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Protein

Tissue factor

Gene

F3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • cytokine receptor activity Source: GO_Central
  • phospholipid binding Source: BHF-UCL
  • protease binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiR-HSA-140834. Extrinsic Pathway of Fibrin Clot Formation.
SIGNORiP13726.

Names & Taxonomyi

Protein namesi
Recommended name:
Tissue factor
Short name:
TF
Alternative name(s):
Coagulation factor III
Thromboplastin
CD_antigen: CD142
Gene namesi
Name:F3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3541. F3.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 251219ExtracellularSequence analysisAdd
BLAST
Transmembranei252 – 27423HelicalSequence analysisAdd
BLAST
Topological domaini275 – 29521CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular space Source: BHF-UCL
  • integral component of membrane Source: ProtInc
  • intrinsic component of external side of plasma membrane Source: BHF-UCL
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA158.

Chemistry

ChEMBLiCHEMBL2095194.
DrugBankiDB00036. Coagulation factor VIIa.

Polymorphism and mutation databases

BioMutaiF3.
DMDMi135666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Add
BLAST
Chaini33 – 295263Tissue factorPRO_0000033638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi81 ↔ 891 Publication
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence analysis
Disulfide bondi218 ↔ 2411 Publication
Lipidationi277 – 2771S-palmitoyl cysteine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

EPDiP13726.
MaxQBiP13726.
PaxDbiP13726.
PeptideAtlasiP13726.
PRIDEiP13726.

PTM databases

iPTMnetiP13726.
PhosphoSiteiP13726.
SwissPalmiP13726.

Expressioni

Tissue specificityi

Lung, placenta and pancreas.1 Publication

Inductioni

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.1 Publication

Gene expression databases

BgeeiENSG00000117525.
CleanExiHS_F3.
GenevisibleiP13726. HS.

Organism-specific databases

HPAiCAB009438.
HPA049292.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
F7P087096EBI-1040727,EBI-355972

GO - Molecular functioni

  • protease binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108451. 8 interactions.
DIPiDIP-6136N.
IntActiP13726. 1 interaction.
STRINGi9606.ENSP00000334145.

Chemistry

BindingDBiP13726.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 498Combined sources
Beta strandi52 – 587Combined sources
Beta strandi62 – 7211Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 858Combined sources
Beta strandi87 – 904Combined sources
Helixi92 – 954Combined sources
Helixi96 – 983Combined sources
Beta strandi103 – 1119Combined sources
Helixi113 – 1153Combined sources
Turni119 – 1224Combined sources
Beta strandi126 – 1283Combined sources
Helixi134 – 1374Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi154 – 1596Combined sources
Beta strandi163 – 1686Combined sources
Beta strandi171 – 1744Combined sources
Helixi175 – 1795Combined sources
Helixi180 – 1823Combined sources
Beta strandi184 – 1918Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi198 – 21013Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi217 – 2248Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi279 – 2846Combined sources
Beta strandi289 – 2935Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHWX-ray3.00C/F33-251[»]
1BOYX-ray2.20A33-251[»]
1DANX-ray2.00T37-116[»]
U122-242[»]
1FAKX-ray2.10T37-242[»]
1J9CX-ray2.90T33-242[»]
1JPSX-ray1.85T33-251[»]
1NL8model-T33-242[»]
1O5DX-ray2.05T34-251[»]
1TFHX-ray2.40A/B33-251[»]
1UJ3X-ray2.10C38-242[»]
1W0YX-ray2.50T33-242[»]
1W2KX-ray3.00T33-242[»]
1WQVX-ray2.50T33-250[»]
1WSSX-ray2.60T33-250[»]
1WTGX-ray2.20T33-250[»]
1WUNX-ray2.40T33-250[»]
1WV7X-ray2.70T33-250[»]
1Z6JX-ray2.00T33-243[»]
2A2QX-ray1.80T38-242[»]
2AEIX-ray2.52T33-243[»]
2AERX-ray1.87T38-242[»]
2B7DX-ray2.24T34-251[»]
2B8OX-ray2.80T38-242[»]
2C4FX-ray1.72T38-112[»]
U123-242[»]
2CEFNMR-A277-295[»]
2CEHNMR-A277-295[»]
2CEZNMR-A277-295[»]
2CFJNMR-A277-295[»]
2EC9X-ray2.00T38-112[»]
U123-242[»]
2F9BX-ray2.54T34-251[»]
2FIRX-ray2.00T38-242[»]
2FLBX-ray1.95T34-251[»]
2FLRX-ray2.35T34-251[»]
2HFTX-ray1.69A33-243[»]
2PUQX-ray2.05T38-241[»]
2ZP0X-ray2.70T33-250[»]
2ZWLX-ray2.20T33-250[»]
2ZZUX-ray2.50T33-250[»]
3ELAX-ray2.20T33-241[»]
3TH2X-ray1.72T38-242[»]
3TH3X-ray2.70T38-242[»]
3TH4X-ray1.80T38-242[»]
4IBLX-ray1.80T33-251[»]
4M7LX-ray3.40T37-245[»]
4YLQX-ray1.40T33-251[»]
4Z6AX-ray2.25T36-242[»]
4ZMAX-ray2.30T33-251[»]
ProteinModelPortaliP13726.
SMRiP13726. Positions 38-242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13726.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi46 – 483WKS motif
Motifi77 – 793WKS motif
Motifi190 – 1923WKS motif

