TFPI1_MACMU
ID TFPI1_MACMU Reviewed; 304 AA.
AC Q28864;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
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; Synonyms=TFPI1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8089087; DOI=10.1093/oxfordjournals.jbchem.a124400;
RA Kamei S., Kamikubo Y., Hamuro T., Fujimoto H., Ishihara M., Yonemura H.,
RA Miyamoto S., Funatsu A., Enjyoji K., Abumiya T.;
RT "Amino acid sequence and inhibitory activity of rhesus monkey tissue factor
RT pathway inhibitor (TFPI): comparison with human TFPI.";
RL J. Biochem. 115:708-714(1994).
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 -!- SUBCELLULAR LOCATION: Secreted.
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}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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DR EMBL; S73337; AAB31955.1; -; mRNA.
DR PIR; JC2264; JC2264.
DR RefSeq; NP_001181951.1; NM_001195022.1.
DR AlphaFoldDB; Q28864; -.
DR SMR; Q28864; -.
DR STRING; 9544.ENSMMUP00000012353; -.
DR MEROPS; I02.012; -.
DR GeneID; 613026; -.
DR KEGG; mcc:613026; -.
DR CTD; 7035; -.
DR eggNOG; KOG4295; Eukaryota.
DR HOGENOM; CLU_058441_2_0_1; -.
DR InParanoid; Q28864; -.
DR OMA; CALKDEP; -.
DR OrthoDB; 1009074at2759; -.
DR TreeFam; TF315349; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
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 /evidence="ECO:0000250"
FT CHAIN 29..304
FT /note="Tissue factor pathway inhibitor"
FT /id="PRO_0000016872"
FT DOMAIN 54..104
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 125..175
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 217..267
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 64..65
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 135..136
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 227..228
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 63..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 79..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 125..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 134..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 150..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 217..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 226..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 242..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 304 AA; 35085 MW; 56E13B3FF16282B0 CRC64;
MIYTMKKVHA LWVSICLMLN LAPAPLNADS EEDEEYTIIT DTELPPLKLM HSFCAFKPDD
GPCKAIMKRF FFNIFTRQCE EFIYGGCGGN QNRFESMEEC KKVCTRDNVH RIIQTALQQE
KPDFCFLEED PGICRGYITR YFYNNQSKQC ERFKYGGCLG NMNNFETLEE CKNTCEDGLN
GFQVDNYGTQ LNAVNNSQTP QSTKVPSFFE FHGPSWCLAP ADRGLCRANE NRFYYNSVIG
KCRPFKYSGC GGNENNFTSK RECLRACKKG FIQRISKGGL IKTKRKRKKQ RVKIAYEEVF
VKNM
