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Database: UniProt
Entry: A0A286XPV6_CAVPO
LinkDB: A0A286XPV6_CAVPO
Original site: A0A286XPV6_CAVPO 
ID   A0A286XPV6_CAVPO        Unreviewed;      2112 AA.
AC   A0A286XPV6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Tenascin C {ECO:0000313|Ensembl:ENSCPOP00000027305.1};
GN   Name=TNC {ECO:0000313|Ensembl:ENSCPOP00000027305.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000027305.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000027305.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000027305.1};
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}.
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DR   EMBL; AAKN02005294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012998381.1; XM_013142927.1.
DR   Ensembl; ENSCPOT00000041519.1; ENSCPOP00000027305.1; ENSCPOG00000003429.4.
DR   GeneID; 100725345; -.
DR   CTD; 3371; -.
DR   VEuPathDB; HostDB:ENSCPOG00000003429; -.
DR   GeneTree; ENSGT00940000155188; -.
DR   OrthoDB; 5489847at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000003429; Expressed in uterine cervix and 11 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 2.
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; 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; 5.
DR   Pfam; PF18720; EGF_Tenascin; 7.
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; 5.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 13.
PE   3: Inferred from homology;
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:UP000005447};
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..2112
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011706081"
FT   DOMAIN          625..715
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..1077
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1078..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..1799
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1800..1888
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1886..2101
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   REGION          936..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2112 AA;  232354 MW;  9835705B41C428E7 CRC64;
     MGAMIQLLLG IFLAFLVLPS EGGVLKKTIR HKRQSGLNVT FPEENQPVVF NHVYNIKLPV
     GSQCSVDLES ASGEKDLALP LEPSESIQEH TVNGENQIVF THRINIPRRA CGCAAAPDVR
     ELLSRLEELE LVVSSLREQC SMGTGCCLQS AEGRLDTRPF CSGRGNFSTE GCGCVCEPGW
     KGPNCSEPEC PGNCNLRGQC LEGQCICDEG FTGEDCSQLA CPSDCNDQGK CVDGVCICFE
     GYAGADCSQE VCPVPCSEEH GRCIDGRCVC QEGFAGDDCK EPLCLNNCYN RGRCVENECV
     CEEGFTGEDC SELVCPNDCF DRGRCLNGTC YCEEGFTGED CGTLTCPNDC HQQGRCEEGQ
     CVCDEGFAGA DCSEKRCPAD CHNRGRCLNG QCECDDGFTG ADCGELKCPN DCSGHGHCVN
     GQCVCDEGYT GDDCSQLRCP NDCHSRGRCI EGKCVCEPGF QGYDCSDMSC PNDCHQHGRC
     VNGMCVCDDN YIGEDCRDRR CPRDCSNRGR CVDGQCLCED GFTGLDCAEL SCPSDCHGQG
     RCVNGQCVCH EGFMGQDCKE RRCPGDCHGQ GRCEDGQCVC HEGFTGIDCG QRSCPNDCSN
     LGQCISGRCI CNAGYTGDDC SQVSPPKDLI VTEVTEETVN LAWDNEMRVT EYLVVYTPTH
     ANGLEMQFRV PGDQTSTIIR ELEPGVEYFI RVFAILENKK SIPVSARVAT YLPAPEGLKF
     KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYQQ TGLAPGQEYE
     ISLHIVKNNT RGPGLKRVTT TRLDAPSQME VKDVTDTTAL VTWFKPLAEI DGIELSYGLK
     DVPGDRTTID LTHDENQYSI GNLKPDTQYE VSLISRRGDM SSNPAKESFT TGLDAPRNLR
     RVSQTDSSIT LEWRNVKAAI DSYRIKYAPI SGGDHAEVDV PKSQQTTTKT TLTGLRPGTE
     YGIGVSAVKE DRESDPATIN AATEIDAPKD LQASETTENS LTLQWKTPLA KFDRYRLNYS
     LPTGQSMEEQ LPRDTTSHVL RGLEPGQEYT VLLTAEKGRH KSKPVRVKAT TEHVPELENL
     TVTEVGWDGL KLNWTAADQA YEHFVIQVQE ANKVEATHNL TVPGSMRAVD LPGLKAGTPY
     RVSIYGVIRG YRTPVLSAEA STGETPNLGE ITVTEVGWDA LKLNWTAPEG AYEHFLIQVQ
     EADTVTVVQN LTVPGGLRSV DLPGLKAATH YRVTIRGVAQ DFSTTPLSVE IWTEEVPSLG
     NLTVTDVSWD AFKLDWTTPD EIYDQFVIEV QEADQVERTH NLTVPGSLRS VKIPGLTAGT
     AYRITLHGEA RGRRTRPLAA EIFTEKLPQL GDLAVTEVGW DGLKLNWTAA DQTYEHFVIQ
     VQEANKVEAT HNLTVPGSMR AVDLPGLKAG TPYRVSIYGV IRGYRTPVLS AEASTAKEPE
     IGNLSVSDIT SESFNLSWTA THGIFETFTI EIIDSNRLLQ MVEYNISGAE RTAQISGLPP
     NTDFIIYLSG LAPSIRTKTI SATATTEAEP EVDNLLVSDA TPDGFRLSWT ADEGMFDSFV
     LKIRDSKKQS EPQEIILPSP ERTRDITNLR EATEYEIELY GVRNGRRSQP VSAKATTAMG
     SPKELIFSDI TENAATVSWK APTAQVESFR VTYVPISGGM PSMVTVDGTT TEARLVQLIP
     GVEYLVSVIA MKGFEESEPV SGSLTTALDG PSSLVIANIT DSEALAMWQP AIALVDNYII
     SYTGERGLVP EITRTVSGNT VEYALTDLEP ATEYTLRIFA EKGPQKSSTM TTRFTTDLDA
     PRDLTASEVQ SETALLTWQP PRASVTGYLL VYESLDGTLK EVILGPDTTS YSLIDLSPST
     HYTARIQALR GPLRSKLIPT VFTTIGLLYP FPKDCSQAML NGDTTSGLYT IYLNNNKTQA
     LEVFCDMSSD GGGWIVFLRR KNGREDFYRN WKAYAAGFGD RNEEFWLGLD NLSKITAQGQ
     YELRVDLQDH GETAYAVYDR FSVGDAKTRY KLKVEGYSGT AGDSMAYHNG RSFSTYDKDT
     DSAITNCALS YKGAFWYKNC HRVNLMGRYG DNNHSQGVNW FHWKGHEYSI QFAEMKLRPS
     NFRNLESRRK RA
//
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