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Tissue factor pathway inhibitor (TFPI) (Extrinsic pathway inhibitor) (EPI) (Lipoprotein-associated coagulation inhibitor) (LACI)

 TFPI1_HUMAN             Reviewed;         304 AA.
P10646; O95103; Q53TS4;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
18-JUL-2018, entry version 216.
RecName: Full=Tissue factor pathway inhibitor;
Short=TFPI;
AltName: Full=Extrinsic pathway inhibitor;
Short=EPI;
AltName: Full=Lipoprotein-associated coagulation inhibitor;
Short=LACI;
Flags: Precursor;
Name=TFPI; Synonyms=LACI, TFPI1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
PubMed=2452157;
Wun T.-C., Kretzmer K.K., Girard T.J., Miletich J.P., Broze G.J. Jr.;
"Cloning and characterization of a cDNA coding for the lipoprotein-
associated coagulation inhibitor shows that it consists of three
tandem Kunitz-type inhibitory domains.";
J. Biol. Chem. 263:6001-6004(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
PubMed=2781520; DOI=10.1016/0049-3848(89)90454-4;
Girard T.J., Warren L.A., Novotny W.F., Bejcek B.E., Miletich J.P.,
Broze G.J. Jr.;
"Identification of the 1.4 kb and 4.0 kb messages for the lipoprotein
associated coagulation inhibitor and expression of the encoded
protein.";
Thromb. Res. 55:37-50(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
PubMed=1993173; DOI=10.1021/bi00220a018;
van der Logt C.P.E., Reitsma P.H., Bertina R.M.;
"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.";
Biochemistry 30:1571-1577(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
PubMed=2002045;
Girard T.J., Eddy R., Wesselschmidt R.L., Macphail L.A., Likert K.M.,
Byers M.G., Shows T.B., Broze G.J. Jr.;
"Structure of the human lipoprotein-associated coagulation inhibitor
gene. Intro/exon gene organization and localization of the gene to
chromosome 2.";
J. Biol. Chem. 266:5036-5041(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
Chang J.-Y., Monroe D.M., Roberts H.R.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 29-304, IDENTIFICATION BY MASS SPECTROMETRY, AND
GLYCOSYLATION AT THR-42; ASN-145; ASN-195; SER-202 AND THR-203.
PubMed=19017259; DOI=10.1111/j.1538-7836.2008.03222.x;
Mori Y., Hamuro T., Nakashima T., Hamamoto T., Natsuka S., Hase S.,
Iwanaga S.;
"Biochemical characterization of plasma-derived tissue factor pathway
inhibitor: post-translational modification of free, full-length form
with particular reference to the sugar chain.";
J. Thromb. Haemost. 7:111-120(2009).
[11]
PROTEIN SEQUENCE OF 29-50.
PubMed=2553722;
Novotny W.F., Girard T.J., Miletich J.P., Broze G.J. Jr.;
"Purification and characterization of the lipoprotein-associated
coagulation inhibitor from human plasma.";
J. Biol. Chem. 264:18832-18837(1989).
[12]
PROTEIN SEQUENCE OF 29-43.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[13]
INHIBITORY SITES.
PubMed=2927510; DOI=10.1038/338518a0;
Girard T.J., Warren L.A., Novotny W.F., Likert K.M., Brown S.G.,
Miletich J.P., Broze G.J. Jr.;
"Functional significance of the Kunitz-type inhibitory domains of
lipoprotein-associated coagulation inhibitor.";
Nature 338:518-520(1989).
[14]
GLYCOSYLATION AT ASN-145; ASN-195; SER-202 AND THR-203.
PubMed=8639592; DOI=10.1021/bi9524880;
Nakahara Y., Miyata T., Hamuro T., Funatsu A., Miyagi M.,
Tsunasawa S., Kato H.;
"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.";
Biochemistry 35:6450-6459(1996).
[15]
REVIEW.
PubMed=2271516; DOI=10.1021/bi00485a001;
Broze G.J. Jr., Girard T.J., Novotny W.F.;
"Regulation of coagulation by a multivalent Kunitz-type inhibitor.";
Biochemistry 29:7539-7546(1990).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
SUBCELLULAR LOCATION (ISOFORM BETA), AND GPI-ANCHOR.
PubMed=22144186; DOI=10.1182/blood-2011-10-388512;
Girard T.J., Tuley E., Broze G.J. Jr.;
"TFPIbeta is the GPI-anchored TFPI isoform on human endothelial cells
and placental microsomes.";
Blood 119:1256-1262(2012).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 121-178 IN COMPLEX WITH
TRYPSIN.