Sequence similaritiesi

Belongs to the tissue factor family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IYA1. Eukaryota.
ENOG4111MW4. LUCA.
GeneTreeiENSGT00390000012668.
HOGENOMiHOG000043076.
HOVERGENiHBG005051.
InParanoidiP13726.
KOiK03901.
OMAiNTNEFLI.
OrthoDBiEOG091G0MKF.
PhylomeDBiP13726.
TreeFamiTF352627.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
IPR016354. Tissue_fac/coagulation_fac-3.
IPR001187. Tissue_factor.
IPR030472. Tissue_Factor_CS.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
PIRSFiPIRSF002498. Tissue_factor_3. 1 hit.
PRINTSiPR00346. TISSUEFACTOR.
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS00621. TISSUE_FACTOR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms may exist.
Isoform 1 (identifier: P13726-1) [UniParc]FASTAAdd to basket
Also known as: flTF

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METPAWPRVP RPETAVARTL LLGWVFAQVA GASGTTNTVA AYNLTWKSTN
60 70 80 90 100
FKTILEWEPK PVNQVYTVQI STKSGDWKSK CFYTTDTECD LTDEIVKDVK
110 120 130 140 150
QTYLARVFSY PAGNVESTGS AGEPLYENSP EFTPYLETNL GQPTIQSFEQ
160 170 180 190 200
VGTKVNVTVE DERTLVRRNN TFLSLRDVFG KDLIYTLYYW KSSSSGKKTA
210 220 230 240 250
KTNTNEFLID VDKGENYCFS VQAVIPSRTV NRKSTDSPVE CMGQEKGEFR
260 270 280 290
EIFYIIGAVV FVVIILVIIL AISLHKCRKA GVGQSWKENS PLNVS
Length:295
Mass (Da):33,068
Last modified:January 1, 1990 - v1
Checksum:iD3486C713ED8EAD0
GO
Isoform 2 (identifier: P13726-2) [UniParc]FASTAAdd to basket
Also known as: asHTF

The sequence of this isoform differs from the canonical sequence as follows:
     199-238: TAKTNTNEFL...TVNRKSTDSP → YSTSLELWYL...WGRAGRRTPH
     239-295: Missing.

Show »
Length:238
Mass (Da):27,145
Checksum:i5021EDB85C12B48C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2601V → A in AAA61151 (PubMed:2823875).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361T → A.1 Publication
Corresponds to variant rs3917604 [ dbSNP | Ensembl ].
VAR_014298
Natural varianti145 – 1451I → V.1 Publication
Corresponds to variant rs3917627 [ dbSNP | Ensembl ].
VAR_014299
Natural varianti163 – 1631R → W.
Corresponds to variant rs5901 [ dbSNP | Ensembl ].
VAR_012008
Natural varianti281 – 2811G → E.
Corresponds to variant rs3789683 [ dbSNP | Ensembl ].
VAR_052280

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei199 – 23840TAKTN…STDSP → YSTSLELWYLWSSSLSSSWL YLYTSVERQEWGRAGRRTPH in isoform 2. 1 PublicationVSP_041896Add
BLAST
Alternative sequencei239 – 29557Missing in isoform 2. 1 PublicationVSP_041897Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AF487337 mRNA. Translation: AAO61150.1.
AF540377 Genomic DNA. Translation: AAN01236.1.
AC093117 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW73044.1.
CH471097 Genomic DNA. Translation: EAW73045.1.
BC011029 mRNA. Translation: AAH11029.1.
CCDSiCCDS53345.1. [P13726-2]
CCDS750.1. [P13726-1]
PIRiA43645. KFHU3.
RefSeqiNP_001171567.1. NM_001178096.1. [P13726-2]
NP_001984.1. NM_001993.4. [P13726-1]
UniGeneiHs.62192.

