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Protein

Tissue factor pathway inhibitor

Gene

TFPI

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

Functioni

Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei64 – 652Reactive bond
Sitei135 – 1362Reactive bond
Sitei227 – 2282Reactive bond
Sitei256 – 2561Not glycosylated

GO - Molecular functioni

  • endopeptidase inhibitor activity Source: ProtInc
  • serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_1573. Extrinsic Pathway of Fibrin Clot Formation.

Protein family/group databases

MEROPSiI02.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Tissue factor pathway inhibitor
Short name:
TFPI
Alternative name(s):
Extrinsic pathway inhibitor
Short name:
EPI
Lipoprotein-associated coagulation inhibitor
Short name:
LACI
Gene namesi
Name:TFPI
Synonyms:LACI, TFPI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11760. TFPI.

Subcellular locationi

Isoform Beta :

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cell surface Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB-KW
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • organelle membrane Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641K → I: Abolishes inhibition of VII(a)/TF.
Mutagenesisi135 – 1351R → L: Abolishes inhibition of X(a).
Mutagenesisi227 – 2271R → L: Abolishes inhibition of VII(a)/TF.

Organism-specific databases

PharmGKBiPA36475.

Chemistry

DrugBankiDB00036. Coagulation factor VIIa.
DB06779. Dalteparin.

Polymorphism and mutation databases

BioMutaiTFPI.
DMDMi125932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28283 PublicationsAdd
BLAST
Chaini29 – 304276Tissue factor pathway inhibitor1 PublicationPRO_0000016871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421O-linked (GalNAc...); partial1 Publication
Disulfide bondi54 ↔ 104PROSITE-ProRule annotation
Disulfide bondi63 ↔ 87PROSITE-ProRule annotation
Disulfide bondi79 ↔ 100PROSITE-ProRule annotation
Disulfide bondi125 ↔ 175
Disulfide bondi134 ↔ 158
Glycosylationi145 – 1451N-linked (GlcNAc...)3 Publications
Disulfide bondi150 ↔ 171
Glycosylationi195 – 1951N-linked (GlcNAc...)2 Publications
Glycosylationi202 – 2021O-linked (GalNAc...); partial2 Publications
Glycosylationi203 – 2031O-linked (GalNAc...)2 Publications
Disulfide bondi217 ↔ 267
Disulfide bondi226 ↔ 250
Disulfide bondi242 ↔ 263

Post-translational modificationi

O-glycosylated.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP10646.
PaxDbiP10646.
PeptideAtlasiP10646.
PRIDEiP10646.

PTM databases

PhosphoSiteiP10646.
UniCarbKBiP10646.

Miscellaneous databases

PMAP-CutDBP10646.

Expressioni

Tissue specificityi

Mostly in endothelial cells.

Gene expression databases

BgeeiP10646.
CleanExiHS_TFPI.
ExpressionAtlasiP10646. baseline and differential.
GenevisibleiP10646. HS.

Organism-specific databases

HPAiCAB020842.
HPA005575.

Interactioni

Protein-protein interaction databases

BioGridi112893. 13 interactions.
STRINGi9606.ENSP00000233156.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 399Combined sources
Helixi52 – 554Combined sources
Beta strandi67 – 737Combined sources
Turni74 – 774Combined sources
Beta strandi78 – 847Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 1048Combined sources
Beta strandi118 – 1203Combined sources
Helixi123 – 1264Combined sources
Beta strandi138 – 1447Combined sources
Turni145 – 1484Combined sources
Beta strandi149 – 1557Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi165 – 1673Combined sources
Helixi168 – 1758Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi232 – 2354Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2455Combined sources
Beta strandi257 – 2604Combined sources
Helixi261 – 2677Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ADZNMR-A118-182[»]
1IRHNMR-A210-270[»]
1TFXX-ray2.60C/D121-178[»]
4BQDX-ray2.48A/B29-107[»]
4DTGX-ray1.80K119-178[»]
ProteinModelPortaliP10646.
SMRiP10646. Positions 30-107, 120-178, 210-270.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10646.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 10451BPTI/Kunitz inhibitor 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 17551BPTI/Kunitz inhibitor 2PROSITE-ProRule annotationAdd
BLAST
Domaini217 – 26751BPTI/Kunitz inhibitor 3PROSITE-ProRule annotationAdd
BLAST

Domaini

This inhibitor contains three inhibitory domains. The first domain interacts with VIIa and TF, the second one with Xa.

