ID I3LDR6_PIG Unreviewed; 2126 AA.
AC I3LDR6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Tenascin C {ECO:0000313|Ensembl:ENSSSCP00000022200.4};
GN Name=TNC {ECO:0000313|Ensembl:ENSSSCP00000022200.4,
GN ECO:0000313|VGNC:VGNC:103192};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000022200.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000022200.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000022200.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000022200.4}
RP IDENTIFICATION.
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 PeptideAtlas; I3LDR6; -.
DR Ensembl; ENSSSCT00000032138.4; ENSSSCP00000022200.4; ENSSSCG00000005494.5.
DR VGNC; VGNC:103192; TNC.
DR GeneTree; ENSGT00940000155188; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000005494; Expressed in stomach and 39 other cell types or tissues.
DR ExpressionAtlas; I3LDR6; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
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; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 13.
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; 4.
DR Pfam; PF18720; EGF_Tenascin; 9.
DR Pfam; PF00147; Fibrinogen_C; 2.
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; 5.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50853; FN3; 12.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:I3LDR6};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 752..844
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 932..1021
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1022..1115
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1116..1202
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1203..1292
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1294..1383
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1385..1475
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1476..1565
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1567..1656
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1657..1746
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1747..1833
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1834..1922
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1920..2115
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 29..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2126 AA; 232653 MW; 9FCCB92F460B2164 CRC64;
MSGGEASHYR GRRLLYKPAK AGCTGHSLPT VTRSPAQAHI PPSSAQRQRG SGRPGAVSAH
TPVLVPWSCF AQGSSLSQLR KEEDFFKKTG NNWFGFYSPF PNPQFCLRVR HPRTQTPWEH
SAKPSSTMGV VTRLLVGTFL ALLALPAQGG VLKKVIRHKR QTGVNVTLPE ESQPVVFNHV
YNIKLPVGSQ CSVDLESASG DKDLAAPSEP SESVQEHTVD GENQIVFTHR INIPRRACGC
AAAPDVKELL SRLEELENLV SSLREQCTSG AGCCLQPAEG RLDTRPFCSG RGNFSTEGCG
CVCEPGWKGP NCSEPECPSN CHLRGQCVDG QCVCNEGFTG EDCSQLACPS DCNDQGKCVN
GVCVCFEGYS GVDCSRETCP VPCSEEHGRC VDGRCVCQEG FAGEDCNEPL CLHNCHGRGR
CVENECVCDE GFTGEDCGEL ICPKDCFDRG RCINGTCYCD EGFEGEDCGR LACPHGCRGR
GRCEEGQCVC DEGFAGADCS ERRCPSDCHN RGRCLDGRCE CDDGFEGEDC GELRCPGGCS
GHGRCVNGQC VCDEGRTGED CSQLRCPNDC HGRGRCVQGR CECEHGFQGY DCSEMSCPHD
CHQHGRCVNG MCVCDDGYTG EDCRELRCPG DCSQRGRCVD GRCVCEHGFA GPDCADLACP
SDCHGRGRCV NGQCVCHEGF TGKDCGQRRC PGDCHGQGRC VDGQCVCHEG FTGLDCGQRS
CPNDCSNWGQ CVSGRCICNE GYSGEDCSQV SPPKDLIVTE VTEETVNLAW DNEMRVTEYL
IVYTPTHEDG LEMQFRVPGD QTSTTIRELE PGVEYFIRVF AILENKKSIP VSARVATYLP
TPEGLKFKSI KETSVEVEWD PLDIAFETWE IIFRNMNKED EGEITKSLRR PETTYRQTGL
APGQEYEISL HIVKNNTRGP GLKRVTTTRL DAPSQIEAKD VTDTTALITW FKPLAEIDGI
ELTYGIKDVP GDRTTIDLTH EENQYSIGNL KPDTEYEVSL ISRRADMSSN PAKETFTTGL
DAPRNLRRIS QTDNSITLEW RNGKAAADTY RIKYAPISGG DHAEVEVPRS PQTTTKATLT
GLRPGTEYGI GVSAVKGDKE SDPATINAAT DLDPPKDFRV SDLKESSLTL LWRMPLAKFD
RYRLNYGLPS GQPVEVQLPR NATSYILRGL EPGQEYTILL TAEKGRHKSK PARVKASTDR
IPELENLTVT EAGWDGLKLN WTAADQAYEH FVIQVQEANG VEAAQNLTVP GGLRAVDVPG
LKAATPYRVT IYGVIQGYRT PVLSAEASTG ETPHLGEVTV SQVGWDALQL NWTAPEGAYE
QFLIQVQETD TAEAAQNLTV PGGLRSVDLP GLKAGTHYSI TIRGLTRDFS TVPLSVEVLT
EEVPDLGNLT VTEVSWDALR LDWTSPEGIY EQYVIEVQEA DQAKEAHSLT VPGSQRSMEI
PGLRAGTPYT ITLHGEVRGH RSPPQTVEVT TAELPQLGDL VVTEAGWDGL KLNWTAADQA
YEHFVIQVQE ANRVEAVQNL TVPGGLRAVD VSGLKAATPY RVTIYGVIRS YRTPGLSAEA
STEAEPEVDN LLVSDATPDG FRLSWTADEG VFDSFVLKIR DTKKQSEPLE ITLLASERTR
DITGLREATE YEIELYGISS GKRSQPVSAI ATTAMGSPKE ITFSDITENS ATVSWMVPTA
QVESFRITYV PITGGAPSVV TVDGTKTQTR LLRLLPGVEY LVSVIAVKGF EESEPVSGTL
TTALDGPSGL VTANITDSEA LAMWQPAIAP VDHYVISYTG DRVPEITRTV SGNTVEYALT
NLEPATEYTL RIFAEKGPQK SSTITTKFTT DLDSPRDLTA TEVQSETALL TWRPPRASVT
GYLLVYESVD GTLKEVVVGP ETTSYSLSGL SPSTHYTARI QALNGPLRSK MSQTVFTTIG
LLYPFPRDCS QAMLNGDTTS GLYTIYVNND KAQKLEVFCD MTSDGGGWIV SITEPDFFRT
HPALWLLKIT AQGQYELRVD LRDHGETAYA VYDRFSVGDA RTRYKLKVEG YSGTAGDSMA
YHNGRSFSTF DKDTDSAITN CALSYKGAFW YKNCHRVNLM GRYGDNSHSQ GVNWFHWKGH
EYSIQFAEMK LRPSNFRNLE GRRKRA
//