PubMed=9242660; DOI=10.1074/jbc.272.32.19931;
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.;
"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.";
J. Biol. Chem. 272:19931-19937(1997).
[20]
STRUCTURE BY NMR OF 121-182.
PubMed=9199408; DOI=10.1006/jmbi.1997.1029;
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.;
"The second Kunitz domain of human tissue factor pathway inhibitor:
cloning, structure determination and interaction with factor Xa.";
J. Mol. Biol. 269:395-407(1997).
[21]
STRUCTURE BY NMR OF 210-270.
PubMed=11772005; DOI=10.1021/bi011299g;
Mine S., Yamazaki T., Miyata T., Hara S., Kato H.;
"Structural mechanism for heparin-binding of the third Kunitz domain
of human tissue factor pathway inhibitor.";
Biochemistry 41:78-85(2002).
[22]
VARIANT MET-292.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[23]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
-!- FUNCTION: 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.
-!- SUBCELLULAR LOCATION: Isoform Alpha: Secreted.
-!- SUBCELLULAR LOCATION: Isoform Beta: Microsome membrane
{ECO:0000269|PubMed:22144186}; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:22144186}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha; Synonyms=TFPIalpha;
IsoId=P10646-1; Sequence=Displayed;
Name=Beta; Synonyms=TFPIbeta;
IsoId=P10646-2; Sequence=VSP_003030, VSP_003031;
Note=GPI-anchored.;
-!- TISSUE SPECIFICITY: Mostly in endothelial cells.
-!- DOMAIN: This inhibitor contains three inhibitory domains. The
first domain interacts with VIIa and TF, the second one with Xa.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592}.
-!- WEB RESOURCE: Name=Wikipedia; Note=TFPI entry;
URL="https://en.wikipedia.org/wiki/TFPI";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tfpi/";
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EMBL; J03225; AAA52022.1; -; mRNA.
EMBL; M58650; AAA59480.1; -; Genomic_DNA.
EMBL; M58644; AAA59480.1; JOINED; Genomic_DNA.
EMBL; M58645; AAA59480.1; JOINED; Genomic_DNA.
EMBL; M58646; AAA59480.1; JOINED; Genomic_DNA.
EMBL; M58647; AAA59480.1; JOINED; Genomic_DNA.
EMBL; M58648; AAA59480.1; JOINED; Genomic_DNA.
EMBL; M58649; AAA59480.1; JOINED; Genomic_DNA.
EMBL; M59499; AAA59526.1; -; Genomic_DNA.
EMBL; M59493; AAA59526.1; JOINED; Genomic_DNA.
EMBL; M59494; AAA59526.1; JOINED; Genomic_DNA.
EMBL; M59495; AAA59526.1; JOINED; Genomic_DNA.
EMBL; M59496; AAA59526.1; JOINED; Genomic_DNA.
EMBL; M59497; AAA59526.1; JOINED; Genomic_DNA.
EMBL; M59498; AAA59526.1; JOINED; Genomic_DNA.
EMBL; AF021834; AAD01700.1; -; mRNA.
EMBL; AY263365; AAO89075.1; -; Genomic_DNA.
EMBL; AC007319; AAY14807.1; -; Genomic_DNA.
EMBL; CH471058; EAX10921.1; -; Genomic_DNA.
EMBL; CH471058; EAX10922.1; -; Genomic_DNA.
EMBL; BC015514; AAH15514.1; -; mRNA.
CCDS; CCDS2294.1; -. [P10646-1]
CCDS; CCDS33349.1; -. [P10646-2]
PIR; A23712; TIHUGK.
RefSeq; NP_001027452.1; NM_001032281.3. [P10646-2]
RefSeq; NP_001305870.1; NM_001318941.2. [P10646-2]
RefSeq; NP_001316168.1; NM_001329239.1. [P10646-1]
RefSeq; NP_001316169.1; NM_001329240.1. [P10646-1]
RefSeq; NP_001316170.1; NM_001329241.1. [P10646-1]
RefSeq; NP_006278.1; NM_006287.5. [P10646-1]
RefSeq; XP_005246876.1; XM_005246819.1. [P10646-1]
RefSeq; XP_006712783.1; XM_006712720.3. [P10646-1]
RefSeq; XP_011510011.1; XM_011511709.2. [P10646-1]
UniGene; Hs.516578; -.
