ID Q6RCS8_PIG Unreviewed; 293 AA.
AC Q6RCS8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Tissue factor {ECO:0000256|ARBA:ARBA00018722, ECO:0000256|PIRNR:PIRNR002498};
DE Short=TF {ECO:0000256|PIRNR:PIRNR002498};
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|EMBL:AAR89391.1};
RN [1] {ECO:0000313|EMBL:AAR89391.1}
RP NUCLEOTIDE SEQUENCE.
RA Ghanekar A., Grant D.R., Levy G.A.;
RT "Porcine tissue factor.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Initiates blood coagulation by forming a complex with
CC circulating factor VII or VIIa. The [TF:VIIa] complex activates factors
CC IX or X by specific limited proteolysis. TF plays a role in normal
CC hemostasis by initiating the cell-surface assembly and propagation of
CC the coagulation protease cascade. {ECO:0000256|ARBA:ARBA00002201,
CC ECO:0000256|PIRNR:PIRNR002498}.
CC -!- SUBUNIT: Interacts with HSPE; the interaction, inhibited by heparin,
CC promotes the generation of activated factor X and activates coagulation
CC in the presence of activated factor VII.
CC {ECO:0000256|ARBA:ARBA00011184}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the tissue factor family.
CC {ECO:0000256|ARBA:ARBA00009197, ECO:0000256|PIRNR:PIRNR002498}.
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DR EMBL; AY504424; AAR89391.1; -; mRNA.
DR RefSeq; NP_998950.1; NM_213785.1.
DR AlphaFoldDB; Q6RCS8; -.
DR ChEMBL; CHEMBL2450; -.
DR GeneID; 396677; -.
DR KEGG; ssc:396677; -.
DR CTD; 2152; -.
DR OrthoDB; 5321079at2759; -.
DR Genevisible; Q6RCS8; SS.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0002541; P:activation of plasma proteins involved in acute inflammatory response; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR InterPro; IPR001187; Tissue_factor.
DR InterPro; IPR030472; Tissue_Factor_CS.
DR PANTHER; PTHR20859; INTERFERON/INTERLEUKIN RECEPTOR; 1.
DR PANTHER; PTHR20859:SF22; TISSUE FACTOR; 1.
DR Pfam; PF09294; Interfer-bind; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR PIRSF; PIRSF002498; Tissue_factor_3; 1.
DR PRINTS; PR00346; TISSUEFACTOR.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS00621; TISSUE_FACTOR; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084,
KW ECO:0000256|PIRNR:PIRNR002498};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR002498-1};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 249..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..114
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF01108"
FT DOMAIN 135..241
FT /note="Interferon/interleukin receptor"
FT /evidence="ECO:0000259|Pfam:PF09294"
FT LIPID 274
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002498-2"
FT DISULFID 81..89
FT /evidence="ECO:0000256|PIRSR:PIRSR002498-1"
FT DISULFID 215..238
FT /evidence="ECO:0000256|PIRSR:PIRSR002498-1"
SQ SEQUENCE 293 AA; 32664 MW; EEB4C23033092696 CRC64;
MATPTGPPVS CPKAAVARAL LLGWVLVQVA GATGTTDVIV AYNLTWKSTN FKTILEWEPK
PINYVYTVQI SPRLGDWKNK CFHTTDTECD VTDEIMRNVK ETYVARVLSY PADTVLTAQE
PPFTNSPPFT PYLDTNLGQP VIQSFEQVGT KLNVTVEAAR TLVRVNGTFL RLRDVFGKDL
NYTLYYWRAS STGKKKATTN TNEFLIDVDK GENYCFSVQA VIPSRRVNQK SPESRIECTS
QEKAVSRELF LIVGAVVFAV IVFVLVPPVS LYKCRKERAG PNWKGRTPPS NVA
//
