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Tissue factor (TF) (Coagulation factor III) (Thromboplastin) (CD antigen CD142)

 TF_HUMAN                Reviewed;         295 AA.
P13726; D3DT47; Q6FHG2; Q86WH4;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
25-OCT-2017, entry version 196.
RecName: Full=Tissue factor;
Short=TF;
AltName: Full=Coagulation factor III;
AltName: Full=Thromboplastin;
AltName: CD_antigen=CD142;
Flags: Precursor;
Name=F3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2823875; DOI=10.1021/bi00391a004;
Scarpati E.M., Wen D., Broze G.J. Jr., Miletich J.P.,
Flandermeyer R.R., Siegel N.R., Sadler J.E.;
"Human tissue factor: cDNA sequence and chromosome localization of the
gene.";
Biochemistry 26:5234-5238(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3297348; DOI=10.1016/0092-8674(87)90669-6;
Morrissey J.H., Fakhrai H., Edgington T.S.;
"Molecular cloning of the cDNA for tissue factor, the cellular
receptor for the initiation of the coagulation protease cascade.";
Cell 50:129-135(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3037536; DOI=10.1073/pnas.84.15.5148;
Spicer E.K., Horton R., Bloem L., Bach R., Williams K.R., Guha A.,
Kraus J., Lin T.C., Nemerson Y., Konigsberg W.H.;
"Isolation of cDNA clones coding for human tissue factor: primary
structure of the protein and cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 84:5148-5152(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3424286; DOI=10.1016/0049-3848(87)90349-5;
Fisher K.L., Gorman C.M., Vehar G.A., O'Brien D.P., Lawn R.M.;
"Cloning and expression of human tissue factor cDNA.";
Thromb. Res. 48:89-99(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2719931; DOI=10.1021/bi00430a050;
Mackman N., Morrissey J.H., Fowler B., Edgington T.S.;
"Complete sequence of the human tissue factor gene, a highly regulated
cellular receptor that initiates the coagulation protease cascade.";
Biochemistry 28:1755-1762(1989).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=12652293; DOI=10.1038/nm841;
Bogdanov V.Y., Balasubramanian V., Hathcock J., Vele O., Lieb M.,
Nemerson Y.;
"Alternatively spliced human tissue factor: a circulating, soluble,
thrombogenic protein.";
Nat. Med. 9:458-462(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-36 AND VAL-145.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
DISULFIDE BONDS, AND PALMITOYLATION AT CYS-277.
PubMed=3166978; DOI=10.1021/bi00412a004;
Bach R., Konigsberg W.H., Nemerson Y.;
"Human tissue factor contains thioester-linked palmitate and stearate
on the cytoplasmic half-cystine.";
Biochemistry 27:4227-4231(1988).
[14]
ALTERNATIVE SPLICING, AND INDUCTION.
PubMed=19168442; DOI=10.1161/CIRCRESAHA.108.183905;
Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S.,
Poller W., Schultheiss H.P., Rauch U.;
"Cdc2-like kinases and DNA topoisomerase I regulate alternative
splicing of tissue factor in human endothelial cells.";
Circ. Res. 104:589-599(2009).
[15]
INTERACTION WITH HPSE.
PubMed=20634491; DOI=10.3324/haematol.2010.023713;
Nadir Y., Brenner B., Fux L., Shafat I., Attias J., Vlodavsky I.;
"Heparanase enhances the generation of activated factor X in the
presence of tissue factor and activated factor VII.";
Haematologica 95:1927-1934(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 33-243.
PubMed=8086403; DOI=10.1021/bi00202a003;
Muller Y.A., Ultsch M.H., Kelley R.F., de Vos A.M.;
"Structure of the extracellular domain of human tissue factor:
location of the factor VIIa binding site.";
Biochemistry 33:10864-10870(1994).
[18]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-243.
PubMed=8609606; DOI=10.1006/jmbi.1996.0073;
Muller Y.A., Ultsch M.H., de Vos A.M.;
"The crystal structure of the extracellular domain of human tissue
factor refined to 1.7-A resolution.";
J. Mol. Biol. 256:144-159(1996).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-251 IN COMPLEX WITH FVIIA.
PubMed=8598903; DOI=10.1038/380041a0;
Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A.,
Konigsberg W.H., Nemreson Y., Kirchhofer D.;
"The crystal structure of the complex of blood coagulation factor VIIa
with soluble tissue factor.";
Nature 380:41-46(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-242 IN COMPLEX WITH FVIIA.
