ID A0A3Q2IDN1_HORSE Unreviewed; 2019 AA.
AC A0A3Q2IDN1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=Tenascin {ECO:0000256|ARBA:ARBA00069274};
DE AltName: Full=Hexabrachion {ECO:0000256|ARBA:ARBA00079678};
DE AltName: Full=Tenascin-C {ECO:0000256|ARBA:ARBA00080298};
GN Name=TNC {ECO:0000313|Ensembl:ENSECAP00000046527.3,
GN ECO:0000313|VGNC:VGNC:24356};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000046527.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000046527.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000046527.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000046527.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000046527.3};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSECAP00000046527.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000046527.3};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed in
CC the triple coiled-coil region and may be stabilized by disulfide rings
CC at both ends. Two of such half-hexabrachions may be disulfide linked
CC within the central globule. Interacts with CSPG4. Interacts (via the
CC 3rd fibronectin type-III domain) with integrin ITGA9:ITGB1.
CC {ECO:0000256|ARBA:ARBA00063616}.
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 Ensembl; ENSECAT00000052336.3; ENSECAP00000046527.3; ENSECAG00000017433.4.
DR VGNC; VGNC:24356; TNC.
DR GeneTree; ENSGT00940000155188; -.
DR Proteomes; UP000002281; Chromosome 25.
DR Bgee; ENSECAG00000017433; Expressed in synovial membrane of synovial joint and 18 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2IDN1; baseline.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0009611; P:response to wounding; IEA:UniProtKB-ARBA.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00063; FN3; 12.
DR CDD; cd00087; FReD; 1.
DR FunFam; 2.60.40.10:FF:000099; Fibronectin 1; 1.
DR FunFam; 2.10.25.10:FF:000001; Tenascin C; 14.
DR FunFam; 2.20.25.10:FF:000006; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000162; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000201; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000207; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000293; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000346; Tenascin C; 2.
DR FunFam; 2.60.40.10:FF:000398; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000529; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000611; Tenascin C; 1.
DR FunFam; 2.60.40.10:FF:000939; Tenascin C; 1.
DR FunFam; 3.90.215.10:FF:000001; Tenascin isoform 1; 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; 13.
DR Gene3D; 2.10.25.10; Laminin; 14.
DR InterPro; IPR050991; ECM_Regulatory_Proteins.
DR InterPro; IPR000742; EGF.
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; PF25024; EGF_TEN; 1.
DR Pfam; PF23106; EGF_Teneurin; 6.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 13.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 13.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 10.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 10.
PE 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q2IDN1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2019
FT /note="Tenascin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040157727"
FT DOMAIN 280..311
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 373..404
