TFPI2_MOUSE
ID TFPI2_MOUSE Reviewed; 230 AA.
AC O35536;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Tissue factor pathway inhibitor 2;
DE Short=TFPI-2;
DE Flags: Precursor;
GN Name=Tfpi2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Placenta;
RX PubMed=8945635; DOI=10.1089/dna.1996.15.947;
RA Miyagi Y., Yasumitsu H., Mizushima H., Koshikawa N., Matsuda Y., Itoh H.,
RA Hori T., Aoki I., Misugi K., Miyazaki K.;
RT "Cloning of the cDNA encoding mouse PP5/TFPI-2 and mapping of the gene to
RT chromosome 6.";
RL DNA Cell Biol. 15:947-954(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10669168;
RA Kazama Y., Kamei S., Kuijper J.L., Foster D.C., Kisiel W.;
RT "Nucleotide sequence of the gene encoding murine tissue factor pathway
RT inhibitor-2.";
RL Thromb. Haemost. 83:141-147(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role in the regulation of plasmin-mediated matrix
CC remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and
CC weakly factor Xa. Has no effect on thrombin (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Finds in a complex with ABCB1, TFPI2 and PPP2R3C; leading to
CC the dephosphorylation of ABCB1. {ECO:0000250|UniProtKB:P48307}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta. Also expressed in
CC liver and kidney.
CC -!- DOMAIN: This inhibitor contains three inhibitory domains.
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DR EMBL; D50586; BAA22585.1; -; mRNA.
DR EMBL; AF180353; AAF40412.1; -; Genomic_DNA.
DR EMBL; BC021639; AAH21639.1; -; mRNA.
DR CCDS; CCDS19892.1; -.
DR RefSeq; NP_033390.1; NM_009364.4.
DR RefSeq; XP_011239357.1; XM_011241055.2.
DR AlphaFoldDB; O35536; -.
DR SMR; O35536; -.
DR STRING; 10090.ENSMUSP00000031674; -.
DR MEROPS; I02.013; -.
DR MEROPS; I02.951; -.
DR GlyGen; O35536; 2 sites.
DR PhosphoSitePlus; O35536; -.
DR CPTAC; non-CPTAC-3502; -.
DR PaxDb; O35536; -.
DR PRIDE; O35536; -.
DR ProteomicsDB; 258864; -.
DR Antibodypedia; 4115; 537 antibodies from 34 providers.
DR DNASU; 21789; -.
DR Ensembl; ENSMUST00000031674; ENSMUSP00000031674; ENSMUSG00000029664.
DR GeneID; 21789; -.
DR KEGG; mmu:21789; -.
DR UCSC; uc009avh.1; mouse.
DR CTD; 7980; -.
DR MGI; MGI:108543; Tfpi2.
DR VEuPathDB; HostDB:ENSMUSG00000029664; -.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000159917; -.
DR HOGENOM; CLU_058441_1_0_1; -.
DR InParanoid; O35536; -.
DR OMA; HKACEAF; -.
DR OrthoDB; 1009074at2759; -.
DR PhylomeDB; O35536; -.
DR TreeFam; TF315349; -.
DR BioGRID-ORCS; 21789; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tfpi2; mouse.
DR PRO; PR:O35536; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O35536; protein.
DR Bgee; ENSMUSG00000029664; Expressed in decidua and 95 other tissues.
DR ExpressionAtlas; O35536; baseline and differential.
DR Genevisible; O35536; MM.
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 GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR CDD; cd00109; KU; 2.
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 InterPro; IPR029860; TFPI2.
DR PANTHER; PTHR10083:SF352; PTHR10083:SF352; 1.
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; 2.
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..22
FT /evidence="ECO:0000250"
FT CHAIN 23..230
FT /note="Tissue factor pathway inhibitor 2"
FT /id="PRO_0000016877"
FT DOMAIN 36..86
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 96..146
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 156..206
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 46..47
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 106..107
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 166..167
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 45..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 61..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 96..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 105..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 121..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 156..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 165..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 181..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 230 AA; 26137 MW; 57EADB2E36521C7B CRC64;
MDPAMPLQLW NLPLLLVGSV LGLTSVSAQG NNLEICLLPL DAGPCQALIP KFYYDRDQQK
CRRFNYGGCL GNANNFHSRD LCQQTCGSIE KVPPVCRSEL KTYPCDKPNI RFFFNLNTMT
CEPLRPGLCS RTINVFSEEA TCKGLCEPRK HIPSFCSSPK DEGLCSANVT RFYFNSRNKT
CETFTYTGCG GNENNFYYLD ACHRACVKGW KKPKRWKIGD FLPRFWKHLS
