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   27-MAR-2024, entry version 233.
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; 33.
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   GlyCosmos; P13726; 2 sites, 1 glycan.
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; 9606-ENSP00000334145; -.
DR   PeptideAtlas; P13726; -.
DR   ProteomicsDB; 52976; -. [P13726-1]
DR   ProteomicsDB; 52977; -. [P13726-2]
DR   Pumba; P13726; -.
DR   ABCD; P13726; 10 sequenced antibodies.
DR   Antibodypedia; 4000; 1131 antibodies from 45 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   AGR; HGNC:3541; -.
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; PINYVYT; -.
DR   OrthoDB; 5321079at2759; -.
DR   PhylomeDB; P13726; -.
DR   TreeFam; TF352627; -.
DR   BioCyc; MetaCyc:ENSG00000117525-MONOMER; -.
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 1149 CRISPR screens.
DR   ChiTaRS; F3; human.
DR   EvolutionaryTrace; P13726; -.
DR   GeneWiki; Tissue_factor; -.
DR   GenomeRNAi; 2152; -.
DR   Pharos; P13726; Tclin.
DR   PRO; PR:P13726; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P13726; Protein.
DR   Bgee; ENSG00000117525; Expressed in mucosa of paranasal sinus and 207 other cell types or tissues.
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:0009897; C:external side of plasma membrane; IC:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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: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:0032008; P:positive regulation of TOR signaling; IMP:BHF-UCL.
DR   GO; GO:0016485; P:protein processing; IDA:BHF-UCL.
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.
DR   Genevisible; P13726; HS.
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
//