TFPI1_RABIT
ID TFPI1_RABIT Reviewed; 300 AA.
AC P19761; Q28828;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 131.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2136251; DOI=10.1093/nar/18.21.6440;
RA Wesselschmidt R.L., Girard T.J., Broze G.J. Jr.;
RT "cDNA sequence of rabbit lipoprotein-associated coagulation inhibitor.";
RL Nucleic Acids Res. 18:6440-6440(1990).
RN [2]
RP SEQUENCE REVISION TO 72; 211 AND 218.
RC TISSUE=Liver;
RX PubMed=1630940; DOI=10.1093/nar/20.13.3548;
RA Warn-Cramer B.J., Broze G.J. Jr., Komives E.A.;
RT "cDNA sequence of rabbit tissue factor pathway inhibitor.";
RL Nucleic Acids Res. 20:3548-3548(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=8503123; DOI=10.1016/0049-3848(93)90059-w;
RA Belaaouaj A., Kuppuswamy M.N., Birktoft J.J., Bajaj S.P.;
RT "Revised cDNA sequence of rabbit tissue factor pathway inhibitor.";
RL Thromb. Res. 69:547-553(1993).
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}.
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DR EMBL; X54708; CAA38515.1; ALT_SEQ; mRNA.
DR EMBL; S61902; AAB26836.1; -; mRNA.
DR PIR; I46937; I46937.
DR PIR; S12143; S12143.
DR RefSeq; NP_001095184.1; NM_001101714.1.
DR AlphaFoldDB; P19761; -.
DR SMR; P19761; -.
DR STRING; 9986.ENSOCUP00000007133; -.
DR MEROPS; I02.011; -.
DR MEROPS; I02.012; -.
DR MEROPS; I02.950; -.
DR ABCD; P19761; 34 sequenced antibodies.
DR GeneID; 100009401; -.
DR KEGG; ocu:100009401; -.
DR CTD; 7035; -.
DR eggNOG; KOG4295; Eukaryota.
DR InParanoid; P19761; -.
DR OrthoDB; 1009074at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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..24
FT CHAIN 25..300
FT /note="Tissue factor pathway inhibitor"
FT /id="PRO_0000016874"
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 213..263
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 223..224
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
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 213..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 222..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 238..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT CONFLICT 31
FT /note="Missing (in Ref. 3; AAB26836)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..272
FT /note="PKSI -> RNLS (in Ref. 3; AAB26836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 34436 MW; A08DE36537708CA6 CRC64;
MKKEHIFWTS ICLLLGLVPA PVSSAAEEDE EFTNITDIKP PLQKPTHSFC AMKVDDGPCR
AYIKRFFFNI LTHQCEEFIY GGCEGNENRF ESLEECKEKC ARDYPKMTTK LTFQKGKPDF
CFLEEDPGIC RGYITRYFYN NQSKQCERFK YGGCLGNLNN FESLEECKNT CENPTSDFQV
DDHRTQLNTV NNTLINQPTK APRRWAFHGP SWCLPPADRG LCQANEIRFF YNAIIGKCRP
FKYSGCGGNE NNFTSKKACI TACKKGFIPK SIKGGLIKTK RKKKKQPVKI TYVETFVKKT
