ID A0A452CE01_BALAS Unreviewed; 1655 AA.
AC A0A452CE01;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Tenascin isoform X3 {ECO:0000313|RefSeq:XP_028021227.1};
GN Name=TNC {ECO:0000313|RefSeq:XP_028021227.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028021227.1};
RN [1] {ECO:0000313|RefSeq:XP_028021227.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028021227.1};
RG RefSeq;
RL Submitted (JAN-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_007178199.1; XM_007178137.1.
DR RefSeq; XP_028021227.1; XM_028165426.1.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 9.
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; 9.
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; 5.
DR Pfam; PF18720; EGF_Tenascin; 6.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF00041; fn3; 9.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00060; FN3; 9.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 6.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 8.
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:UP000261681};
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..1655
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019377192"
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..1076
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1077..1165
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1166..1254
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1255..1342
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1343..1431
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1429..1644
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
SQ SEQUENCE 1655 AA; 182225 MW; 424935AB59D36A12 CRC64;
MGVVTRLLAG IFLALLALPA EGGVLKKVIR HKRQSGLNVT LPEENQPVVF NHVYNIKLPV
GSQCSVDLES ASGEKDLVPL SEPRESFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK
ELLSRLEELE NLVSSLREQC TLGAGCCFQP AEGRLDTKPF CSGRGNFSTE GCGCVCEPGW
KGPNCSEPEC PGNCHLRGQC LDGQCVCDKG FMGDDCGQLV CPSDCNDQGK CMNGTCVCFE
GYSGVDCGQE PCPVPCSEEH GRCVDGRCVC QDGFAGEDCN EPLCLHNCHG RGRCVENECV
CDEGFTGDDC GELICPNDCF DRGRCVNGTC YCDEGFVGED CGQLACPHAC HGRGRCDEGQ
CVCDEGFAGA DCSEKRCPSD CHDRGRCLDG HCECDDGFTG ADCGELRCPR DCSGHGRCVN
GQCVCDEGRT GEDCGQLRCP NDCHGRGRCV QGRCKCELGF QGYDCGEMSC PHDCHQHGRC
VNGMCVCDDA YMGEDCRELR CPRDCSQRGR CVDGRCVCED GFTGPDCADL SCPGDCHGRG
RCVDGQCVCH EGFTGKDCGQ RRCPDDCHGQ GRCVDGQCVC HEGFTGLDCG QRSCPNDCSN
WGQCVSGRCI CNEGYTGEDC SQVSPPKDLI VTEVTEETIN LAWENEMRVT EYLIVYTPTH
EDGLEMQFRV PGDQTSTTIQ ELEPGVEYLI RVFAILENKK SIPVSARVAT YLPTPEGLKF
KSIRETSVEV EWDPLDIAFE TWEVIFRNMN KEDEGEITKS LRRPETTYQQ TGLAPGQEYE
ISLHIVKNNT RGPGLKRVTT TRLDAPSQIE VKDVTDTTAL ITWSKPLAEI DSIELTYGIK
DVPGDRTSID LTHEENQYSI GSLKPDTDYE VSLISRRADM SSIPARETFT TGLDAPRNLR
RISQTENSIT LEWRNVKAAA DSYRIKYAPI SGGDHAEVEV PRSQQTTTKT TLTGLRPGTE
YGIGVSAVKG DKESDPTTIN AATDLDAPKD LQVSEPTETS VTLRWQMPLA KFDRYRLNYS
LPSGQPVEVQ LPRGTTSYIL KGLEPGQEYT ILLTAEKGRH KSKPARVQAT TEAEPEVDNL
LVSDATPDGF RLSWTADEGV FDSFVLKIRD TKKQSEPLEI ILLAPERTRD ITGLREATEY
EIELYGISSG RRSQPVSAIA TTAMGSPKEI VFSDITENSA TVSWKAPTTQ VESFRVTSVP
TAGGTPSVVT VDGTKTQTRL LRLLPGVEYL VSVIALKGFE ESEPVLGTFT TALDGPSGLV
TANITDSEAL AMWQPAIAPV DNYVISYTGE REPEITRTVS GNTVEYALTN LKPATEYTLR
IFAEKGPQKS SIITTKFMTD LDSPRDFTAT DVQSETAVLT WRPPRASVTG YLLVFESVDG
TIKEVVVDPD TTSYSLAELS PSTHYMAKIQ ALNGPLRSKI IKTTFTTTGV LYPFPRDCSQ
TMLNGDTTSG VYTIYLNNDK TQKQEVFCDM TSDGGGWIVF LRRKNGREDF YRNWKAYTAG
FGDLKEEFWL GLDTLNKITA QGQYELRVDL RDHGQSAYAV YDKFSVGDAR TRYRLKVEGY
SGTAGDSMAY HNGRSFSTFD KDTDSAITNC ALSYKGAFWY KNCHRVNLMG RYGDRSHSQG
VNWFHWKGHE YSIQFAEMKL RPSNFRNLEG RRKRA
//
