TFPI2_BOVIN
ID TFPI2_BOVIN Reviewed; 234 AA.
AC Q7YRQ8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tissue factor pathway inhibitor 2;
DE Short=TFPI-2;
DE Flags: Precursor;
GN Name=TFPI2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12921785; DOI=10.1016/s0003-9861(03)00332-1;
RA Du X., Deng F.-M., Chand H.S., Kisiel W.;
RT "Molecular cloning, expression, and characterization of bovine tissue
RT factor pathway inhibitor-2.";
RL Arch. Biochem. Biophys. 417:96-104(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000269|PubMed:12921785}.
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 {ECO:0000269|PubMed:12921785}.
CC -!- DOMAIN: This inhibitor contains three inhibitory domains.
CC {ECO:0000250}.
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DR EMBL; AY234861; AAO84035.1; -; mRNA.
DR EMBL; BC103205; AAI03206.1; -; mRNA.
DR RefSeq; NP_877589.1; NM_182788.1.
DR AlphaFoldDB; Q7YRQ8; -.
DR SMR; Q7YRQ8; -.
DR STRING; 9913.ENSBTAP00000021062; -.
DR MEROPS; I02.013; -.
DR MEROPS; I02.951; -.
DR PaxDb; Q7YRQ8; -.
DR Ensembl; ENSBTAT00000021062; ENSBTAP00000021062; ENSBTAG00000015844.
DR GeneID; 360007; -.
DR KEGG; bta:360007; -.
DR CTD; 7980; -.
DR VEuPathDB; HostDB:ENSBTAG00000015844; -.
DR VGNC; VGNC:35794; TFPI2.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000159917; -.
DR HOGENOM; CLU_058441_1_0_1; -.
DR InParanoid; Q7YRQ8; -.
DR OMA; HKACEAF; -.
DR OrthoDB; 1009074at2759; -.
DR TreeFam; TF315349; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000015844; Expressed in urethra and 103 other tissues.
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; 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; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..234
FT /note="Tissue factor pathway inhibitor 2"
FT /id="PRO_0000244394"
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 155..205
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 165..166
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
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 155..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 164..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 180..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 234 AA; 26675 MW; 401EEC84D589B422 CRC64;
MDSVRPLWLM LLSLLLVGTA LGDASQAPPG NNAEICLLPP DDGPCRARIP SYYYDRYTQS
CREFMYGGCE GNANNFETLE ACNEACWKIE KVPKICRLKV NKKQCGELRE QYFFNLSSMT
CKKFISGGCH SNENRFPDEA TCMDFCAPKR APVFCYSPKD EGLCSANVTR YYFNPRHKAC
EAFNYTGCGG NDNNFVNLKD CKRTCVKALK KEKNKKMPRL LLANRRLKIK KKQF
