ID H2S3Y5_TAKRU Unreviewed; 292 AA.
AC H2S3Y5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Tissue factor {ECO:0000256|ARBA:ARBA00018722};
DE AltName: Full=Coagulation factor III {ECO:0000256|ARBA:ARBA00031171};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000007107.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000007107.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000007107.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; H2S3Y5; -.
DR STRING; 31033.ENSTRUP00000063466; -.
DR Ensembl; ENSTRUT00000007152.3; ENSTRUP00000007107.3; ENSTRUG00000003042.3.
DR GeneTree; ENSGT00390000012668; -.
DR HOGENOM; CLU_114774_0_0_1; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
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 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 PRINTS; PR00346; TISSUEFACTOR.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
PE 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 21..106
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF01108"
FT DOMAIN 130..238
FT /note="Interferon/interleukin receptor"
FT /evidence="ECO:0000259|Pfam:PF09294"
SQ SEQUENCE 292 AA; 33383 MW; C4A815F8C119F389 CRC64;
KGSNLQSSHT CVLESRSNGT FQPFAASYPR AYNVTWKSTN FKTVLTWDPK PSHLYSYTVE
FFRKVDQDQR RINPHCIRSS FPQCDLSNSL TELRSSYMAE ILSEPPLGET SELTEFPYSR
SPRFCPYNDT DIGKPDFKLE VSADKKKTSL FVTDPLTALF KDGRQLNIRD IFSDQLMYKV
TYRKNKSTGK KEHISKTNVI ELTNLDQGES YCFSIQAYIP SRTITKQLGE ESQFQCSEEN
SSILKGKAES ESESDLFIAI VHVVHSITQA RNLSRCDAAT FNIEKTINTR IR
//