Sequence similaritiesi

Contains 3 BPTI/Kunitz inhibitor domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG86404.
GeneTreeiENSGT00740000114929.
HOGENOMiHOG000231818.
HOVERGENiHBG056804.
InParanoidiP10646.
KOiK03909.
OMAiFIQRISK.
OrthoDBiEOG73FQKT.
PhylomeDBiP10646.
TreeFamiTF315349.

Family and domain databases

Gene3Di4.10.410.10. 3 hits.
InterProiIPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR029864. TFPI1.
[Graphical view]
PANTHERiPTHR10083:SF204. PTHR10083:SF204. 1 hit.
PfamiPF00014. Kunitz_BPTI. 3 hits.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 3 hits.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 3 hits.
PROSITEiPS00280. BPTI_KUNITZ_1. 3 hits.
PS50279. BPTI_KUNITZ_2. 3 hits.
[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

Isoform Alpha (identifier: P10646-1) [UniParc]FASTAAdd to basket

Also known as: TFPIalpha

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
MIYTMKKVHA LWASVCLLLN LAPAPLNADS EEDEEHTIIT DTELPPLKLM
60 70 80 90 100
HSFCAFKADD GPCKAIMKRF FFNIFTRQCE EFIYGGCEGN QNRFESLEEC
110 120 130 140 150
KKMCTRDNAN RIIKTTLQQE KPDFCFLEED PGICRGYITR YFYNNQTKQC
160 170 180 190 200
ERFKYGGCLG NMNNFETLEE CKNICEDGPN GFQVDNYGTQ LNAVNNSLTP
210 220 230 240 250
QSTKVPSLFE FHGPSWCLTP ADRGLCRANE NRFYYNSVIG KCRPFKYSGC
260 270 280 290 300
GGNENNFTSK QECLRACKKG FIQRISKGGL IKTKRKRKKQ RVKIAYEEIF

VKNM
Length:304
Mass (Da):35,015
Last modified:July 1, 1989 - v1
Checksum:i5281E32B758B44FE
GO
Isoform Beta (identifier: P10646-2) [UniParc]FASTAAdd to basket

Also known as: TFPIbeta

The sequence of this isoform differs from the canonical sequence as follows:
     210-251: EFHGPSWCLT...CRPFKYSGCG → VTKEGTNDGW...LGLDSISCLC
     252-304: Missing.

Note: GPI-anchored.
Show »
Length:251
Mass (Da):28,653
Checksum:i9B3F276A52B4F0B9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti292 – 2921V → M.1 Publication
Corresponds to variant rs5940 [ dbSNP | Ensembl ].
VAR_012004

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei210 – 25142EFHGP…YSGCG → VTKEGTNDGWKNAAHIYQVF LNAFCIHASMFFLGLDSISC LC in isoform Beta. 2 PublicationsVSP_003030Add
BLAST
Alternative sequencei252 – 30453Missing in isoform Beta. 2 PublicationsVSP_003031Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03225 mRNA. Translation: AAA52022.1.
M58650
, M58644, M58645, M58646, M58647, M58648, M58649 Genomic DNA. Translation: AAA59480.1.
M59499
, M59493, M59494, M59495, M59496, M59497, M59498 Genomic DNA. Translation: AAA59526.1.
AF021834 mRNA. Translation: AAD01700.1.
AY263365 Genomic DNA. Translation: AAO89075.1.
AC007319 Genomic DNA. Translation: AAY14807.1.
CH471058 Genomic DNA. Translation: EAX10921.1.
CH471058 Genomic DNA. Translation: EAX10922.1.
BC015514 mRNA. Translation: AAH15514.1.
CCDSiCCDS2294.1. [P10646-1]
CCDS33349.1. [P10646-2]
PIRiA23712. TIHUGK.
RefSeqiNP_001027452.1. NM_001032281.2. [P10646-2]
NP_006278.1. NM_006287.4. [P10646-1]
XP_005246875.1. XM_005246818.1. [P10646-1]
XP_005246876.1. XM_005246819.1. [P10646-1]
XP_005246877.1. XM_005246820.1. [P10646-2]
XP_006712783.1. XM_006712720.2. [P10646-1]
XP_011510009.1. XM_011511707.1. [P10646-1]
XP_011510010.1. XM_011511708.1. [P10646-1]
XP_011510011.1. XM_011511709.1. [P10646-1]
UniGeneiHs.516578.

