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TF_BOVIN
ID   TF_BOVIN                Reviewed;         292 AA.
AC   P30931; Q08DD5;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 142.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Adrenal gland;
RX   PubMed=1764065; DOI=10.1016/0006-291x(91)92058-r;
RA   Takayenoki Y., Muta T., Miyata T., Iwanaga S.;
RT   "cDNA and amino acid sequences of bovine tissue factor.";
RL   Biochem. Biophys. Res. Commun. 181:1145-1150(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; S74147; AAB20755.1; -; mRNA.
DR   EMBL; BC123808; AAI23809.2; -; mRNA.
DR   PIR; JQ1319; KFBO3.
DR   RefSeq; NP_776303.1; NM_173878.2.
DR   RefSeq; XP_015319808.1; XM_015464322.1.
DR   AlphaFoldDB; P30931; -.
DR   SMR; P30931; -.
DR   STRING; 9913.ENSBTAP00000009341; -.
DR   PaxDb; P30931; -.
DR   PRIDE; P30931; -.
DR   Ensembl; ENSBTAT00000009341; ENSBTAP00000009341; ENSBTAG00000007101.
DR   GeneID; 280686; -.
DR   KEGG; bta:280686; -.
DR   CTD; 2152; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007101; -.
DR   VGNC; VGNC:28687; F3.
DR   eggNOG; ENOG502RA1F; Eukaryota.
DR   GeneTree; ENSGT00390000012668; -.
DR   HOGENOM; CLU_082139_0_0_1; -.
DR   InParanoid; P30931; -.
DR   OMA; KFTPYNQ; -.
DR   OrthoDB; 1000890at2759; -.
DR   TreeFam; TF352627; -.
DR   Reactome; R-BTA-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000007101; Expressed in zone of skin and 100 other tissues.
DR   GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:1905286; C:serine-type peptidase complex; IEA:Ensembl.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
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: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; 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   Blood coagulation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis; Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..35
FT   CHAIN           36..292
FT                   /note="Tissue factor"
FT                   /id="PRO_0000033636"
FT   TOPO_DOM        36..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           46..48
FT                   /note="WKS motif"
FT   LIPID           274
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        81..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        215..238
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  32475 MW;  5E471D92BFBCE163 CRC64;
     MATPNGPRVP CPQAAVARAL LFGLVLIQGA GVAGTTDVVV AYNITWKSTN FKTILEWEPK
     PINHVYTVQI SPRLGNWKNK CFYTTNTECD VTDEIVKNVR ETYLARVLSY PADTSSSTVE
     PPFTNSPEFT PYLETNLGQP TIQSFEQVGT KLNVTVQDAR TLVRANSAFL SLRDVFGKDL
     NYTLYYWKAS STGKKKATTN TNGFLIDVDK GENYCFHVQA VILSRRVNQK SPESPIKCTS
     HEKVLSTELF FIIGTVMLVI IIFIVVLSVS LHKCRKVRAE RSGKENTPLN AA
 
 
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