYLN GDKAEALEVF
     CDMTSDGGGW IVFLRRKNGR ENFYQNWKAY AAGFGDRREE FWLGLDNLNK ITAQGQYELR
     VDLRDHGETA FAVYDKFSVG DAKTRYKLKV EGYSGTAGDS MAYHNGRSFS TFDKDTDSAI
     TNCALSYKGA FWYRNCHRVN LMGRYGDNNH SQGVNWFHWK GHEHSIQFAE MKLRPSNFRN
     LEGRRKRA
//