TFPI1_MOUSE
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 03-AUG-2022, entry version 180.
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. [O54819-1]
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 GlyGen; O54819; 4 sites.
DR iPTMnet; O54819; -.
DR PhosphoSitePlus; O54819; -.
DR CPTAC; non-CPTAC-4064; -.
DR MaxQB; O54819; -.
DR PaxDb; O54819; -.
DR PeptideAtlas; O54819; -.
DR PRIDE; O54819; -.
DR ProteomicsDB; 262802; -. [O54819-1]
DR ProteomicsDB; 262803; -. [O54819-2]
DR ABCD; O54819; 14 sequenced antibodies.
DR Antibodypedia; 790; 734 antibodies from 41 providers.
DR DNASU; 21788; -.
DR Ensembl; ENSMUST00000028487; ENSMUSP00000028487; ENSMUSG00000027082. [O54819-1]
DR Ensembl; ENSMUST00000111718; ENSMUSP00000107347; ENSMUSG00000027082. [O54819-1]
DR GeneID; 21788; -.
DR KEGG; mmu:21788; -.
DR UCSC; uc008kij.1; mouse. [O54819-1]
DR UCSC; uc008kim.1; mouse. [O54819-2]
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; CALKDEP; -.
DR OrthoDB; 1009074at2759; -.
DR PhylomeDB; O54819; -.
DR TreeFam; TF315349; -.
DR Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR BioGRID-ORCS; 21788; 3 hits in 74 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 237 other tissues.
DR ExpressionAtlas; O54819; baseline and differential.
DR Genevisible; O54819; MM.
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; 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 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
