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Database: UniProt
Entry: A0A452FG37_CAPHI
LinkDB: A0A452FG37_CAPHI
Original site: A0A452FG37_CAPHI 
ID   A0A452FG37_CAPHI        Unreviewed;      1695 AA.
AC   A0A452FG37;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Tenascin C {ECO:0000313|Ensembl:ENSCHIP00000023328.1};
GN   Name=TNC {ECO:0000313|Ensembl:ENSCHIP00000023328.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000023328.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000023328.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000023328.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   EMBL; LWLT01000007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; A0A452FG37; -.
DR   Ensembl; ENSCHIT00000031188.1; ENSCHIP00000023328.1; ENSCHIG00000020744.1.
DR   GeneTree; ENSGT00940000155188; -.
DR   Proteomes; UP000291000; Chromosome 8.
DR   Bgee; ENSCHIG00000020744; Expressed in spleen and 16 other cell types or tissues.
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; 6.
DR   Pfam; PF18720; EGF_Tenascin; 7.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 8.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 8.
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; 5.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 7.
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:UP000291000};
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..1695
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019259082"
FT   DOMAIN          672..762
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          763..852
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          853..948
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1035..1125
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1126..1216
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1293..1381
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1383..1471
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1469..1684
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
SQ   SEQUENCE   1695 AA;  186520 MW;  D659B4FBBCBF45D4 CRC64;
     MGVMTQLWAG LFLALLALPA EGGVLKKVIR HKRQSGVNVT LPEENQPVVF NHVYNIKLPV
     GSQCSVDLES ASGEKDLAPP SEPQESFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK
     ELLSRLEELE NLVSSLREQC TSGAGCCLQS AEGRVDTRPF CSGRGNFSTE GCGCVCEPGW
     KGPNCSEPEC PGNCHLRGQC LDGQCVCDEG FTGEDCGLLA CPSDCNDQGK CVDGACVCFE
     GYSGLDCSQE TCPVPCSEEH GRCVDGRCVC QEGFAGEDCR EPLCLHNCHG RGRCVENECV
     CDEGFTGEDC GELVCPNDCF DRGRCLNGTC SCDEGFTGED CGQLACPHAC HGRGRCDEGQ
     CVCDEGFAGP DCSERRCPSD CHERGRCVDG RCECNDGFTG ADCGELRCPR DCSGHGHCVN
     GQCVCDEGHT GEDCAQRRCP SDCHGRGRCV DGRCECQPGF QGDDCGEMSC PHDCHQHGRC
     VNGMCVCDDA YTGEDCRELR CPQDCSQRGR CVDGRCVCED GFTGPDCADL ACPGDCHGRG
     RCVDGQCVCL EGFTGPDCAQ RRCPGDCHGQ GRCVDGQCVC HEGFTGPDCA QRSCPNDCSN
     WGQCVSGRCI CNEGYTGEDC SQDLCVTLNT HTHVRTTSYL GVRGSERFWN CPKDTQLIDH
     TMKRLPPFYL PTPEGLKFKS IKETSVEVEW DPLDIAFETW EVIFRNMNKD DEGEITKSLR
     RPETTYRQTG LAPGQEYEIS LHIVKNNTRG PGLKRVTTTR LDAPSQIEVK DVTDTTALIT
     WSKPLAEIDS IELTYGVKDV PGDRTSIDLT HEENQYSIGN LKPDTEYEVA LISRRVDMSS
     NPAKETFTTG LDAPRNLRRI SQTDNSITLE WRNVKAAANS YRIKYAPISG GDHAEVEVPR
     SRQTTTRTTL TGLRPGTEYG IGVSAVKGDK ESDPATINAA TELDTPKDLR VSEPTETSLT
     LLWRTPVAKF DRYRLNYSLP SGQPVEVQLP RDTTSYVLRG LEPGQEYTVL LTAEKGRHKS
     KPARLQASTG EALPLLENLT ISDINPYGFT VSWMASENAF DSFLVTVVDS GKLLDPQEFT
     LSGTQRKLEL RGLITGIGYE VMVSGFTQGH QTKPLRAEII TEAEPEVDNL LVSDATPDGF
     RLSWTADEGV FDSFVLKIRD TKKQSEPLEI TLLAPERTRD ITGLREATEY EIELYGVSSG
     RRSQPVTAIA TTAMGSPKEI IFSDITENAA TVSWTAPTTQ VESFRITYVP IAGGRALGVQ
     ELDRQQSSCG LMSYPMADYL SNTSLSFLAA LDGPSSLVTA NITDSEALAM WQPAIAPVDN
     YVISYTGERV PEITRMVSGN TVEYALTNLE PATEYTLRIF AEKGPHLLTY LILNVFSSPD
     LDSPRDFTAT EVQSESALLT WRPPRASVTG YLLVYESVDG TIKEVVVDPD TTSYSLTDLS
     PSTYYTARIQ ALNGTLRSKT VKTIFTTTGV LYRFPRDCSQ AMLNGDTTSG VYTIYLNNDK
     TQKQEVFCDM TSDGGGWIVF LRRKNGREDF YRNWKAYAAG FGDLKEEFWI GLDTLSKITA
     QGQYELRVDL RDHGQSAYAV YDKFSVGDAR TRYRLKVEGY SGTAGDSMAY HNGRSFSTFD
     KDTDSAITNC ALSYKGAFWY KNCHRVNLMG RYGDNSHSQG VNWFHWKGHE HSIQFAEMKL
     RPSNFRNLEG RRKRA
//
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