TF_HUMAN
ID TF_HUMAN Reviewed; 295 AA.
AC P13726; D3DT47; Q6FHG2; Q86WH4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Tissue factor;
DE Short=TF;
DE AltName: Full=Coagulation factor III;
DE AltName: Full=Thromboplastin;
DE AltName: CD_antigen=CD142;
DE Flags: Precursor;
GN Name=F3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2823875; DOI=10.1021/bi00391a004;
RA Scarpati E.M., Wen D., Broze G.J. Jr., Miletich J.P., Flandermeyer R.R.,
RA Siegel N.R., Sadler J.E.;
RT "Human tissue factor: cDNA sequence and chromosome localization of the
RT gene.";
RL Biochemistry 26:5234-5238(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3297348; DOI=10.1016/0092-8674(87)90669-6;
RA Morrissey J.H., Fakhrai H., Edgington T.S.;
RT "Molecular cloning of the cDNA for tissue factor, the cellular receptor for
RT the initiation of the coagulation protease cascade.";
RL Cell 50:129-135(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3037536; DOI=10.1073/pnas.84.15.5148;
RA Spicer E.K., Horton R., Bloem L., Bach R., Williams K.R., Guha A.,
RA Kraus J., Lin T.C., Nemerson Y., Konigsberg W.H.;
RT "Isolation of cDNA clones coding for human tissue factor: primary structure
RT of the protein and cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5148-5152(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3424286; DOI=10.1016/0049-3848(87)90349-5;
RA Fisher K.L., Gorman C.M., Vehar G.A., O'Brien D.P., Lawn R.M.;
RT "Cloning and expression of human tissue factor cDNA.";
RL Thromb. Res. 48:89-99(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2719931; DOI=10.1021/bi00430a050;
RA Mackman N., Morrissey J.H., Fowler B., Edgington T.S.;
RT "Complete sequence of the human tissue factor gene, a highly regulated
RT cellular receptor that initiates the coagulation protease cascade.";
RL Biochemistry 28:1755-1762(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12652293; DOI=10.1038/nm841;
RA Bogdanov V.Y., Balasubramanian V., Hathcock J., Vele O., Lieb M.,
RA Nemerson Y.;
RT "Alternatively spliced human tissue factor: a circulating, soluble,
RT thrombogenic protein.";
RL Nat. Med. 9:458-462(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-36 AND VAL-145.
RG SeattleSNPs variation discovery resource;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP DISULFIDE BONDS, AND PALMITOYLATION AT CYS-277.
RX PubMed=3166978; DOI=10.1021/bi00412a004;
RA Bach R., Konigsberg W.H., Nemerson Y.;
RT "Human tissue factor contains thioester-linked palmitate and stearate on
RT the cytoplasmic half-cystine.";
RL Biochemistry 27:4227-4231(1988).
RN [14]
RP ALTERNATIVE SPLICING, AND INDUCTION.
RX PubMed=19168442; DOI=10.1161/circresaha.108.183905;
RA Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S.,
RA Poller W., Schultheiss H.P., Rauch U.;
RT "Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of
RT tissue factor in human endothelial cells.";
RL Circ. Res. 104:589-599(2009).
RN [15]
RP INTERACTION WITH HPSE.
RX PubMed=20634491; DOI=10.3324/haematol.2010.023713;
RA Nadir Y., Brenner B., Fux L., Shafat I., Attias J., Vlodavsky I.;
RT "Heparanase enhances the generation of activated factor X in the presence
RT of tissue factor and activated factor VII.";
RL Haematologica 95:1927-1934(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 33-243.
RX PubMed=8086403; DOI=10.1021/bi00202a003;
RA Muller Y.A., Ultsch M.H., Kelley R.F., de Vos A.M.;
RT "Structure of the extracellular domain of human tissue factor: location of
RT the factor VIIa binding site.";
RL Biochemistry 33:10864-10870(1994).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-243.
