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Database: UniProt
Entry: A0A2U4C9K5_TURTR
LinkDB: A0A2U4C9K5_TURTR
Original site: A0A2U4C9K5_TURTR 
ID   A0A2U4C9K5_TURTR        Unreviewed;      2110 AA.
AC   A0A2U4C9K5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Tenascin isoform X2 {ECO:0000313|RefSeq:XP_019802046.1};
GN   Name=TNC {ECO:0000313|RefSeq:XP_019802046.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019802046.1};
RN   [1] {ECO:0000313|RefSeq:XP_019802046.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019802046.1};
RG   RefSeq;
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}.
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DR   RefSeq; XP_019802046.1; XM_019946487.2.
DR   GeneID; 101319123; -.
DR   OrthoDB; 5489847at2759; -.
DR   Proteomes; UP000245320; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 13.
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; 14.
DR   Gene3D; 2.10.25.10; Laminin; 14.
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; 2.
DR   Pfam; PF18720; EGF_Tenascin; 9.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 14.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 14.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 11.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 13.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..2110
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015769603"
FT   DOMAIN          625..717
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          805..896
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          897..986
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          987..1075
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1076..1165
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..1348
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1349..1439
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          1531..1620
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1621..1710
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1711..1797
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1798..1886
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1884..2099
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
SQ   SEQUENCE   2110 AA;  231474 MW;  9BF3C05AF4575E33 CRC64;
     MGVVTRLLAG IFLALLALPA EGGVLKKVIR HKRQSGVNVT LPEENQPVVF NHVYNIKLPV
     GSQCSVDLES ASGEKDLVPL SEPRESFQEH TVDGENQIVF THRINIPRRA CGCAAAPDIK
     ELLSRLEELE NLVSSLREQC TLGAGCCFQP AEGHLDTKPF CSGRGNFSTE GCGCVCEPGW
     KGPNCSEPEC PGNCHLRGQC LDGQCVCDKG FTGEDCGQLA CPSDCNDQGK CMNGTCVCFE
     GYSGVDCSQE PCPVPCSEEH GRCVDGRCVC QDGFAGEDCN EPLCLHNCRG RGSCVENECV
     CDEGFTGEDC GELVCPNDCF DRGRCVNGTC YCDEGFAGED CGQLACPHAC HGRGRCDEGQ
     CVCDEGFAGA DCSEKRCPSD CHDRGRCLDG HCECDDGFTG VDCGELRCPR DCSGHGRCVN
     GQCVCNEGRT GEDCGQLRCP NDCHGRGRCV QGRCECELGF QGYDCSEMSC PHDCYQHGRC
     LNGMCVCDDA YMGEDCRELR CPQDCSQRGR CVDGRCVCED GFAGPDCADL SCPGDCHGRG
     RCVDGQCVCH EGFTGKDCGQ RRCPDDCHGQ GRCVDGQCVC HEGFTGLDCG QRSCPNDCSN
     WGQCISGRCI CNEGYTGEDC SQVSPPKDLI VTEVTEETIN LAWENEMRVT EYLIVYTPTH
     EDGLEMQFRV PGNQTSTTIQ ELEPGVEYLI RVFAVLENKK SIPVSARVAT YLPTPEGLKF
     KSIKETSVEV EWDPVDIAFE TWEVIFRNMN KEDEEEITKS LRRPETTYRQ TGLAPGQEYE
     ISLHIVKNNT RGPSLKRVTT TRLDAPSQIE VKDVTDTTAL ITWSKPLAEI DSIELTYGIK
     DVPGDRTSID LTHEENQYSI GNLKPDTEYE VSLISHRADM SSSPARETFT TGLDAPRNLR
     RISQTDNSIT LEWRNVKAAA DNYRIKYAPI SGGDHAEVEV PRRQQTTTKT TLTGLRPGTE
     YGIGVSAVKG DKESDPATIN AATDLDAPRD LRVSETTETS LTLLWQAPLA KCDRYRLNYS
     LPSGQPVEVQ LPRGTTSYVL KGLEPGQEYT ILLTAEKGRH KSKPARVQAS TDHAPEMENL
     TVTEAGWDGL KLNWTTADQA YEHFVIQVQE ANRVEAAQNL TVPGSLRAAD IQGLKAATPY
     RVTIYGVIRG HRTPMLSAEA STGEAPHLGE VTVSEVGWDA LKLHWTAPEG AYEQFLIQVQ
     ETDTEEAAQN LTVPGGLRSV DLPGLKADTH YRVTIRGVTR DFSTTPLSVE VLTEEVPDLG
     NLTVTEVSWD ALRLDWTSPD GIYEQFVIEI QAADQTQEAH SLTVPGSLCS AEIPGLRAGT
     PYTITLRGEV RGRSTQPLAV EVITAELPQL GHLAVTEAGW DGLKLNWTTA DQAYEHFVIQ
     VQEANRVEAA QNLTVPGSLR AADIQGLKAA TPYRVTIYGV IRGYRTPMLS AEASTAGEPE
     IGNLNVSDIT PESFNLSWTA TDGAFKTFTI EIIDSNRFLE TMEYNISGAE RTAHISGLRP
     NNDFIVYLSG LTPSIRTKTI SATATTEAEP EVDNLLVSDA TPDGFRLSWT ADEGVFDSFV
     LKIRDTKKQS EPLEITLLAP ERTRDITGLR EATEYEIELY GISSGRRSQP VSAIATTAMG
     SPKEIVFSDI TENSATVSWK APTTQVESFR VTSVPTAGGT PSVVTVAGTK TQTRLLRLLP
     GVEYLVSVTA LKGFEESTPV SGMLTTALDG PSGLVTANIT DSEALATWQP AIAPVDNYVI
     SYTGEREPEI TRKVSGNTVE YALTNLEPAT EYTLRIFAEK GPQKSSTITT KFMTDLDSPR
     DFTATEVQSE TAVLTWRPPR ASVTGYLLVY ESVDGTTKEV VVDPDTTSYS LAELSPSTHY
     MAKIQALNGP LRSKIIKTTF TTTGVLYPFP RDCSQAMLNG DTTSGVYTVY LNNNKTQKQE
     VFCDMTSDGG GWIVFLRRKN GREDFYRNWK AYTAGFGDLK EEFWLGLDTL NKITAQGQYE
     LRVDLRDHGQ SAYAVYDKFS VGDARTRYRL KVEGYSGTAG DSMAYHNGRS FSTFDKDTDS
     AITNCALSYK GAFWYKNCHR VNLMGRYGDN NHSQGVNWFH WKGHEYSIQF AEMKLRPSNF
     RNLEGRRKRA
//
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