ID   TF_CAVPO                Reviewed;         289 AA.
AC   Q9JLU8;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Tissue factor;
DE            Short=TF;
DE   AltName: Full=Coagulation factor III;
DE   AltName: CD_antigen=CD142;
DE   Flags: Precursor;
GN   Name=F3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=10744153;
RA   Shi R.J., Li W.Z., Marder V.J., Sporn L.A.;
RT   "Cloning of guinea pig tissue factor cDNA: comparison of primary structure
RT   among six mammalian species.";
RL   Thromb. Haemost. 83:455-461(2000).
CC   -!- FUNCTION: Initiates blood coagulation by forming a complex with
CC       circulating factor VII or VIIa. The [TF:VIIa] complex activates factors
CC       IX or X by specific limited proteolysis. TF plays a role in normal
CC       hemostasis by initiating the cell-surface assembly and propagation of
CC       the coagulation protease cascade.
CC   -!- SUBUNIT: Interacts with HSPE; the interaction, inhibited by heparin,
CC       promotes the generation of activated factor X and activates coagulation
CC       in the presence of activated factor VII. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P13726}; Single-
CC       pass type I membrane protein {ECO:0000250|UniProtKB:P13726}.
CC   -!- SIMILARITY: Belongs to the tissue factor family. {ECO:0000305}.
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DR   EMBL; AF131949; AAF36523.1; -; mRNA.
DR   RefSeq; NP_001166375.1; NM_001172904.1.
DR   AlphaFoldDB; Q9JLU8; -.
DR   SMR; Q9JLU8; -.
DR   STRING; 10141.ENSCPOP00000001894; -.
DR   GeneID; 100135463; -.
DR   KEGG; cpoc:100135463; -.
DR   CTD; 2152; -.
DR   eggNOG; ENOG502RA1F; Eukaryota.
DR   InParanoid; Q9JLU8; -.
DR   OrthoDB; 1000890at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR   InterPro; IPR001187; Tissue_factor.
DR   PANTHER; PTHR20859:SF22; PTHR20859:SF22; 1.
DR   Pfam; PF09294; Interfer-bind; 1.
DR   Pfam; PF01108; Tissue_fac; 1.
DR   PIRSF; PIRSF002498; Tissue_factor_3; 1.
DR   PRINTS; PR00346; TISSUEFACTOR.
DR   SUPFAM; SSF49265; SSF49265; 2.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..289
FT                   /note="Tissue factor"
FT                   /id="PRO_0000033637"
FT   TOPO_DOM        33..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..289
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           44..46
FT                   /note="WKS motif"
FT   MOTIF           75..77
FT                   /note="WKS motif"
FT   LIPID           271
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..87
FT                   /evidence="ECO:0000250"
FT   DISULFID        213..236
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  32457 MW;  7AB97F8F58199FB1 CRC64;
     MTTPAWPRLP HPEIAVVPTL LLGWVLVQVA GAEGIPVKPY NLTWKSTNFK TILEWEPKPI
     NNVYTVQIST ALEDWKSICF SITATECDLT SEMAPNVQQT YLARVISLLP NSTGFLEDAV
     YSNSPEFTPY QETNLGQPKI ESFKLVGTKL NVTVRDTQTL ARSNGTFLSL RDIFGKNLQY
     MLYYWRSSTT GKKTAMTNTN EFLIDVDKGQ DYCFFVQAVI PSRKDNKKSP ESITVCTRLE
     KGKFREMSFI VVPVILVIIV VIALFLLVCK CRKAKARQSG KEGSPLNIA