PubMed=9925787; DOI=10.1006/jmbi.1998.2452;
Zhang E., St Charles R., Tulinsky A.;
"Structure of extracellular tissue factor complexed with factor VIIa
inhibited with a BPTI mutant.";
J. Mol. Biol. 285:2089-2104(1999).
-!- FUNCTION: Initiates blood coagulation by forming a complex with
circulating factor VII or VIIa. The [TF:VIIa] complex activates
factors IX or X by specific limited protolysis. TF plays a role in
normal hemostasis by initiating the cell-surface assembly and
propagation of the coagulation protease cascade.
{ECO:0000269|PubMed:12652293}.
-!- SUBUNIT: Interacts with HSPE; the interaction, inhibited by
heparin, promotes the generation of activated factor X and
activates coagulation in the presence of activated factor VII.
{ECO:0000269|PubMed:20634491, ECO:0000269|PubMed:8598903,
ECO:0000269|PubMed:9925787}.
-!- INTERACTION:
P55085:F2RL1; NbExp=2; IntAct=EBI-1040727, EBI-4303189;
P08709:F7; NbExp=7; IntAct=EBI-1040727, EBI-355972;
-!- SUBCELLULAR LOCATION: Isoform 1: Membrane
{ECO:0000269|PubMed:12652293}; Single-pass type I membrane protein
{ECO:0000269|PubMed:12652293}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:12652293}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms may exist.;
Name=1; Synonyms=flTF;
IsoId=P13726-1; Sequence=Displayed;
Name=2; Synonyms=asHTF;
IsoId=P13726-2; Sequence=VSP_041896, VSP_041897;
-!- TISSUE SPECIFICITY: Lung, placenta and pancreas.
{ECO:0000269|PubMed:12652293}.
-!- INDUCTION: TF expression is highly dependent upon cell type. TF
can also be induced by the inflammatory mediators interleukin 1
and TNF-alpha, as well as by endotoxin, to appear on monocytes and
vascular endothelial cells as a component of cellular immune
response. {ECO:0000269|PubMed:19168442}.
-!- SIMILARITY: Belongs to the tissue factor family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f3/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=TF";
-!- WEB RESOURCE: Name=Wikipedia; Note=Tissue factor entry;
URL="https://en.wikipedia.org/wiki/Tissue_factor";
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EMBL; M16553; AAA61151.1; -; mRNA.
EMBL; J02931; AAA61150.1; -; mRNA.
EMBL; M27436; AAA36734.1; -; mRNA.
EMBL; J02846; AAA61152.1; -; Genomic_DNA.
EMBL; BT019808; AAV38611.1; -; mRNA.
EMBL; CR541792; CAG46591.1; -; mRNA.
EMBL; AF487337; AAO61150.1; -; mRNA.
EMBL; AF540377; AAN01236.1; -; Genomic_DNA.
EMBL; AC093117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471097; EAW73044.1; -; Genomic_DNA.
EMBL; CH471097; EAW73045.1; -; Genomic_DNA.
EMBL; BC011029; AAH11029.1; -; mRNA.
CCDS; CCDS53345.1; -. [P13726-2]
CCDS; CCDS750.1; -. [P13726-1]
PIR; A43645; KFHU3.
RefSeq; NP_001171567.1; NM_001178096.1. [P13726-2]
RefSeq; NP_001984.1; NM_001993.4. [P13726-1]
UniGene; Hs.62192; -.
PDB; 1AHW; X-ray; 3.00 A; C/F=33-251.
PDB; 1BOY; X-ray; 2.20 A; A=33-251.
PDB; 1DAN; X-ray; 2.00 A; T=37-116, U=122-242.
PDB; 1FAK; X-ray; 2.10 A; T=37-242.
PDB; 1J9C; X-ray; 2.90 A; T=33-242.
PDB; 1JPS; X-ray; 1.85 A; T=33-251.
PDB; 1NL8; Model; -; T=33-242.
PDB; 1O5D; X-ray; 2.05 A; T=34-251.
PDB; 1TFH; X-ray; 2.40 A; A/B=33-251.