PDB; 1ADZ; NMR; -; A=118-182.
PDB; 1IRH; NMR; -; A=210-270.
PDB; 1TFX; X-ray; 2.60 A; C/D=121-178.
PDB; 4BQD; X-ray; 2.48 A; A/B=29-107.
PDB; 4DTG; X-ray; 1.80 A; K=119-178.
PDB; 5NMV; X-ray; 1.65 A; K=29-107.
PDBsum; 1ADZ; -.
PDBsum; 1IRH; -.
PDBsum; 1TFX; -.
PDBsum; 4BQD; -.
PDBsum; 4DTG; -.
PDBsum; 5NMV; -.
ProteinModelPortal; P10646; -.
SMR; P10646; -.
BioGrid; 112893; 13.
CORUM; P10646; -.
STRING; 9606.ENSP00000233156; -.
ChEMBL; CHEMBL3713062; -.
DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DrugBank; DB06779; Dalteparin.
MEROPS; I02.950; -.
GlyConnect; 602; -.
iPTMnet; P10646; -.
PhosphoSitePlus; P10646; -.
UniCarbKB; P10646; -.
BioMuta; TFPI; -.
DMDM; 125932; -.
EPD; P10646; -.
MaxQB; P10646; -.
PaxDb; P10646; -.
PeptideAtlas; P10646; -.
PRIDE; P10646; -.
ProteomicsDB; 52636; -.
ProteomicsDB; 52637; -. [P10646-2]
DNASU; 7035; -.
Ensembl; ENST00000233156; ENSP00000233156; ENSG00000003436. [P10646-1]
Ensembl; ENST00000339091; ENSP00000342306; ENSG00000003436. [P10646-2]
Ensembl; ENST00000392365; ENSP00000376172; ENSG00000003436. [P10646-1]
Ensembl; ENST00000409676; ENSP00000386344; ENSG00000003436. [P10646-2]
GeneID; 7035; -.
KEGG; hsa:7035; -.
UCSC; uc002upy.4; human. [P10646-1]
CTD; 7035; -.
DisGeNET; 7035; -.
EuPathDB; HostDB:ENSG00000003436.14; -.
GeneCards; TFPI; -.
HGNC; HGNC:11760; TFPI.
HPA; CAB020842; -.
HPA; HPA005575; -.
MIM; 152310; gene.
neXtProt; NX_P10646; -.
OpenTargets; ENSG00000003436; -.
PharmGKB; PA36475; -.
eggNOG; KOG4295; Eukaryota.
eggNOG; ENOG410XQNP; LUCA.
GeneTree; ENSGT00740000114929; -.
HOGENOM; HOG000231818; -.
HOVERGEN; HBG056804; -.
InParanoid; P10646; -.
KO; K03909; -.
OMA; FIQRISK; -.
OrthoDB; EOG091G14M8; -.
PhylomeDB; P10646; -.
TreeFam; TF315349; -.
Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation.
SIGNOR; P10646; -.
ChiTaRS; TFPI; human.
EvolutionaryTrace; P10646; -.
GeneWiki; Tissue_factor_pathway_inhibitor; -.
GenomeRNAi; 7035; -.
PMAP-CutDB; P10646; -.
PRO; PR:P10646; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000003436; -.
CleanEx; HS_TFPI; -.
ExpressionAtlas; P10646; baseline and differential.
Genevisible; P10646; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0007598; P:blood coagulation, extrinsic pathway; TAS:Reactome.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IEP:UniProtKB.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
CDD; cd00109; KU; 3.
Gene3D; 4.10.410.10; -; 3.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
InterPro; IPR008296; TFPI-like.
InterPro; IPR029864; TFPI1.
PANTHER; PTHR10083:SF317; PTHR10083:SF317; 1.
Pfam; PF00014; Kunitz_BPTI; 3.
PIRSF; PIRSF001620; TFPI; 1.
PRINTS; PR00759; BASICPTASE.
SMART; SM00131; KU; 3.
SUPFAM; SSF57362; SSF57362; 3.
PROSITE; PS00280; BPTI_KUNITZ_1; 3.
PROSITE; PS50279; BPTI_KUNITZ_2; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; GPI-anchor; Hemostasis;
Lipoprotein; Membrane; Microsome; Polymorphism; Protease inhibitor;
Reference proteome; Repeat; Secreted; Serine protease inhibitor;
Signal.
