ID A0A2K5VXA0_MACFA Unreviewed; 297 AA.
AC A0A2K5VXA0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Tissue factor {ECO:0000256|ARBA:ARBA00018722};
DE AltName: Full=Coagulation factor III {ECO:0000256|ARBA:ARBA00031171};
GN Name=F3 {ECO:0000313|Ensembl:ENSMFAP00000029349.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000029349.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000029349.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000029349.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00002201}.
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.
CC {ECO:0000256|ARBA:ARBA00011184}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the tissue factor family.
CC {ECO:0000256|ARBA:ARBA00009197}.
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DR AlphaFoldDB; A0A2K5VXA0; -.
DR Ensembl; ENSMFAT00000003545.2; ENSMFAP00000029349.2; ENSMFAG00000041937.2.
DR VEuPathDB; HostDB:ENSMFAG00000041937; -.
DR GeneTree; ENSGT00390000012668; -.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000041937; Expressed in heart and 13 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1905286; C:serine-type peptidase complex; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0002541; P:activation of plasma proteins involved in acute inflammatory response; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:Ensembl.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; INTERFERON/INTERLEUKIN RECEPTOR; 1.
DR PANTHER; PTHR20859:SF22; TISSUE FACTOR; 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; Fibronectin type III; 2.
DR PROSITE; PS00621; TISSUE_FACTOR; 1.
PE 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002498-1};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..115
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF01108"
FT DOMAIN 139..245
FT /note="Interferon/interleukin receptor"
FT /evidence="ECO:0000259|Pfam:PF09294"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 279
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002498-2"
FT DISULFID 82..90
FT /evidence="ECO:0000256|PIRSR:PIRSR002498-1"
FT DISULFID 219..243
FT /evidence="ECO:0000256|PIRSR:PIRSR002498-1"
SQ SEQUENCE 297 AA; 33417 MW; 94A495BE9DDACE71 CRC64;
TWRPLPGPGS RTPRPQSLGR SCSAGSSPRW PALQGTTNTV AAYNLTWKST NFKTILEWEP
KPINQVYTVQ ISTKSGDWKS KCFYTADTEC DLTDEIVKDV KQTYLARVFS YPAGHVESTG
STEEPPYENS PEFTPYLETN LGQPTIQSFE QVGTKVNVTV QDEWTLVRRN DTFLSLRDVF
GKDLIYTLYY WKSSSSGKKT AKTNTNEFLI DVDKGENYCF SVQAVIPSRR TANRKSTDSP
VECMGHEKGE SREIFYIIGA VVFVVIILVI ILAISLHKCK KARVGRSWKE NSPLNVA
//