Genome annotation databases

EnsembliENST00000233156; ENSP00000233156; ENSG00000003436.
ENST00000339091; ENSP00000342306; ENSG00000003436. [P10646-2]
ENST00000392365; ENSP00000376172; ENSG00000003436.
ENST00000409676; ENSP00000386344; ENSG00000003436. [P10646-2]
GeneIDi7035.
KEGGihsa:7035.
UCSCiuc002upy.3. human. [P10646-1]
uc002uqa.2. human. [P10646-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

TFPI entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03225 mRNA. Translation: AAA52022.1.
M58650
, M58644, M58645, M58646, M58647, M58648, M58649 Genomic DNA. Translation: AAA59480.1.
M59499
, M59493, M59494, M59495, M59496, M59497, M59498 Genomic DNA. Translation: AAA59526.1.
AF021834 mRNA. Translation: AAD01700.1.
AY263365 Genomic DNA. Translation: AAO89075.1.
AC007319 Genomic DNA. Translation: AAY14807.1.
CH471058 Genomic DNA. Translation: EAX10921.1.
CH471058 Genomic DNA. Translation: EAX10922.1.
BC015514 mRNA. Translation: AAH15514.1.
CCDSiCCDS2294.1. [P10646-1]
CCDS33349.1. [P10646-2]
PIRiA23712. TIHUGK.
RefSeqiNP_001027452.1. NM_001032281.2. [P10646-2]
NP_006278.1. NM_006287.4. [P10646-1]
XP_005246875.1. XM_005246818.1. [P10646-1]
XP_005246876.1. XM_005246819.1. [P10646-1]
XP_005246877.1. XM_005246820.1. [P10646-2]
XP_006712783.1. XM_006712720.2. [P10646-1]
XP_011510009.1. XM_011511707.1. [P10646-1]
XP_011510010.1. XM_011511708.1. [P10646-1]
XP_011510011.1. XM_011511709.1. [P10646-1]
UniGeneiHs.516578.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ADZNMR-A118-182[»]
1IRHNMR-A210-270[»]
1TFXX-ray2.60C/D121-178[»]
4BQDX-ray2.48A/B29-107[»]
4DTGX-ray1.80K119-178[»]
ProteinModelPortaliP10646.
SMRiP10646. Positions 30-107, 120-178, 210-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112893. 13 interactions.
STRINGi9606.ENSP00000233156.

Chemistry

DrugBankiDB00036. Coagulation factor VIIa.
DB06779. Dalteparin.

Protein family/group databases

MEROPSiI02.011.

PTM databases

PhosphoSiteiP10646.
UniCarbKBiP10646.

Polymorphism and mutation databases

BioMutaiTFPI.
DMDMi125932.

Proteomic databases

MaxQBiP10646.
PaxDbiP10646.
PeptideAtlasiP10646.
PRIDEiP10646.

Protocols and materials databases

DNASUi7035.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233156; ENSP00000233156; ENSG00000003436.
ENST00000339091; ENSP00000342306; ENSG00000003436. [P10646-2]
ENST00000392365; ENSP00000376172; ENSG00000003436.
ENST00000409676; ENSP00000386344; ENSG00000003436. [P10646-2]
GeneIDi7035.
KEGGihsa:7035.
UCSCiuc002upy.3. human. [P10646-1]
uc002uqa.2. human. [P10646-2]

Organism-specific databases

CTDi7035.
GeneCardsiGC02M188328.
HGNCiHGNC:11760. TFPI.
HPAiCAB020842.
HPA005575.
MIMi152310. gene.
neXtProtiNX_P10646.
PharmGKBiPA36475.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG86404.
GeneTreeiENSGT00740000114929.
HOGENOMiHOG000231818.
HOVERGENiHBG056804.
InParanoidiP10646.
KOiK03909.
OMAiFIQRISK.
OrthoDBiEOG73FQKT.
PhylomeDBiP10646.
TreeFamiTF315349.

Enzyme and pathway databases

ReactomeiREACT_1573. Extrinsic Pathway of Fibrin Clot Formation.

Miscellaneous databases

ChiTaRSiTFPI. human.
EvolutionaryTraceiP10646.
GeneWikiiTissue_factor_pathway_inhibitor.
GenomeRNAii7035.
NextBioi27483.
PMAP-CutDBP10646.
PROiP10646.
SOURCEiSearch...

Gene expression databases

BgeeiP10646.
CleanExiHS_TFPI.
ExpressionAtlasiP10646. baseline and differential.
GenevisibleiP10646. HS.