RX PubMed=8609606; DOI=10.1006/jmbi.1996.0073;
RA Muller Y.A., Ultsch M.H., de Vos A.M.;
RT "The crystal structure of the extracellular domain of human tissue factor
RT refined to 1.7-A resolution.";
RL J. Mol. Biol. 256:144-159(1996).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-251 IN COMPLEX WITH FVIIA.
RX PubMed=8598903; DOI=10.1038/380041a0;
RA Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H.,
RA Nemreson Y., Kirchhofer D.;
RT "The crystal structure of the complex of blood coagulation factor VIIa with
RT soluble tissue factor.";
RL Nature 380:41-46(1996).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-242 IN COMPLEX WITH FVIIA.
RX PubMed=9925787; DOI=10.1006/jmbi.1998.2452;
RA Zhang E., St Charles R., Tulinsky A.;
RT "Structure of extracellular tissue factor complexed with factor VIIa
RT inhibited with a BPTI mutant.";
RL J. Mol. Biol. 285:2089-2104(1999).
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:0000269|PubMed:12652293}.
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. {ECO:0000269|PubMed:20634491,
CC ECO:0000269|PubMed:8598903, ECO:0000269|PubMed:9925787}.
CC -!- INTERACTION:
CC P13726; P55085: F2RL1; NbExp=2; IntAct=EBI-1040727, EBI-4303189;
CC P13726; P08709: F7; NbExp=7; IntAct=EBI-1040727, EBI-355972;
CC P13726; Q9UM19: HPCAL4; NbExp=3; IntAct=EBI-1040727, EBI-744820;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane
CC {ECO:0000269|PubMed:12652293}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12652293}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:12652293}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms may exist.;
CC Name=1; Synonyms=flTF;
CC IsoId=P13726-1; Sequence=Displayed;
CC Name=2; Synonyms=asHTF;
CC IsoId=P13726-2; Sequence=VSP_041896, VSP_041897;
CC -!- TISSUE SPECIFICITY: Lung, placenta and pancreas.
CC {ECO:0000269|PubMed:12652293}.
CC -!- INDUCTION: TF expression is highly dependent upon cell type. TF can
CC also be induced by the inflammatory mediators interleukin 1 and TNF-
CC alpha, as well as by endotoxin, to appear on monocytes and vascular
CC endothelial cells as a component of cellular immune response.
CC {ECO:0000269|PubMed:19168442}.
CC -!- SIMILARITY: Belongs to the tissue factor family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/f3/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Tissue factor entry;
CC URL="https://en.wikipedia.org/wiki/Tissue_factor";
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DR EMBL; M16553; AAA61151.1; -; mRNA.
DR EMBL; J02931; AAA61150.1; -; mRNA.
DR EMBL; M27436; AAA36734.1; -; mRNA.
DR EMBL; J02846; AAA61152.1; -; Genomic_DNA.
DR EMBL; BT019808; AAV38611.1; -; mRNA.
DR EMBL; CR541792; CAG46591.1; -; mRNA.
DR EMBL; AF487337; AAO61150.1; -; mRNA.
DR EMBL; AF540377; AAN01236.1; -; Genomic_DNA.
DR EMBL; AC093117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73044.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73045.1; -; Genomic_DNA.
DR EMBL; BC011029; AAH11029.1; -; mRNA.
DR CCDS; CCDS53345.1; -. [P13726-2]
DR CCDS; CCDS750.1; -. [P13726-1]
DR PIR; A43645; KFHU3.
DR RefSeq; NP_001171567.1; NM_001178096.1. [P13726-2]
DR RefSeq; NP_001984.1; NM_001993.4. [P13726-1]
DR PDB; 1AHW; X-ray; 3.00 A; C/F=33-251.
DR PDB; 1BOY; X-ray; 2.20 A; A=33-251.
DR PDB; 1DAN; X-ray; 2.00 A; T=37-116, U=122-242.
DR PDB; 1FAK; X-ray; 2.10 A; T=37-242.
DR PDB; 1J9C; X-ray; 2.90 A; T=33-242.
DR PDB; 1JPS; X-ray; 1.85 A; T=33-251.
DR PDB; 1O5D; X-ray; 2.05 A; T=34-251.
DR PDB; 1TFH; X-ray; 2.40 A; A/B=33-251.
