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   27-MAR-2024, entry version 171.
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   GlyCosmos; P20352; 4 sites, No reported glycans.
DR   GlyGen; P20352; 4 sites.
DR   iPTMnet; P20352; -.
DR   PhosphoSitePlus; P20352; -.
DR   SwissPalm; P20352; -.
DR   jPOST; P20352; -.
DR   MaxQB; P20352; -.
DR   PaxDb; 10090-ENSMUSP00000029771; -.
DR   PeptideAtlas; P20352; -.
DR   ProteomicsDB; 262806; -.
DR   Pumba; P20352; -.
DR   ABCD; P20352; 1 sequenced antibody.
DR   DNASU; 14066; -.
DR   GeneID; 14066; -.
DR   KEGG; mmu:14066; -.
DR   UCSC; uc008ree.2; mouse.
DR   AGR; MGI:88381; -.
DR   CTD; 2152; -.
DR   MGI; MGI:88381; F3.
DR   eggNOG; ENOG502RA1F; Eukaryota.
DR   InParanoid; P20352; -.
DR   OrthoDB; 5321079at2759; -.
DR   PhylomeDB; P20352; -.
DR   TreeFam; TF352627; -.
DR   Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   BioGRID-ORCS; 14066; 3 hits in 79 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:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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: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: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:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR   GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR   GO; GO:0016485; P:protein processing; ISO:MGI.
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   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
//