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 625..715
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 805..894
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 895..987
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 988..1077
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1167..1259
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1260..1350
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1440..1529
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1530..1619
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1620..1706
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1707..1795
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1793..2008
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DISULFID 284..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 301..310
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 377..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 394..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2019 AA; 220851 MW; C9CECFE58AC4C27A CRC64;
MGAMTRLLAG IFLALLALST EGGVLKKVIR HKRESGVNIS LPEENQPVVF NHVYNIKLPV
GSQCSVDLES GSGAKDLAPP LEPSESFQEH TVDGNNQIVF THRINIPRRA CGCAAAPDVK
ELLSRLEELE NLVSSLREQC TTGAGCCLQP AEGRLDTRPF CSGRGNFSAE GCGCVCEPGW
KGPNCSEPEC PGNCHLRGQC LDGQCLCDEG FTGEDCSQLA CPSDCNDQGK CVNGVCICFE
GYAGADCSQE VCPVPCSAEH GRCVDGQCVC QDGFAGEDCN EPLCLNNCNN RGRCVENECV
CDAGFTGEDC SELICPKDCF DRGRCINGTC YCEEGFTGED CGQLTCPNAC RGQGRCEEGQ
CVCDEGFAGV DCGEKRCPAD CHNHGRCVDG QCECDDGYTG ADCGELQCPN GCSGHGRCVN
GQCVCDEGYT GEDCAQLRCP SDCNSRGRCV QGKCVCEQGF QGYDCSEMSC PHDCHQHGRC
VNGMCICDDG YTGEDCRELR CPRDCSHRGR CVDGRCVCED GFTGPDCAEL SCPSDCHGQG
RCVNGQCVCH EGFTGKDCKE RRCPSDCHGR GRCVDGQCIC QEGFTAPDCG QRSCPNDCSN
WGQCVAGRCI CNEGYTGEDC SEVSPPKDLI VTEVTEETVN LAWDNEMRVT EYLVTYTPTH
EGGLEMQFRV PGNQTSTIIQ ELEPGVEYFI RVFAILENKK SIPVSARVAT YLPAPEGLKF
KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETTYRQ TGLAPGQEYE
ISLHIVKNNT RGPGLKRVTT TRLDAPSQIE VKDVTDTTAL ITWFKPLAEI DGIELTYGVK
DVPGDRTTID LTQDENQYSI GNLKPDTEYE VSLISRRGDM SSNPSKETFT TGLDAPRNLR
RVSQTDNSIT LEWRNGKAAI DNYRIKYAPI SGGDHAEVEV PRSPQATTKT TLTGLRPGTE
YGIGVSAVKG DKESDPATIN AATDLDAPKD LRVSETADTS LTLVWRTPSA KFDHYRLNYS
LPSGQPVEVR LPKATTSYVL RGLEPGQEYP ILLTSEKGRH KSKPARVTAS TDHTPELENL
TVTKVGWDGL KLNWTTADQA YEHFVIQVQE VNRVEAAQNL TVPGSLRAVE VPGLKAATPY
RVTIYGVIRG HRTPVLSAEA STGESPNLGE VTVSKLGWDA LKLNWTAPEG AYEQFLIQVQ
ETDRVEAAQN LTVPGGLRSV DLPGLKASTR YSITIRGVTR DFSTAPLSVE VLTEEVPDLG
NLTVTEVSWD ALRLDWTTPD EIYEQFVIEV QEADQAKEAH SLTVPGSLRS VEIPDLRAGT
PYTVTLHGEV RGRRTRPLAV EVMTEELPEL GDLVVTEAGW DGLKLNWTAA DQAYELFVIQ
VQEVNRVEAA QNLTVPGSLR AVEVPGLKAA TPYRVTIYGV IRGYKTPVLS AEASTAGEPE
IGNLNVSAIT PESFNLSWTA TDGAFETFTI EIIDSNRFLE TMEYNVSGAE RTAHISGLRP
SNDFIIYLSG LAPSIRTKTI SATATTAMGS PKEIIFSDIT ENSATVSWMA PTAQVESFRI
TYVPIAGGTP SVVTVDGTKT QTRLVKLLPG AEYLVSIIAM KGFEESEPVS GSFTTALDGP
SGLVTANITD SEALAIWQPA IAPVDSYVIS YTGERVPEIT RTVSGNTVEY ALTSLEPATE
YTLRIFAEQG PQKSSAITTK FTTDLDSPRD LTATEVQSET ALLTWRPPRA SVTGYLLVYE
SVDGTVKEVI LGPDTTSYSL AELSPSTHYT VKIQALNGPL RSKLVQTFFT TVGLLYPFPR
DCSQAMLNGD TTSGLYTIYL NGDKAQPLEV FCDMTSDGGG WIVFLRRKNG REDFYRNWKA
YATGFGDRRE EFWLGLDNLN KITSQGQYEL RVDLRDHGKS AYAVYDRFSV GDAKTRYKLK
VEGYSGTAGD SMAYHNGRSF STYDKDTDSA ITNCALSYKG AFWYKNCHRV NLMGRYGDNN
HSQGVNWFHW KGHEYSIQFA EMKLRPSNFR NLEGRRKRA
//
