ID F7A8C6_ORNAN Unreviewed; 2168 AA.
AC F7A8C6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Tenascin C {ECO:0000313|Ensembl:ENSOANP00000016817.3};
GN Name=TNC {ECO:0000313|Ensembl:ENSOANP00000016817.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000016817.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000016817.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000016817.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000016817.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000016817.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the tenascin family.
CC {ECO:0000256|ARBA:ARBA00008673}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 9258.ENSOANP00000016817; -.
DR Ensembl; ENSOANT00000016820.4; ENSOANP00000016817.3; ENSOANG00000010612.4.
DR eggNOG; KOG1225; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000155188; -.
DR HOGENOM; CLU_001162_1_1_1; -.
DR TreeFam; TF329915; -.
DR Proteomes; UP000002279; Chromosome 4.
DR Bgee; ENSOANG00000010612; Expressed in testis and 7 other cell types or tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0045545; F:syndecan binding; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00063; FN3; 14.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 15.
DR Gene3D; 2.10.25.10; Laminin; 13.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
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; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR PANTHER; PTHR46708:SF1; TENASCIN; 1.
DR Pfam; PF07974; EGF_2; 4.
DR Pfam; PF18720; EGF_Tenascin; 8.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 15.
DR Pfam; PF12661; hEGF; 1.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 15.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 12.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 14.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2168
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027573367"
FT DOMAIN 248..279
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 372..403
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 558..589
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 593..683
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 773..863
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 864..956
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 957..1044
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1045..1137
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1138..1226
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1227..1317
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1318..1409
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1410..1497
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1498..1588
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1589..1678
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1679..1768
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1769..1855
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1856..1944
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1942..2157
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DISULFID 252..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 269..278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 376..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 393..402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 562..572
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 579..588
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2168 AA; 237762 MW; 5780378D3128A844 CRC64;
MGALTRVLAC TLIVLLCCLA DGGLIKKIIR HKRQSGENIT MSEDSEPVVF NHIYNIKLPV
GSHCSVDLDA PSGDKNLVSE DEPGNHFQEH TMNQENQIVF THRINIPRRA CGCAAAPDIK
DLLSRLEELE GLVSSLRELC ATGAGCRPQP AEGRLDTTPF CNGRGNYSTE SCGCICELGW
KGPNCSEPDC VGNCNNRGQC INGQCICDDG FMGEDCSQPA CPNDCNDQGK CISGVCVCFD
GYTGPDCNEE VCPLPCSEHG RCVNGQCVCH EGFSGEDCQE PLCLNNCYNR GRCVENECVC
DEGFTGDDCS ELICPNDCYD RGRCINGTCF CEKGFTGEDC GQRMCPNDCN RHGRCEEGQC
VCDDGFTGDD CNERRCPGDC SDHGRCIHGQ CVCNEGYTGE DCSALRCLND CNNHGRCIAG
KCVCEPGFVG HDCGDMQCPG DCHQHGRCVN GMCVCDEGYM GEDCHDQRCP KDCHGRGRCA
DGKCVCDEGF AGEDCGELSC PNDCHQQGRC VNGQCVCHEG FEGKDCKDPR CPHDCHHQGH
CVHGQCVCHD GFQGVDCRER SCLNDCSHHG QCVDGHCVCN DGYMGEDCSE VSPPKDLIVT
EVTEQTVNLA WDNEMKVTEY LITYTPTHMD GLEMKFRVPG DQTSTTIREL EPGVEYFIRV
FAILENKQSI PVSARVATYL PAPEGLKFKS VKETSVEVEW DPLDIAFEKW EIIFRNMNKD
DGEEITRSLR RPETTYQQTG LAPGQEYEIS LHIVKNNTRG PGLKRVTTTR LDAPSQIEVK
DVTDTTALIT WFKPLAEIDT IELSYGTKGV PGDVTTIEFS SDENQYSIDN LKPDTEYEVS
LISRRGDMTP SNPAKETFTT GLDAPRNLKR VSQTDSSITL EWKNGKADID NYRIKFAPIA
GGDHAERDVL KSKQPTTRVT LTDLRPGTEY GIGVTAVKND KESNPATINA ATDLDAPKEL
QVSEHTETSL SLLWRRPLAK FDRYRLTYNS SSGKHHEMEL PGGTSSYVLR GLNPGIDYSI
NLVAEKGRHK SKAARVKGAT EKTSELRDLS VLEVSWEALQ VNWTAADGAY EEFVIQVQEP
DNPEEAKNVT VPGVLRSVDI IGLKAATPYK VTAYGVNQGY RTKPLSAEAS TVETPKLGDL
TVSEVSWEAL KVNWTAQGGA YEKFVIQVQE ADNLEETKNV TVPGVLRSVD MTGLKAGTPY
RITIYGLIRG FTTKPLSAES ITEQVPELGN LMVSELSWES LQVNWSAADG AFEHFVLAVQ
EAGSLGGSHH LTIPGGLRSV HVTGLQGGAS YRITLHGVTG GLNTVPLTAE VMTEEAPHLG
RLTVSDISWE ALKLNWTSDV PFENFVIQVQ EFHDPEETQN LTVPSGLTSL EVSGLKASTP
YRITLYGEIG GYTSEPLSAQ ATTEEAPELG EVTVSEVSWE ALQVNWTAAD GDYEEFVIQV
QEADNLEVQN LTVPGGLRSV DVTGLKAATL YKVTIFGLIQ GYRTNPLSAE ASTAKEPEVG
NLTISSITHE SFNLSWTAPD EAFETFTIEI IDSNRLLEPL EFNISGTLRT MHISGLFPQT
DFIAYLSGVA PGVHTQAISA AATTEAEPEV DNLLVSDAIP DGFRLSWTAD EGAFDNFVLK
IRDTKRQSDP LEITVLASER TRDITGLKEG TEYDIELYGI INGRRSQPVN AVATTAVGAP
REISFSDITD NSATVSWTPP RAQVQGYRIT YVPIRGGSPS VVTVDGTVTQ TPLVKLIPGV
EYLVSIISIK GFEESEPISG SLTTALDSPS GLVAANVTDS EALAMWQPAI ATVENYVISY
VGGNEPEVTR TVSGNTVEYA LSDLEPATDY TLRIFAEKGP LKSSILTTKF TTDLDSPRDL
IASEVQSEAA LLSWRPPRAS VTGYLLIYQS VDGTIKEVVV GPDTNTYSLT DLNPSTHYTA
KVQALNGDLK SKIIQTFFTT IGLLYPYPKD CSQTMLNGET TSGLYTIYLN GDKAQAIEVF
CDMTSDGGGW IVFLRRSNGR QDFYQNWRTY AAGFGNRRDE FWLGLDNLHK ITAQGQYELR
VDLQDRGDTA YAIYNKFSIG DSKSRYKLNV EGYSGTAGDS MTYHTGRSFS TYDKDTDSAI
TNCALSYKGA FWYKNCHRVN LMGRYGDNSH SQGVNWFHWK GHEHSIQFAE MKLRPSSFRN
LEGRRKRA
//