SIGNAL 1 28 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:19017259,
ECO:0000269|PubMed:2553722}.
CHAIN 29 304 Tissue factor pathway inhibitor.
{ECO:0000269|PubMed:2452157}.
/FTId=PRO_0000016871.
DOMAIN 54 104 BPTI/Kunitz inhibitor 1.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DOMAIN 125 175 BPTI/Kunitz inhibitor 2.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DOMAIN 217 267 BPTI/Kunitz inhibitor 3.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
SITE 64 65 Reactive bond.
SITE 135 136 Reactive bond.
SITE 227 228 Reactive bond.
SITE 256 256 Not glycosylated.
CARBOHYD 42 42 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:19017259}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19017259,
ECO:0000269|PubMed:8639592}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19017259,
ECO:0000269|PubMed:8639592}.
CARBOHYD 202 202 O-linked (GalNAc...) serine; partial.
{ECO:0000269|PubMed:19017259,
ECO:0000269|PubMed:8639592}.
CARBOHYD 203 203 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19017259,
ECO:0000269|PubMed:8639592}.
DISULFID 54 104 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 63 87 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 79 100 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 125 175
DISULFID 134 158
DISULFID 150 171
DISULFID 217 267
DISULFID 226 250
DISULFID 242 263
VAR_SEQ 210 251 EFHGPSWCLTPADRGLCRANENRFYYNSVIGKCRPFKYSGC
G -> VTKEGTNDGWKNAAHIYQVFLNAFCIHASMFFLGLD
SISCLC (in isoform Beta).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_003030.
VAR_SEQ 252 304 Missing (in isoform Beta).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_003031.
VARIANT 292 292 V -> M (in dbSNP:rs5940).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_012004.
MUTAGEN 64 64 K->I: Abolishes inhibition of VII(a)/TF.
MUTAGEN 135 135 R->L: Abolishes inhibition of X(a).
MUTAGEN 227 227 R->L: Abolishes inhibition of VII(a)/TF.
STRAND 31 39 {ECO:0000244|PDB:4BQD}.
HELIX 51 55 {ECO:0000244|PDB:5NMV}.
STRAND 67 73 {ECO:0000244|PDB:5NMV}.
TURN 74 77 {ECO:0000244|PDB:5NMV}.
STRAND 78 84 {ECO:0000244|PDB:5NMV}.
STRAND 94 96 {ECO:0000244|PDB:5NMV}.
HELIX 97 104 {ECO:0000244|PDB:5NMV}.
STRAND 112 115 {ECO:0000244|PDB:1ADZ}.
HELIX 123 126 {ECO:0000244|PDB:4DTG}.
STRAND 138 144 {ECO:0000244|PDB:4DTG}.
TURN 145 148 {ECO:0000244|PDB:4DTG}.
STRAND 149 155 {ECO:0000244|PDB:4DTG}.
STRAND 157 159 {ECO:0000244|PDB:4DTG}.
STRAND 165 167 {ECO:0000244|PDB:4DTG}.
HELIX 168 175 {ECO:0000244|PDB:4DTG}.
STRAND 178 180 {ECO:0000244|PDB:1ADZ}.
STRAND 215 219 {ECO:0000244|PDB:1IRH}.
STRAND 224 226 {ECO:0000244|PDB:1IRH}.
STRAND 232 235 {ECO:0000244|PDB:1IRH}.
TURN 237 239 {ECO:0000244|PDB:1IRH}.
STRAND 241 245 {ECO:0000244|PDB:1IRH}.
STRAND 257 260 {ECO:0000244|PDB:1IRH}.
HELIX 261 267 {ECO:0000244|PDB:1IRH}.
SEQUENCE 304 AA; 35015 MW; 5281E32B758B44FE CRC64;
MIYTMKKVHA LWASVCLLLN LAPAPLNADS EEDEEHTIIT DTELPPLKLM HSFCAFKADD
GPCKAIMKRF FFNIFTRQCE EFIYGGCEGN QNRFESLEEC KKMCTRDNAN RIIKTTLQQE
KPDFCFLEED PGICRGYITR YFYNNQTKQC ERFKYGGCLG NMNNFETLEE CKNICEDGPN
GFQVDNYGTQ LNAVNNSLTP QSTKVPSLFE FHGPSWCLTP ADRGLCRANE NRFYYNSVIG
KCRPFKYSGC GGNENNFTSK QECLRACKKG FIQRISKGGL IKTKRKRKKQ RVKIAYEEIF
VKNM


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