Reviewed, UniProtKB/Swiss-Prot P13726 (TF_HUMAN)

Names and origin

Protein names

Recommended name:
    Tissue factor
      Short name=TF
Alternative name(s):
    Coagulation factor III
    Thromboplastin
    CD_antigen=CD142

Gene names

Name:

F3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Subcellular location	Membrane; Single-pass type I membrane protein.
Induction	TF expression is highly dependent upon cell type. TF can also be induced by the inflammatory mediators interleukin 1 and TNF, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response.
Sequence similarities	Belongs to the tissue factor family.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of blood coagulation via clotting cascade Inferred by curator. Source: UniProtKB activation of caspase activity Inferred from direct assay. Source: UniProtKB activation of plasma proteins involved in acute inflammatory response Inferred from direct assay. Source: UniProtKB anti-apoptosis Traceable author statement. Source: UniProtKB blood coagulation, extrinsic pathway Inferred from Experiment. Source: Reactome positive regulation of angiogenesis Inferred from direct assay. Source: UniProtKB positive regulation of cell migration Traceable author statement. Source: UniProtKB positive regulation of endothelial cell proliferation Inferred from direct assay. Source: UniProtKB positive regulation of platelet-derived growth factor receptor signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of positive chemotaxis Inferred by curator. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from mutant phenotype. Source: UniProtKB
Cellular component	extracellular matrix Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB integral to membrane Ref.3 Traceable author statement. Source: ProtInc intrinsic to external side of plasma membrane Inferred by curator. Source: UniProtKB
Molecular function	cell surface binding Inferred from direct assay. Source: UniProtKB phospholipid binding Inferred from direct assay. Source: UniProtKB protease binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Chain

33 – 295

263

Tissue factor

PRO_0000033638

Regions

Topological domain

33 – 251

219

Extracellular Potential

Transmembrane

252 – 274

23

Potential

Topological domain

275 – 295

21

Cytoplasmic Potential

Motif

46 – 48

3

WKS motif

Motif

77 – 79

3

WKS motif

Motif

190 – 192

3

WKS motif

Amino acid modifications

Lipidation

277

1

S-palmitoyl cysteine Ref.11

Glycosylation

156

1

N-linked (GlcNAc...) Potential

Glycosylation

169

1

N-linked (GlcNAc...) Potential

Disulfide bond

81 ↔ 89

Ref.11

Disulfide bond

218 ↔ 241

Ref.11

Natural variations

Natural variant

36

1

T → A: dbSNP rs3917604. Ref.8

VAR_014298

Natural variant

145

1

I → V: dbSNP rs3917627. Ref.8

VAR_014299

Natural variant

163

1

R → W: dbSNP rs5901.

VAR_012008

Natural variant

281

1

G → E: dbSNP rs3789683.

VAR_052280

Experimental info

Sequence conflict

260

1

V → A in AAA61151. Ref.1

Secondary structure

1

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295

Helix Strand Turn

Details...