PDB; 1UJ3; X-ray; 2.10 A; C=38-242.
PDB; 1W0Y; X-ray; 2.50 A; T=33-242.
PDB; 1W2K; X-ray; 3.00 A; T=33-242.
PDB; 1WQV; X-ray; 2.50 A; T=33-250.
PDB; 1WSS; X-ray; 2.60 A; T=33-250.
PDB; 1WTG; X-ray; 2.20 A; T=33-250.
PDB; 1WUN; X-ray; 2.40 A; T=33-250.
PDB; 1WV7; X-ray; 2.70 A; T=33-250.
PDB; 1Z6J; X-ray; 2.00 A; T=33-243.
PDB; 2A2Q; X-ray; 1.80 A; T=38-242.
PDB; 2AEI; X-ray; 2.52 A; T=33-243.
PDB; 2AER; X-ray; 1.87 A; T=38-242.
PDB; 2B7D; X-ray; 2.24 A; T=34-251.
PDB; 2B8O; X-ray; 2.80 A; T=38-242.
PDB; 2C4F; X-ray; 1.72 A; T=38-112, U=123-242.
PDB; 2CEF; NMR; -; A=277-295.
PDB; 2CEH; NMR; -; A=277-295.
PDB; 2CEZ; NMR; -; A=277-295.
PDB; 2CFJ; NMR; -; A=277-295.
PDB; 2EC9; X-ray; 2.00 A; T=38-112, U=123-242.
PDB; 2F9B; X-ray; 2.54 A; T=34-251.
PDB; 2FIR; X-ray; 2.00 A; T=38-242.
PDB; 2FLB; X-ray; 1.95 A; T=34-251.
PDB; 2FLR; X-ray; 2.35 A; T=34-251.
PDB; 2HFT; X-ray; 1.69 A; A=33-243.
PDB; 2PUQ; X-ray; 2.05 A; T=38-241.
PDB; 2ZP0; X-ray; 2.70 A; T=33-250.
PDB; 2ZWL; X-ray; 2.20 A; T=33-250.
PDB; 2ZZU; X-ray; 2.50 A; T=33-250.
PDB; 3ELA; X-ray; 2.20 A; T=33-241.
PDB; 3TH2; X-ray; 1.72 A; T=38-242.
PDB; 3TH3; X-ray; 2.70 A; T=38-242.
PDB; 3TH4; X-ray; 1.80 A; T=38-242.
PDB; 4IBL; X-ray; 1.80 A; T=33-251.
PDB; 4M7L; X-ray; 3.40 A; T=37-245.
PDB; 4YLQ; X-ray; 1.40 A; T=33-251.
PDB; 4Z6A; X-ray; 2.25 A; T=36-242.
PDB; 4ZMA; X-ray; 2.30 A; T=33-251.
PDB; 5W06; X-ray; 2.60 A; T=37-245.
PDBsum; 1AHW; -.
PDBsum; 1BOY; -.
PDBsum; 1DAN; -.
PDBsum; 1FAK; -.
PDBsum; 1J9C; -.
PDBsum; 1JPS; -.
PDBsum; 1NL8; -.
PDBsum; 1O5D; -.
PDBsum; 1TFH; -.
PDBsum; 1UJ3; -.
PDBsum; 1W0Y; -.
PDBsum; 1W2K; -.
PDBsum; 1WQV; -.
PDBsum; 1WSS; -.
PDBsum; 1WTG; -.
PDBsum; 1WUN; -.
PDBsum; 1WV7; -.
PDBsum; 1Z6J; -.
PDBsum; 2A2Q; -.
PDBsum; 2AEI; -.
PDBsum; 2AER; -.
PDBsum; 2B7D; -.
PDBsum; 2B8O; -.
PDBsum; 2C4F; -.
PDBsum; 2CEF; -.
PDBsum; 2CEH; -.
PDBsum; 2CEZ; -.
PDBsum; 2CFJ; -.
PDBsum; 2EC9; -.
PDBsum; 2F9B; -.
PDBsum; 2FIR; -.
PDBsum; 2FLB; -.
PDBsum; 2FLR; -.
PDBsum; 2HFT; -.
PDBsum; 2PUQ; -.
PDBsum; 2ZP0; -.
PDBsum; 2ZWL; -.
PDBsum; 2ZZU; -.
PDBsum; 3ELA; -.