Genome annotation databases

EnsembliENST00000334047; ENSP00000334145; ENSG00000117525. [P13726-1]
ENST00000370207; ENSP00000359226; ENSG00000117525. [P13726-2]
GeneIDi2152.
KEGGihsa:2152.
UCSCiuc001dqr.4. human. [P13726-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Tissue factor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AF487337 mRNA. Translation: AAO61150.1.
AF540377 Genomic DNA. Translation: AAN01236.1.
AC093117 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW73044.1.
CH471097 Genomic DNA. Translation: EAW73045.1.
BC011029 mRNA. Translation: AAH11029.1.
CCDSiCCDS53345.1. [P13726-2]
CCDS750.1. [P13726-1]
PIRiA43645. KFHU3.
RefSeqiNP_001171567.1. NM_001178096.1. [P13726-2]
NP_001984.1. NM_001993.4. [P13726-1]
UniGeneiHs.62192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHWX-ray3.00C/F33-251[»]
1BOYX-ray2.20A33-251[»]
1DANX-ray2.00T37-116[»]
U122-242[»]
1FAKX-ray2.10T37-242[»]
1J9CX-ray2.90T33-242[»]
1JPSX-ray1.85T33-251[»]
1NL8model-T33-242[»]
1O5DX-ray2.05T34-251[»]
1TFHX-ray2.40A/B33-251[»]
1UJ3X-ray2.10C38-242[»]
1W0YX-ray2.50T33-242[»]
1W2KX-ray3.00T33-242[»]
1WQVX-ray2.50T33-250[»]
1WSSX-ray2.60T33-250[»]
1WTGX-ray2.20T33-250[»]
1WUNX-ray2.40T33-250[»]
1WV7X-ray2.70T33-250[»]
1Z6JX-ray2.00T33-243[»]
2A2QX-ray1.80T38-242[»]
2AEIX-ray2.52T33-243[»]
2AERX-ray1.87T38-242[»]
2B7DX-ray2.24T34-251[»]
2B8OX-ray2.80T38-242[»]
2C4FX-ray1.72T38-112[»]
U123-242[»]
2CEFNMR-A277-295[»]
2CEHNMR-A277-295[»]
2CEZNMR-A277-295[»]
2CFJNMR-A277-295[»]
2EC9X-ray2.00T38-112[»]
U123-242[»]
2F9BX-ray2.54T34-251[»]
2FIRX-ray2.00T38-242[»]
2FLBX-ray1.95T34-251[»]
2FLRX-ray2.35T34-251[»]
2HFTX-ray1.69A33-243[»]
2PUQX-ray2.05T38-241[»]
2ZP0X-ray2.70T33-250[»]
2ZWLX-ray2.20T33-250[»]
2ZZUX-ray2.50T33-250[»]
3ELAX-ray2.20T33-241[»]
3TH2X-ray1.72T38-242[»]
3TH3X-ray2.70T38-242[»]
3TH4X-ray1.80T38-242[»]
4IBLX-ray1.80T33-251[»]
4M7LX-ray3.40T37-245[»]
4YLQX-ray1.40T33-251[»]
4Z6AX-ray2.25T36-242[»]
4ZMAX-ray2.30T33-251[»]
ProteinModelPortaliP13726.
SMRiP13726. Positions 38-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108451. 8 interactions.
DIPiDIP-6136N.
IntActiP13726. 1 interaction.
STRINGi9606.ENSP00000334145.

Chemistry

BindingDBiP13726.
ChEMBLiCHEMBL2095194.
DrugBankiDB00036. Coagulation factor VIIa.

PTM databases

iPTMnetiP13726.
PhosphoSiteiP13726.
SwissPalmiP13726.

Polymorphism and mutation databases

BioMutaiF3.
DMDMi135666.

Proteomic databases

EPDiP13726.
MaxQBiP13726.
PaxDbiP13726.
PeptideAtlasiP13726.
PRIDEiP13726.

Protocols and materials databases

DNASUi2152.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334047; ENSP00000334145; ENSG00000117525. [P13726-1]
ENST00000370207; ENSP00000359226; ENSG00000117525. [P13726-2]
GeneIDi2152.
KEGGihsa:2152.
UCSCiuc001dqr.4. human. [P13726-1]

Organism-specific databases

CTDi2152.
GeneCardsiF3.
HGNCiHGNC:3541. F3.
HPAiCAB009438.
HPA049292.
MIMi134390. gene.
neXtProtiNX_P13726.
PharmGKBiPA158.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IYA1. Eukaryota.
ENOG4111MW4. LUCA.
GeneTreeiENSGT00390000012668.
HOGENOMiHOG000043076.
HOVERGENiHBG005051.
InParanoidiP13726.
KOiK03901.
OMAiNTNEFLI.
OrthoDBiEOG091G0MKF.
PhylomeDBiP13726.
TreeFamiTF352627.

Enzyme and pathway databases

ReactomeiR-HSA-140834. Extrinsic Pathway of Fibrin Clot Formation.
SIGNORiP13726.

Miscellaneous databases

ChiTaRSiF3. human.
EvolutionaryTraceiP13726.
GeneWikiiTissue_factor.
GenomeRNAii2152.
PROiP13726.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117525.
CleanExiHS_F3.
GenevisibleiP13726. HS.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
IPR016354. Tissue_fac/coagulation_fac-3.
IPR001187. Tissue_factor.
IPR030472. Tissue_Factor_CS.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
PIRSFiPIRSF002498. Tissue_factor_3. 1 hit.
PRINTSiPR00346. TISSUEFACTOR.
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS00621. TISSUE_FACTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTF_HUMAN
AccessioniPrimary (citable) accession number: P13726
Secondary accession number(s): D3DT47, Q6FHG2, Q86WH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: September 7, 2016
This is version 186 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.