Beta strand

42 – 49

8

Beta strand

52 – 58

7

Beta strand

62 – 72

11

Beta strand

78 – 84

7

Beta strand

87 – 90

4

Helix

92 – 95

4

Beta strand

103 – 111

9

Beta strand

125 – 128

4

Helix

134 – 137

4

Beta strand

145 – 150

6

Beta strand

152 – 159

8

Beta strand

163 – 168

6

Beta strand

171 – 174

4

Helix

175 – 179

5

Helix

180 – 182

3

Beta strand

184 – 193

10

Beta strand

198 – 210

13

Beta strand

217 – 224

8

Beta strand

229 – 231

3

Beta strand

240 – 243

4

Sequences

	Sequence		Length	Mass (Da)
	P13726-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: D3486C713ED8EAD0	FASTA	295	33,068
	10 20 30 40 50 60 METPAWPRVP RPETAVARTL LLGWVFAQVA GASGTTNTVA AYNLTWKSTN FKTILEWEPK 70 80 90 100 110 120 PVNQVYTVQI STKSGDWKSK CFYTTDTECD LTDEIVKDVK QTYLARVFSY PAGNVESTGS 130 140 150 160 170 180 AGEPLYENSP EFTPYLETNL GQPTIQSFEQ VGTKVNVTVE DERTLVRRNN TFLSLRDVFG 190 200 210 220 230 240 KDLIYTLYYW KSSSSGKKTA KTNTNEFLID VDKGENYCFS VQAVIPSRTV NRKSTDSPVE 250 260 270 280 290 CMGQEKGEFR EIFYIIGAVV FVVIILVIIL AISLHKCRKA GVGQSWKENS PLNVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human tissue factor: cDNA sequence and chromosome localization of the gene." Scarpati E.M., Wen D., Broze G.J. Jr., Miletich J.P., Flandermeyer R.R., Siegel N.R., Sadler J.E. Biochemistry 26:5234-5238(1987) [PubMed: 2823875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initiation of the coagulation protease cascade." Morrissey J.H., Fakhrai H., Edgington T.S. Cell 50:129-135(1987) [PubMed: 3297348] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA." Spicer E.K., Horton R., Bloem L., Bach R., Williams K.R., Guha A., Kraus J., Lin T.C., Nemerson Y., Konigsberg W.H. Proc. Natl. Acad. Sci. U.S.A. 84:5148-5152(1987) [PubMed: 3037536] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning and expression of human tissue factor cDNA." Fisher K.L., Gorman C.M., Vehar G.A., O'Brien D.P., Lawn R.M. Thromb. Res. 48:89-99(1987) [PubMed: 3424286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Complete sequence of the human tissue factor gene, a highly regulated cellular receptor that initiates the coagulation protease cascade." Mackman N., Morrissey J.H., Fowler B., Edgington T.S. Biochemistry 28:1755-1762(1989) [PubMed: 2719931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	SeattleSNPs variation discovery resource Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-36 AND VAL-145.
[9]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[11]	"Human tissue factor contains thioester-linked palmitate and stearate on the cytoplasmic half-cystine." Bach R., Konigsberg W.H., Nemerson Y. Biochemistry 27:4227-4231(1988) [PubMed: 3166978] [Abstract] Cited for: DISULFIDE BONDS, PALMITOYLATION AT CYS-277.
[12]	"Structure of the extracellular domain of human tissue factor: location of the factor VIIa binding site." Muller Y.A., Ultsch M.H., Kelley R.F., de Vos A.M. Biochemistry 33:10864-10870(1994) [PubMed: 8086403] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 33-243.
[13]	"The crystal structure of the extracellular domain of human tissue factor refined to 1.7-A resolution." Muller Y.A., Ultsch M.H., de Vos A.M. J. Mol. Biol. 256:144-159(1996) [PubMed: 8609606] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-243.
[14]	"The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor." Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H., Nemreson Y., Kirchhofer D. Nature 380:41-46(1996) [PubMed: 8598903] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-251 IN COMPLEX WITH FVIIA.
[15]	"Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant." Zhang E., St Charles R., Tulinsky A. J. Mol. Biol. 285:2089-2104(1999) [PubMed: 9925787] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-242 IN COMPLEX WITH FVIIA.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Tissue factor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16553 mRNA. Translation: AAA61151.1.
J02931 mRNA. Translation: AAA61150.1.
M27436 mRNA. Translation: AAA36734.1.
J02846 Genomic DNA. Translation: AAA61152.1.
BT019808 mRNA. Translation: AAV38611.1.
CR541792 mRNA. Translation: CAG46591.1.
AF540377 Genomic DNA. Translation: AAN01236.1.
AL138758 Genomic DNA. No translation available.
BC011029 mRNA. Translation: AAH11029.1.

IPI

IPI00010338.

PIR

KFHU3. A43645.

RefSeq

NP_001984.1.