PDBsum; 3TH2; -.
PDBsum; 3TH3; -.
PDBsum; 3TH4; -.
PDBsum; 4IBL; -.
PDBsum; 4M7L; -.
PDBsum; 4YLQ; -.
PDBsum; 4Z6A; -.
PDBsum; 4ZMA; -.
PDBsum; 5W06; -.
ProteinModelPortal; P13726; -.
SMR; P13726; -.
BioGrid; 108451; 8.
CORUM; P13726; -.
DIP; DIP-6136N; -.
IntAct; P13726; 3.
STRING; 9606.ENSP00000334145; -.
BindingDB; P13726; -.
ChEMBL; CHEMBL4081; -.
DrugBank; DB07207; 2-(4-HYDROXY-5-PHENYL-1H-PYRAZOL-3-YL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE.
DrugBank; DB13150; Coagulation factor VII human.
DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
iPTMnet; P13726; -.
PhosphoSitePlus; P13726; -.
SwissPalm; P13726; -.
BioMuta; F3; -.
DMDM; 135666; -.
EPD; P13726; -.
MaxQB; P13726; -.
PaxDb; P13726; -.
PeptideAtlas; P13726; -.
PRIDE; P13726; -.
DNASU; 2152; -.
Ensembl; ENST00000334047; ENSP00000334145; ENSG00000117525. [P13726-1]
Ensembl; ENST00000370207; ENSP00000359226; ENSG00000117525. [P13726-2]
GeneID; 2152; -.
KEGG; hsa:2152; -.
UCSC; uc001dqr.4; human. [P13726-1]
CTD; 2152; -.
DisGeNET; 2152; -.
EuPathDB; HostDB:ENSG00000117525.13; -.
GeneCards; F3; -.
HGNC; HGNC:3541; F3.
HPA; CAB009438; -.
HPA; HPA049292; -.
HPA; HPA069132; -.
MIM; 134390; gene.
neXtProt; NX_P13726; -.
OpenTargets; ENSG00000117525; -.
PharmGKB; PA158; -.
eggNOG; ENOG410IYA1; Eukaryota.
eggNOG; ENOG4111MW4; LUCA.
GeneTree; ENSGT00390000012668; -.
HOGENOM; HOG000043076; -.
HOVERGEN; HBG005051; -.
InParanoid; P13726; -.
KO; K03901; -.
OMA; NTNEFLI; -.
OrthoDB; EOG091G0MKF; -.
PhylomeDB; P13726; -.
TreeFam; TF352627; -.
Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation.
SIGNOR; P13726; -.
ChiTaRS; F3; human.
EvolutionaryTrace; P13726; -.
GeneWiki; Tissue_factor; -.
GenomeRNAi; 2152; -.
PRO; PR:P13726; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117525; -.
CleanEx; HS_F3; -.
Genevisible; P13726; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IC:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:1905286; C:serine-type peptidase complex; IPI:BHF-UCL.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0002543; P:activation of blood coagulation via clotting cascade; IC:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
GO; GO:0002541; P:activation of plasma proteins involved in acute inflammatory response; IDA:BHF-UCL.
GO; GO:0007596; P:blood coagulation; IDA:BHF-UCL.
GO; GO:0007598; P:blood coagulation, extrinsic pathway; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IC:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015373; Interferon/interleukin_rcp_dom.
InterPro; IPR001187; Tissue_factor.
InterPro; IPR030472; Tissue_Factor_CS.
PANTHER; PTHR20859:SF22; PTHR20859:SF22; 1.
Pfam; PF09294; Interfer-bind; 1.
Pfam; PF01108; Tissue_fac; 1.
PIRSF; PIRSF002498; Tissue_factor_3; 1.
PRINTS; PR00346; TISSUEFACTOR.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS00621; TISSUE_FACTOR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation;
Complete proteome; Disulfide bond; Glycoprotein; Hemostasis;
Lipoprotein; Membrane; Palmitate; Polymorphism; Reference proteome;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 32
CHAIN 33 295 Tissue factor.
/FTId=PRO_0000033638.
TOPO_DOM 33 251 Extracellular. {ECO:0000255}.
TRANSMEM 252 274 Helical. {ECO:0000255}.
TOPO_DOM 275 295 Cytoplasmic. {ECO:0000255}.