DR PDB; 1UJ3; X-ray; 2.10 A; C=38-242.
DR PDB; 1W0Y; X-ray; 2.50 A; T=33-242.
DR PDB; 1W2K; X-ray; 3.00 A; T=33-242.
DR PDB; 1WQV; X-ray; 2.50 A; T=33-250.
DR PDB; 1WSS; X-ray; 2.60 A; T=33-250.
DR PDB; 1WTG; X-ray; 2.20 A; T=33-250.
DR PDB; 1WUN; X-ray; 2.40 A; T=33-250.
DR PDB; 1WV7; X-ray; 2.70 A; T=33-250.
DR PDB; 1Z6J; X-ray; 2.00 A; T=33-243.
DR PDB; 2A2Q; X-ray; 1.80 A; T=38-242.
DR PDB; 2AEI; X-ray; 2.52 A; T=33-243.
DR PDB; 2AER; X-ray; 1.87 A; T=38-242.
DR PDB; 2B7D; X-ray; 2.24 A; T=34-251.
DR PDB; 2B8O; X-ray; 2.80 A; T=38-242.
DR PDB; 2C4F; X-ray; 1.72 A; T=38-112, U=123-242.
DR PDB; 2CEF; NMR; -; A=277-295.
DR PDB; 2CEH; NMR; -; A=277-295.
DR PDB; 2CEZ; NMR; -; A=277-295.
DR PDB; 2CFJ; NMR; -; A=277-295.
DR PDB; 2EC9; X-ray; 2.00 A; T=38-112, U=123-242.
DR PDB; 2F9B; X-ray; 2.54 A; T=34-251.
DR PDB; 2FIR; X-ray; 2.00 A; T=38-242.
DR PDB; 2FLB; X-ray; 1.95 A; T=34-251.
DR PDB; 2FLR; X-ray; 2.35 A; T=34-251.
DR PDB; 2HFT; X-ray; 1.69 A; A=33-243.
DR PDB; 2PUQ; X-ray; 2.05 A; T=38-241.
DR PDB; 2ZP0; X-ray; 2.70 A; T=33-250.
DR PDB; 2ZWL; X-ray; 2.20 A; T=33-250.
DR PDB; 2ZZU; X-ray; 2.50 A; T=33-250.
DR PDB; 3ELA; X-ray; 2.20 A; T=33-241.
DR PDB; 3TH2; X-ray; 1.72 A; T=38-242.
DR PDB; 3TH3; X-ray; 2.70 A; T=38-242.
DR PDB; 3TH4; X-ray; 1.80 A; T=38-242.
DR PDB; 4IBL; X-ray; 1.80 A; T=33-251.
DR PDB; 4M7L; X-ray; 3.40 A; T=37-245.
DR PDB; 4YLQ; X-ray; 1.40 A; T=33-251.
DR PDB; 4Z6A; X-ray; 2.25 A; T=36-242.
DR PDB; 4ZMA; X-ray; 2.30 A; T=33-251.
DR PDB; 5W06; X-ray; 2.60 A; T=37-245.
DR PDB; 6R2W; X-ray; 1.25 A; T=33-242.
DR PDB; 6Z9W; X-ray; 2.70 A; C/F=21-29.
DR PDBsum; 1AHW; -.
DR PDBsum; 1BOY; -.
DR PDBsum; 1DAN; -.
DR PDBsum; 1FAK; -.
DR PDBsum; 1J9C; -.
DR PDBsum; 1JPS; -.
DR PDBsum; 1O5D; -.
DR PDBsum; 1TFH; -.
DR PDBsum; 1UJ3; -.
DR PDBsum; 1W0Y; -.
DR PDBsum; 1W2K; -.
DR PDBsum; 1WQV; -.
DR PDBsum; 1WSS; -.
DR PDBsum; 1WTG; -.
DR PDBsum; 1WUN; -.
DR PDBsum; 1WV7; -.
DR PDBsum; 1Z6J; -.
DR PDBsum; 2A2Q; -.
DR PDBsum; 2AEI; -.
