TF_RABIT
ID TF_RABIT Reviewed; 292 AA.
AC P24055;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 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=Heart;
RX PubMed=1840552; DOI=10.1016/0378-1119(91)90184-d;
RA Andrews B.S., Rehemtulla A., Fowler B.J., Edgington T.S., Mackman N.;
RT "Conservation of tissue factor primary sequence among three mammalian
RT species.";
RL Gene 98:265-269(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-292.
RC STRAIN=New Zealand white; TISSUE=Brain;
RX PubMed=1746002;
RA Pawashe A., Ezekowitz M., Lin T.C., Horton R., Bach R., Konigsberg W.;
RT "Molecular cloning, characterization and expression of cDNA for rabbit
RT brain tissue factor.";
RL Thromb. Haemost. 66:315-320(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 36-240.
RX PubMed=9605315; DOI=10.1002/pro.5560070504;
RA Muller Y.A., Kelley R.F., de Vos A.M.;
RT "Hinge bending within the cytokine receptor superfamily revealed by the 2.4
RT A crystal structure of the extracellular domain of rabbit tissue factor.";
RL Protein Sci. 7:1106-1115(1998).
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 -!- TISSUE SPECIFICITY: Brain, heart.
CC -!- SIMILARITY: Belongs to the tissue factor family. {ECO:0000305}.
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DR EMBL; M55390; AAA63469.1; -; mRNA.
DR EMBL; X53521; CAA37597.1; -; mRNA.
DR PIR; JU0441; KFRB3.
DR RefSeq; NP_001075760.1; NM_001082291.1.
DR PDB; 1A21; X-ray; 2.35 A; A/B=33-251.
DR PDBsum; 1A21; -.
DR AlphaFoldDB; P24055; -.
DR SMR; P24055; -.
DR STRING; 9986.ENSOCUP00000004179; -.
DR GeneID; 100009127; -.
DR KEGG; ocu:100009127; -.
DR CTD; 2152; -.
DR eggNOG; ENOG502RA1F; Eukaryota.
DR HOGENOM; CLU_082139_0_0_1; -.
DR InParanoid; P24055; -.
DR OMA; KFTPYNQ; -.
DR OrthoDB; 1000890at2759; -.
DR TreeFam; TF352627; -.
DR EvolutionaryTrace; P24055; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0002541; P:activation of plasma proteins involved in acute inflammatory response; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
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 InterPro; IPR030472; Tissue_Factor_CS.
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.
DR PROSITE; PS00621; TISSUE_FACTOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT CHAIN 33..292
FT /note="Tissue factor"
FT /id="PRO_0000033640"
FT TOPO_DOM 33..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..126
FT /note="Fibronectin type-III 1"
FT DOMAIN 148..240
FT /note="Fibronectin type-III 2"
FT MOTIF 44..46
FT /note="WKS motif"
FT MOTIF 75..77
FT /note="WKS motif"
FT LIPID 274
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
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 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..87
FT DISULFID 216..239
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 76..88
FT /evidence="ECO:0007829|PDB:1A21"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1A21"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1A21"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:1A21"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 196..208
FT /evidence="ECO:0007829|PDB:1A21"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1A21"
SQ SEQUENCE 292 AA; 32738 MW; 4860A1CADBACCF71 CRC64;
MAPPTRLQVP RPGTAVPYTV LLGWLLAQVA RAADTTGRAY NLTWKSTNFK TILEWEPKSI
DHVYTVQIST RLENWKSKCF LTAETECDLT DEVVKDVGQT YMARVLSYPA RNGNTTGFPE
EPPFRNSPEF TPYLDTNLGQ PTIQSFEQVG TKLNVTVQDA RTLVRRNGTF LSLRAVFGKD
LNYTLYYWRA SSTGKKTATT NTNEFLIDVD KGENYCFSVQ AVIPSRKRKQ RSPESLTECT
SREQGRAREM FFIIGAVVVV ALLIIVLSVT VYKCRKARAG PSGKESSPLN IA
