TFPI1_RAT
ID TFPI1_RAT Reviewed; 302 AA.
AC Q02445;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Tissue factor pathway inhibitor;
DE Short=TFPI;
DE AltName: Full=Extrinsic pathway inhibitor;
DE Short=EPI;
DE AltName: Full=Lipoprotein-associated coagulation inhibitor;
DE Short=LACI;
DE Flags: Precursor;
GN Name=Tfpi;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1639767; DOI=10.1093/oxfordjournals.jbchem.a123818;
RA Enjyoji K., Emi M., Mukai T., Kato H.;
RT "cDNA cloning and expression of rat tissue factor pathway inhibitor
RT (TFPI).";
RL J. Biochem. 111:681-687(1992).
CC -!- FUNCTION: Inhibits factor X (X(a)) directly and, in a Xa-dependent way,
CC inhibits VIIa/tissue factor activity, presumably by forming a
CC quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic
CC action and also the ability to associate with lipoproteins in plasma
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Most abundant in heart, lung, kidney, and aortic
CC endothelial cells.
CC -!- DOMAIN: This inhibitor contains three inhibitory domains. The first
CC domain interacts with VIIa and TF, the second one with Xa (By
CC similarity). {ECO:0000250}.
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DR EMBL; D10926; BAA01724.1; -; mRNA.
DR PIR; JX0213; TIRTGK.
DR RefSeq; NP_058896.1; NM_017200.1.
DR RefSeq; XP_006234502.1; XM_006234440.3.
DR RefSeq; XP_006234503.1; XM_006234441.2.
DR RefSeq; XP_006234506.1; XM_006234444.2.
DR AlphaFoldDB; Q02445; -.
DR SMR; Q02445; -.
DR BioGRID; 248083; 1.
DR STRING; 10116.ENSRNOP00000006787; -.
DR MEROPS; I02.011; -.
DR MEROPS; I02.012; -.
DR MEROPS; I02.950; -.
DR GlyGen; Q02445; 3 sites.
DR PaxDb; Q02445; -.
DR PRIDE; Q02445; -.
DR Ensembl; ENSRNOT00000100291; ENSRNOP00000078992; ENSRNOG00000005039.
DR GeneID; 29436; -.
DR KEGG; rno:29436; -.
DR UCSC; RGD:61914; rat.
DR CTD; 7035; -.
DR RGD; 61914; Tfpi.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000160767; -.
DR HOGENOM; CLU_058441_2_0_1; -.
DR InParanoid; Q02445; -.
DR OMA; CALKDEP; -.
DR OrthoDB; 1009074at2759; -.
DR PhylomeDB; Q02445; -.
DR TreeFam; TF315349; -.
DR Reactome; R-RNO-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR PRO; PR:Q02445; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005039; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q02445; baseline and differential.
DR Genevisible; Q02445; RN.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:RGD.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR CDD; cd00109; KU; 3.
DR Gene3D; 4.10.410.10; -; 3.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR008296; TFPI-like.
DR Pfam; PF00014; Kunitz_BPTI; 3.
DR PIRSF; PIRSF001620; TFPI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 3.
DR SUPFAM; SSF57362; SSF57362; 3.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 3.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 3.
PE 2: Evidence at transcript level;
KW Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis;
KW Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..28
FT CHAIN 29..302
FT /note="Tissue factor pathway inhibitor"
FT /id="PRO_0000016875"
FT DOMAIN 53..103
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 124..174
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 222..272
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 63..64
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 134..135
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 232..233
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 62..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 78..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 124..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 133..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 149..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 222..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 231..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 247..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 302 AA; 34554 MW; F9AE82130A24A59F CRC64;
MTNKLKKDHA FWAAVCLLLS IVPELLNALP EEDDDTINTD SELRPMKPLH TFCAMKAEDG
PCKAMIRSYY FNMNSHQCEE FIYGGCRGNK NRFDTLEECR KTCIPGYKKT TIKTTSGAEK
PDFCFLEEDP GICRGFMTRY FYNNQSKQCE QFKYGGCLGN SNNFETLEEC RNTCEDPVNE
VQKGDYVTNQ ITVTDRTTVN NVVIPQATKA PSQWDYDGPS WCLEPADSGL CKASEKRFYY
NPAIGKCRQF NYTGCGGNNN NFTTKQDCNR ACKKDSSKKS SKRAKTQRRR KSFVKVMYEN
IH