Family and domain databases

Gene3Di4.10.410.10. 3 hits.
InterProiIPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR029864. TFPI1.
[Graphical view]
PANTHERiPTHR10083:SF204. PTHR10083:SF204. 1 hit.
PfamiPF00014. Kunitz_BPTI. 3 hits.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 3 hits.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 3 hits.
PROSITEiPS00280. BPTI_KUNITZ_1. 3 hits.
PS50279. BPTI_KUNITZ_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains."
    Wun T.-C., Kretzmer K.K., Girard T.J., Miletich J.P., Broze G.J. Jr.
    J. Biol. Chem. 263:6001-6004(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
  2. "Identification of the 1.4 kb and 4.0 kb messages for the lipoprotein associated coagulation inhibitor and expression of the encoded protein."
    Girard T.J., Warren L.A., Novotny W.F., Bejcek B.E., Miletich J.P., Broze G.J. Jr.
    Thromb. Res. 55:37-50(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
  3. "Intron-exon organization of the human gene coding for the lipoprotein-associated coagulation inhibitor: the factor Xa dependent inhibitor of the extrinsic pathway of coagulation."
    van der Logt C.P.E., Reitsma P.H., Bertina R.M.
    Biochemistry 30:1571-1577(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
  4. "Structure of the human lipoprotein-associated coagulation inhibitor gene. Intro/exon gene organization and localization of the gene to chromosome 2."
    Girard T.J., Eddy R., Wesselschmidt R.L., Macphail L.A., Likert K.M., Byers M.G., Shows T.B., Broze G.J. Jr.
    J. Biol. Chem. 266:5036-5041(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
  5. Chang J.-Y., Monroe D.M., Roberts H.R.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
  6. SeattleSNPs variation discovery resource
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
    Tissue: Pancreas.
  10. "Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain."
    Mori Y., Hamuro T., Nakashima T., Hamamoto T., Natsuka S., Hase S., Iwanaga S.
    J. Thromb. Haemost. 7:111-120(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-304, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT THR-42; ASN-145; ASN-195; SER-202 AND THR-203.
  11. "Purification and characterization of the lipoprotein-associated coagulation inhibitor from human plasma."
    Novotny W.F., Girard T.J., Miletich J.P., Broze G.J. Jr.
    J. Biol. Chem. 264:18832-18837(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-50.
  12. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-43.
  13. "Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor."
    Girard T.J., Warren L.A., Novotny W.F., Likert K.M., Brown S.G., Miletich J.P., Broze G.J. Jr.
    Nature 338:518-520(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITORY SITES.
  14. "Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: one N- and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2."
    Nakahara Y., Miyata T., Hamuro T., Funatsu A., Miyagi M., Tsunasawa S., Kato H.
    Biochemistry 35:6450-6459(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-145; ASN-195; SER-202 AND THR-203.
  15. "Regulation of coagulation by a multivalent Kunitz-type inhibitor."
    Broze G.J. Jr., Girard T.J., Novotny W.F.
    Biochemistry 29:7539-7546(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145.
    Tissue: Plasma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "TFPIbeta is the GPI-anchored TFPI isoform on human endothelial cells and placental microsomes."
    Girard T.J., Tuley E., Broze G.J. Jr.
    Blood 119:1256-1262(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM BETA), GPI-ANCHOR.
  19. "The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition."
    Stubbs M.T., Morenweiser R., Stuerzebecher J., Bauer M., Bode W., Huber R., Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H., Auerswald E.A.
    J. Biol. Chem. 272:19931-19937(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 121-178 IN COMPLEX WITH TRYPSIN.
  20. "The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa."
    Burgering M.J.M., Orbons L.P.M., van der Doelen A., Mulders J., Theunissen H.J.M., Grootenhuis P.D.J., Bode W., Huber R., Stubbs M.T.
    J. Mol. Biol. 269:395-407(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 121-182.
  21. "Structural mechanism for heparin-binding of the third Kunitz domain of human tissue factor pathway inhibitor."
    Mine S., Yamazaki T., Miyata T., Hara S., Kato H.
    Biochemistry 41:78-85(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 210-270.
  22. Cited for: VARIANT MET-292.

Entry informationi

Entry nameiTFPI1_HUMAN
AccessioniPrimary (citable) accession number: P10646
Secondary accession number(s): O95103, Q53TS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 22, 2015
This is version 192 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, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.