TF_MOUSE
ID TF_MOUSE Reviewed; 294 AA.
AC P20352;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 164.
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; Synonyms=Cf-3, Cf3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1985911; DOI=10.1016/s0021-9258(18)52463-7;
RA Ranganathan G., Blatti S.P., Subramaniam M., Fass D.N., Maihle N.J.,
RA Getz M.J.;
RT "Cloning of murine tissue factor and regulation of gene expression by
RT transforming growth factor type beta 1.";
RL J. Biol. Chem. 266:496-501(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=2761539; DOI=10.1128/mcb.9.6.2567-2573.1989;
RA Hartzell S., Ryder K., Lanahan A., Lau L.F., Nathans D.;
RT "A growth factor-responsive gene of murine BALB/c 3T3 cells encodes a
RT protein homologous to human tissue factor.";
RL Mol. Cell. Biol. 9:2567-2573(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37 AND ASN-57.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INDUCTION.
RX PubMed=23291174; DOI=10.1016/j.bbrc.2012.12.098;
RA Oishi K., Koyanagi S., Ohkura N.;
RT "The molecular clock regulates circadian transcription of tissue factor
RT gene.";
RL Biochem. Biophys. Res. Commun. 431:332-335(2013).
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 -!- INDUCTION: Expression in the liver oscillates in a circadian manner.
CC {ECO:0000269|PubMed:23291174}.
CC -!- SIMILARITY: Belongs to the tissue factor family. {ECO:0000305}.
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DR EMBL; M57896; AAA63400.1; -; mRNA.
DR EMBL; M26071; AAA40414.1; -; mRNA.
DR EMBL; BC016397; AAH16397.1; -; mRNA.
DR CCDS; CCDS17805.1; -.
DR PIR; A32318; KFMS3.
DR RefSeq; NP_034301.3; NM_010171.3.
DR AlphaFoldDB; P20352; -.
DR SMR; P20352; -.
DR ComplexPortal; CPX-279; Coagulation factor VIIa - tissue factor complex.
DR STRING; 10090.ENSMUSP00000029771; -.
DR ChEMBL; CHEMBL5787; -.
DR GlyGen; P20352; 4 sites.
DR iPTMnet; P20352; -.
DR PhosphoSitePlus; P20352; -.
DR SwissPalm; P20352; -.
DR jPOST; P20352; -.
DR MaxQB; P20352; -.
DR PaxDb; P20352; -.
DR PeptideAtlas; P20352; -.
DR PRIDE; P20352; -.
DR ProteomicsDB; 262806; -.
DR ABCD; P20352; 1 sequenced antibody.
DR DNASU; 14066; -.
DR GeneID; 14066; -.
DR KEGG; mmu:14066; -.
DR UCSC; uc008ree.2; mouse.
DR CTD; 2152; -.
DR MGI; MGI:88381; F3.
DR eggNOG; ENOG502RA1F; Eukaryota.
DR InParanoid; P20352; -.
DR OrthoDB; 1000890at2759; -.
DR PhylomeDB; P20352; -.
DR TreeFam; TF352627; -.
DR Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR BioGRID-ORCS; 14066; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Olfr54; mouse.
DR PRO; PR:P20352; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P20352; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR GO; GO:1905286; C:serine-type peptidase complex; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0002543; P:activation of blood coagulation via clotting cascade; IC:ComplexPortal.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0002541; P:activation of plasma proteins involved in acute inflammatory response; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; ISO:MGI.
DR GO; GO:0007598; P:blood coagulation, extrinsic pathway; IC:ComplexPortal.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IC:ComplexPortal.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IC:ComplexPortal.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; IC:ComplexPortal.
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 Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT CHAIN 29..294
FT /note="Tissue factor"
FT /id="PRO_0000033639"
FT TOPO_DOM 29..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 245..247
FT /note="WKS motif"
FT LIPID 275
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..83
FT /evidence="ECO:0000250"
FT DISULFID 218..241
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="I -> T (in Ref. 2; AAA40414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 32935 MW; A306101293C31FA0 CRC64;
MAILVRPRLL AALAPTFLGC LLLQVIAGAG IPEKAFNLTW ISTDFKTILE WQPKPTNYTY
TVQISDRSRN WKNKCFSTTD TECDLTDEIV KDVTWAYEAK VLSVPRRNSV HGDGDQLVIH
GEEPPFTNAP KFLPYRDTNL GQPVIQQFEQ DGRKLNVVVK DSLTLVRKNG TFLTLRQVFG
KDLGYIITYR KGSSTGKKTN ITNTNEFSID VEEGVSYCFF VQAMIFSRKT NQNSPGSSTV
CTEQWKSFLG ETLIIVGAVV LLATIFIILL SISLCKRRKN RAGQKGKNTP SRLA