DR PDBsum; 2AER; -.
DR PDBsum; 2B7D; -.
DR PDBsum; 2B8O; -.
DR PDBsum; 2C4F; -.
DR PDBsum; 2CEF; -.
DR PDBsum; 2CEH; -.
DR PDBsum; 2CEZ; -.
DR PDBsum; 2CFJ; -.
DR PDBsum; 2EC9; -.
DR PDBsum; 2F9B; -.
DR PDBsum; 2FIR; -.
DR PDBsum; 2FLB; -.
DR PDBsum; 2FLR; -.
DR PDBsum; 2HFT; -.
DR PDBsum; 2PUQ; -.
DR PDBsum; 2ZP0; -.
DR PDBsum; 2ZWL; -.
DR PDBsum; 2ZZU; -.
DR PDBsum; 3ELA; -.
DR PDBsum; 3TH2; -.
DR PDBsum; 3TH3; -.
DR PDBsum; 3TH4; -.
DR PDBsum; 4IBL; -.
DR PDBsum; 4M7L; -.
DR PDBsum; 4YLQ; -.
DR PDBsum; 4Z6A; -.
DR PDBsum; 4ZMA; -.
DR PDBsum; 5W06; -.
DR PDBsum; 6R2W; -.
DR PDBsum; 6Z9W; -.
DR AlphaFoldDB; P13726; -.
DR BMRB; P13726; -.
DR SMR; P13726; -.
DR BioGRID; 108451; 32.
DR ComplexPortal; CPX-2808; Coagulation factor VIIa - tissue factor complex.
DR CORUM; P13726; -.
DR DIP; DIP-6136N; -.
DR IntAct; P13726; 7.
DR STRING; 9606.ENSP00000334145; -.
DR BindingDB; P13726; -.
DR ChEMBL; CHEMBL4081; -.
DR DrugBank; DB07207; 2-(4-HYDROXY-5-PHENYL-1H-PYRAZOL-3-YL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE.
DR DrugBank; DB07247; [2'-HYDROXY-3'-(1H-PYRROLO[3,2-C]PYRIDIN-2-YL)-BIPHENYL-3-YLMETHYL]-UREA.
DR DrugBank; DB08232; [5-(5-Amino-1H-pyrrolo[3,2-b]pyridin-2-yl)-6-hydroxy-3'-nitro-3-biphenylyl]acetic acid.
DR DrugBank; DB13150; Coagulation factor VII human.
DR DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DR DrugBank; DB06552; rNAPc2.
DR DrugBank; DB16732; Tisotumab vedotin.
DR DrugCentral; P13726; -.
DR TCDB; 8.A.132.2.1; the interferon/interleukin receptor (iir) family.
DR GlyConnect; 1811; 1 N-Linked glycan (1 site).
DR GlyGen; P13726; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P13726; -.
DR PhosphoSitePlus; P13726; -.
DR SwissPalm; P13726; -.
DR BioMuta; F3; -.
DR DMDM; 135666; -.
DR CPTAC; CPTAC-1479; -.
DR EPD; P13726; -.
DR jPOST; P13726; -.
DR MassIVE; P13726; -.
DR MaxQB; P13726; -.
DR PaxDb; P13726; -.
DR PeptideAtlas; P13726; -.
DR PRIDE; P13726; -.
DR ProteomicsDB; 52976; -. [P13726-1]
DR ProteomicsDB; 52977; -. [P13726-2]
DR ABCD; P13726; 10 sequenced antibodies.
DR Antibodypedia; 4000; 920 antibodies from 44 providers.
DR DNASU; 2152; -.
DR Ensembl; ENST00000334047.12; ENSP00000334145.7; ENSG00000117525.14. [P13726-1]
DR Ensembl; ENST00000370207.4; ENSP00000359226.4; ENSG00000117525.14. [P13726-2]
DR GeneID; 2152; -.
DR KEGG; hsa:2152; -.
DR MANE-Select; ENST00000334047.12; ENSP00000334145.7; NM_001993.5; NP_001984.1.
DR UCSC; uc001dqr.4; human. [P13726-1]
DR CTD; 2152; -.