MOTIF 46 48 WKS motif.
MOTIF 77 79 WKS motif.
MOTIF 190 192 WKS motif.
LIPID 277 277 S-palmitoyl cysteine.
{ECO:0000269|PubMed:3166978}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 81 89 {ECO:0000269|PubMed:3166978}.
DISULFID 218 241 {ECO:0000269|PubMed:3166978}.
VAR_SEQ 199 238 TAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSP
-> YSTSLELWYLWSSSLSSSWLYLYTSVERQEWGRAGRRT
PH (in isoform 2).
{ECO:0000303|PubMed:12652293}.
/FTId=VSP_041896.
VAR_SEQ 239 295 Missing (in isoform 2).
{ECO:0000303|PubMed:12652293}.
/FTId=VSP_041897.
VARIANT 36 36 T -> A (in dbSNP:rs3917604).
{ECO:0000269|Ref.9}.
/FTId=VAR_014298.
VARIANT 145 145 I -> V (in dbSNP:rs3917627).
{ECO:0000269|Ref.9}.
/FTId=VAR_014299.
VARIANT 163 163 R -> W (in dbSNP:rs5901).
/FTId=VAR_012008.
VARIANT 281 281 G -> E (in dbSNP:rs3789683).
/FTId=VAR_052280.
CONFLICT 260 260 V -> A (in Ref. 1; AAA61151).
{ECO:0000305}.
STRAND 42 49 {ECO:0000244|PDB:4YLQ}.
STRAND 52 58 {ECO:0000244|PDB:4YLQ}.
STRAND 62 72 {ECO:0000244|PDB:4YLQ}.
STRAND 73 75 {ECO:0000244|PDB:1UJ3}.
STRAND 78 85 {ECO:0000244|PDB:4YLQ}.
STRAND 87 90 {ECO:0000244|PDB:4YLQ}.
HELIX 92 95 {ECO:0000244|PDB:4YLQ}.
HELIX 96 98 {ECO:0000244|PDB:2HFT}.
STRAND 103 111 {ECO:0000244|PDB:4YLQ}.
HELIX 113 115 {ECO:0000244|PDB:1Z6J}.
TURN 119 122 {ECO:0000244|PDB:4YLQ}.
STRAND 126 128 {ECO:0000244|PDB:4YLQ}.
HELIX 134 137 {ECO:0000244|PDB:4YLQ}.
STRAND 145 151 {ECO:0000244|PDB:4YLQ}.
STRAND 154 159 {ECO:0000244|PDB:4YLQ}.
STRAND 163 168 {ECO:0000244|PDB:4YLQ}.
STRAND 171 174 {ECO:0000244|PDB:4YLQ}.
HELIX 175 179 {ECO:0000244|PDB:4YLQ}.
HELIX 180 182 {ECO:0000244|PDB:4YLQ}.
STRAND 184 191 {ECO:0000244|PDB:4YLQ}.
STRAND 194 196 {ECO:0000244|PDB:3TH2}.
STRAND 198 210 {ECO:0000244|PDB:4YLQ}.
STRAND 213 215 {ECO:0000244|PDB:1WV7}.
STRAND 217 224 {ECO:0000244|PDB:4YLQ}.
STRAND 229 231 {ECO:0000244|PDB:4YLQ}.
STRAND 240 243 {ECO:0000244|PDB:1BOY}.
STRAND 279 284 {ECO:0000244|PDB:2CEF}.
STRAND 289 293 {ECO:0000244|PDB:2CEF}.
SEQUENCE 295 AA; 33068 MW; D3486C713ED8EAD0 CRC64;
METPAWPRVP RPETAVARTL LLGWVFAQVA GASGTTNTVA AYNLTWKSTN FKTILEWEPK
PVNQVYTVQI STKSGDWKSK CFYTTDTECD LTDEIVKDVK QTYLARVFSY PAGNVESTGS
AGEPLYENSP EFTPYLETNL GQPTIQSFEQ VGTKVNVTVE DERTLVRRNN TFLSLRDVFG
KDLIYTLYYW KSSSSGKKTA KTNTNEFLID VDKGENYCFS VQAVIPSRTV NRKSTDSPVE
CMGQEKGEFR EIFYIIGAVV FVVIILVIIL AISLHKCRKA GVGQSWKENS PLNVS


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