UniGene

Hs.62192

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AHW	X-ray	3.00	C/F	33-251	[»]
1BOY	X-ray	2.20	A	33-251	[»]
1DAN	X-ray	2.00	T	37-116	[»]
			U	122-242	[»]
1FAK	X-ray	2.10	T	37-242	[»]
1J9C	X-ray	2.90	T	33-242	[»]
1JPS	X-ray	1.85	T	33-251	[»]
1NL8	model	-	T	33-242	[»]
1O5D	X-ray	2.05	T	34-251	[»]
1TFH	X-ray	2.40	A/B	33-251	[»]
1UJ3	X-ray	2.10	C	38-242	[»]
1W0Y	X-ray	2.50	T	33-242	[»]
1W2K	X-ray	3.00	T	33-242	[»]
1WQV	X-ray	2.50	T	33-250	[»]
1WSS	X-ray	2.60	T	33-250	[»]
1WTG	X-ray	2.20	T	33-250	[»]
1WUN	X-ray	2.40	T	33-250	[»]
1WV7	X-ray	2.70	T	33-250	[»]
1Z6J	X-ray	2.00	T	33-243	[»]
2A2Q	X-ray	1.80	T	38-242	[»]
2AEI	X-ray	2.52	T	33-243	[»]
2AER	X-ray	1.87	T	38-242	[»]
2B7D	X-ray	2.24	T	34-251	[»]
2B8O	X-ray	2.80	T	38-242	[»]
2C4F	X-ray	1.72	T	38-112	[»]
			U	123-242	[»]
2CEF	NMR	-	A	277-295	[»]
2CEH	NMR	-	A	277-295	[»]
2CEZ	NMR	-	A	277-295	[»]
2CFJ	NMR	-	A	277-295	[»]
2EC9	X-ray	2.00	T	38-112	[»]
			U	123-242	[»]
2F9B	X-ray	2.54	T	34-251	[»]
2FIR	X-ray	2.00	T	38-242	[»]
2FLB	X-ray	1.95	T	34-251	[»]
2FLR	X-ray	2.35	T	34-251	[»]
2HFT	X-ray	1.69	A	33-243	[»]
2PUQ	X-ray	2.05	T	38-241	[»]
2ZP0	X-ray	2.70	T	33-250	[»]
2ZWL	X-ray	2.20	T	33-250	[»]
2ZZU	X-ray	2.50	T	33-250	[»]
3ELA	X-ray	2.20	T	33-241	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6136N.

STRING

P13726.

PTM databases

PhosphoSite

P13726.

Proteomic databases

PRIDE

P13726.

Genome annotation databases

Ensembl

ENST00000334047; ENSP00000334145; ENSG00000117525; Homo sapiens. [Genome view]

GeneID

2152.

KEGG

hsa:2152.

NMPDR

fig|9606.3.peg.1526.

UCSC

uc001dqr.1. human.

Organism-specific databases

CTD

2152.

GeneCards

GC01M094706.

H-InvDB

HIX0000795.

HGNC

HGNC:3541. F3.

HPA

CAB009438.

MIM

134390. gene.

PharmGKB

PA24407.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20681.

HOGENOM

HBG445882.

HOVERGEN

P13726.

InParanoid

P13726.

OMA

NTNEFLI.

OrthoDB

EOG9TXFBN.

PhylomeDB

P13726.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P13726.

Bgee

P13726.

CleanEx

HS_F3.

Genevestigator

P13726.

GermOnline

ENSG00000117525. Homo sapiens.

Family and domain databases

InterPro

IPR008957. Fibronectin_typ-III-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
IPR016354. Tissue_fac/coagulation_fac-3.
IPR001187. Tissue_factor.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 1 hit.

Pfam

PF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]

PIRSF

PIRSF002498. Tissue_factor_3. 1 hit.

PRINTS

PR00346. TISSUEFACTOR.

PROSITE

PS00621. TISSUE_FACTOR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00036. Coagulation factor VIIa.

NextBio

8697.

SOURCE

Search...

Entry information

Entry name

TF_HUMAN

Accession

Primary (citable) accession number: P13726
Secondary accession number(s): Q6FHG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	January 19, 2010
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.