DR DisGeNET; 2152; -.
DR GeneCards; F3; -.
DR HGNC; HGNC:3541; F3.
DR HPA; ENSG00000117525; Low tissue specificity.
DR MIM; 134390; gene.
DR neXtProt; NX_P13726; -.
DR OpenTargets; ENSG00000117525; -.
DR PharmGKB; PA158; -.
DR VEuPathDB; HostDB:ENSG00000117525; -.
DR eggNOG; ENOG502RA1F; Eukaryota.
DR GeneTree; ENSGT00390000012668; -.
DR HOGENOM; CLU_082139_0_0_1; -.
DR InParanoid; P13726; -.
DR OMA; KFTPYNQ; -.
DR OrthoDB; 1000890at2759; -.
DR PhylomeDB; P13726; -.
DR TreeFam; TF352627; -.
DR PathwayCommons; P13726; -.
DR Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P13726; -.
DR SIGNOR; P13726; -.
DR BioGRID-ORCS; 2152; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; F3; human.
DR EvolutionaryTrace; P13726; -.
DR GeneWiki; Tissue_factor; -.
DR GenomeRNAi; 2152; -.
DR Pharos; P13726; Tchem.
DR PRO; PR:P13726; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P13726; protein.
DR Bgee; ENSG00000117525; Expressed in mucosa of paranasal sinus and 205 other tissues.
DR Genevisible; P13726; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IC:BHF-UCL.
DR GO; GO:0016020; C:membrane; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:1905286; C:serine-type peptidase complex; IPI:BHF-UCL.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0002543; P:activation of blood coagulation via clotting cascade; IC:BHF-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0002541; P:activation of plasma proteins involved in acute inflammatory response; IDA:BHF-UCL.
DR GO; GO:0007596; P:blood coagulation; IDA:BHF-UCL.
DR GO; GO:0007598; P:blood coagulation, extrinsic pathway; IC:ComplexPortal.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IC:ComplexPortal.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IC:ComplexPortal.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:ARUK-UCL.
DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IC:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
DR GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0009611; P:response to wounding; IC:ComplexPortal.
DR Gene3D; 2.60.40.10; -; 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:SF22; PTHR20859:SF22; 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; SSF49265; 2.
DR PROSITE; PS00621; TISSUE_FACTOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation; Disulfide bond;
KW Glycoprotein; Hemostasis; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT CHAIN 33..295
FT /note="Tissue factor"
FT /id="PRO_0000033638"
FT TOPO_DOM 33..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 46..48
FT /note="WKS motif"
FT MOTIF 77..79
FT /note="WKS motif"
FT MOTIF 190..192
FT /note="WKS motif"
FT LIPID 277
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:3166978"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..89
FT /evidence="ECO:0000269|PubMed:3166978"
FT DISULFID 218..241
FT /evidence="ECO:0000269|PubMed:3166978"
FT VAR_SEQ 199..238
FT /note="TAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSP -> YSTSLELW
FT YLWSSSLSSSWLYLYTSVERQEWGRAGRRTPH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12652293"
FT /id="VSP_041896"
FT VAR_SEQ 239..295
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12652293"
FT /id="VSP_041897"
FT VARIANT 36
FT /note="T -> A (in dbSNP:rs3917604)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_014298"
FT VARIANT 145
FT /note="I -> V (in dbSNP:rs3917627)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_014299"
FT VARIANT 163
FT /note="R -> W (in dbSNP:rs5901)"
FT /id="VAR_012008"
FT VARIANT 281
FT /note="G -> E (in dbSNP:rs3789683)"
FT /id="VAR_052280"
FT CONFLICT 260
FT /note="V -> A (in Ref. 1; AAA61151)"
FT /evidence="ECO:0000305"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1UJ3"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6R2W"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:6R2W"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2HFT"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:6R2W"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1Z6J"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:4YLQ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6R2W"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:6R2W"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:6R2W"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3TH2"
FT STRAND 198..210
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1WV7"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6R2W"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1BOY"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:2CEF"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2CEF"
SQ 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
