ID   TFPI1_MOUSE             Reviewed;         306 AA.
AC   O54819; Q9Z2U8;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 189.
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   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] (ISOFORM ALPHA).
RC   STRAIN=129;
RX   PubMed=9493581;
RA   Chang J.-Y., Monroe D.M., Oliver J.A., Liles D.K., Roberts H.R.;
RT   "Cloning, expression, and characterization of mouse tissue factor pathway
RT   inhibitor (TFPI).";
RL   Thromb. Haemost. 79:306-309(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RX   PubMed=9974373;
RA   Chang J.-Y., Monroe D.M., Oliver J.A., Roberts H.R.;
RT   "TFPIbeta, a second product from the mouse tissue factor pathway inhibitor
RT   (TFPI) gene.";
RL   Thromb. Haemost. 81:45-49(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha; Synonyms=TFPIalpha;
CC         IsoId=O54819-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=TFPIbeta;
CC         IsoId=O54819-2; Sequence=VSP_003032, VSP_003033;
CC   -!- TISSUE SPECIFICITY: Isoform alpha is expressed in heart and spleen;
CC       isoform beta in heart and lung.
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; AF004833; AAC40035.1; -; mRNA.
DR   EMBL; AF016313; AAD01586.1; -; mRNA.
DR   EMBL; AK028356; BAC25901.1; -; mRNA.
DR   CCDS; CCDS16185.1; -. [O54819-1]
DR   RefSeq; NP_035706.1; NM_011576.1. [O54819-1]
DR   RefSeq; XP_006499208.1; XM_006499145.2. [O54819-1]
DR   RefSeq; XP_006499209.1; XM_006499146.3.
DR   RefSeq; XP_006499210.1; XM_006499147.3.
DR   RefSeq; XP_006499211.1; XM_006499148.3.
DR   RefSeq; XP_006499212.1; XM_006499149.3. [O54819-2]
DR   AlphaFoldDB; O54819; -.
DR   SMR; O54819; -.
DR   STRING; 10090.ENSMUSP00000107347; -.
DR   ChEMBL; CHEMBL4523142; -.
DR   MEROPS; I02.011; -.
DR   GlyCosmos; O54819; 4 sites, No reported glycans.
DR   GlyGen; O54819; 4 sites.
DR   iPTMnet; O54819; -.
DR   PhosphoSitePlus; O54819; -.
DR   CPTAC; non-CPTAC-4064; -.
DR   MaxQB; O54819; -.
DR   PaxDb; 10090-ENSMUSP00000107347; -.
DR   PeptideAtlas; O54819; -.
DR   ProteomicsDB; 262802; -. [O54819-1]
DR   ProteomicsDB; 262803; -. [O54819-2]
DR   ABCD; O54819; 14 sequenced antibodies.
DR   Antibodypedia; 790; 1192 antibodies from 41 providers.
DR   DNASU; 21788; -.
DR   Ensembl; ENSMUST00000028487.10; ENSMUSP00000028487.4; ENSMUSG00000027082.16. [O54819-1]
DR   Ensembl; ENSMUST00000111718.8; ENSMUSP00000107347.2; ENSMUSG00000027082.16. [O54819-1]
DR   GeneID; 21788; -.
DR   KEGG; mmu:21788; -.
DR   UCSC; uc008kij.1; mouse. [O54819-1]
DR   UCSC; uc008kim.1; mouse. [O54819-2]
DR   AGR; MGI:1095418; -.
DR   CTD; 7035; -.
DR   MGI; MGI:1095418; Tfpi.
DR   VEuPathDB; HostDB:ENSMUSG00000027082; -.
DR   eggNOG; KOG4295; Eukaryota.
DR   GeneTree; ENSGT00940000160767; -.
DR   HOGENOM; CLU_058441_2_0_1; -.
DR   InParanoid; O54819; -.
DR   OMA; WWILCAV; -.
DR   OrthoDB; 3558236at2759; -.
DR   PhylomeDB; O54819; -.
DR   TreeFam; TF315349; -.
DR   Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   BioGRID-ORCS; 21788; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Tfpi; mouse.
DR   PRO; PR:O54819; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O54819; Protein.
DR   Bgee; ENSMUSG00000027082; Expressed in gastrula and 240 other cell types or tissues.
DR   ExpressionAtlas; O54819; baseline and differential.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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:0071383; P:cellular response to steroid hormone stimulus; IEA:Ensembl.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; ISO:MGI.
DR   CDD; cd22613; Kunitz_TFPI1_1-like; 1.
DR   CDD; cd22614; Kunitz_TFPI1_2-like; 1.
DR   CDD; cd22615; Kunitz_TFPI1_TFPI2_3-like; 1.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 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   PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR   PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 3.
DR   PIRSF; PIRSF001620; TFPI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 3.
DR   SUPFAM; SSF57362; BPTI-like; 3.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 3.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 3.
DR   Genevisible; O54819; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Blood coagulation; Disulfide bond; Glycoprotein;
KW   Hemostasis; Protease inhibitor; Reference proteome; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..306
FT                   /note="Tissue factor pathway inhibitor"
FT                   /id="PRO_0000016873"
FT   DOMAIN          50..100
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          121..171
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          225..275
FT                   /note="BPTI/Kunitz inhibitor 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            60..61
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            131..132
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            235..236
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        59..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        75..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        121..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        130..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        146..167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        225..275
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        234..258
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        250..271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   VAR_SEQ         218..253
FT                   /note="DYRGRPWCLQPADSGLCKASERRFYYNSATGKCHRF -> VTKEETNGGWKN
FT                   ADYTYQGFLSSVYIHVLYFVFRIG (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:9974373"
FT                   /id="VSP_003032"
FT   VAR_SEQ         254..306
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:9974373"
FT                   /id="VSP_003033"
FT   CONFLICT        68
FT                   /note="F -> L (in Ref. 2; AAD01586)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   306 AA;  34987 MW;  D3EA3297E4B6A359 CRC64;
     MTYKMKKEYA FWATVCLLLS LVPEFLNALS EEADDTDSEL GSMKPLHTFC AMKADDGPCK
     AMIRSYFFNM YTHQCEEFIY GGCEGNENRF DTLEECKKTC IPGYEKTAVK AASGAERPDF
     CFLEEDPGLC RGYMKRYLYN NQTKQCERFV YGGCLGNRNN FETLDECKKI CENPVHSPSP
     VNEVQMSDYV TDGNTVTDRS TVNNIVVPQS PKVPRRRDYR GRPWCLQPAD SGLCKASERR
     FYYNSATGKC HRFNYTGCGG NNNNFTTRRR CLRSCKTGLI KNKSKGVVKI QRRKAPFVKV
     VYESIN
//