ID A0A093CY28_TAUER Unreviewed; 260 AA.
AC A0A093CY28;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Tissue factor {ECO:0000256|ARBA:ARBA00018722};
DE AltName: Full=Coagulation factor III {ECO:0000256|ARBA:ARBA00031171};
DE Flags: Fragment;
GN ORFNames=N340_09023 {ECO:0000313|EMBL:KFV17789.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV17789.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV17789.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV17789.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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. {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 EMBL; KL468057; KFV17789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CY28; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 220..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..79
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF01108"
FT DOMAIN 101..208
FT /note="Interferon/interleukin receptor"
FT /evidence="ECO:0000259|Pfam:PF09294"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV17789.1"
FT NON_TER 260
FT /evidence="ECO:0000313|EMBL:KFV17789.1"
SQ SEQUENCE 260 AA; 29387 MW; 4C675A3AD2EDE042 CRC64;
GNPELPTAVN ITWSSINFKT ILQWQPKPSG YFYTVEIHGQ TSNTKKKCIL TADTECDVTD
VLRDVRETYT AHILSVTSSG MDNFEEPPFA VSEKFTPYNQ TVLGKPEIQN YTQKGSELNV
VFQDPLTPYT FPNGSFQSIR DIFQHDLEYK LYYWKDQSSG KKDTTTKSHK FEVGVDNTKN
YCFYIQGIIP SRRENRNGQE SMVVCTSIER GTLDEYGAEV FIIIAVIAIA VITLAVVLSV
ILCKRKKAKA AREKEPLNGV
//
