ID A0A0Q3T2V1_AMAAE Unreviewed; 283 AA.
AC A0A0Q3T2V1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Tissue factor {ECO:0000256|ARBA:ARBA00018722};
DE AltName: Full=Coagulation factor III {ECO:0000256|ARBA:ARBA00031171};
GN ORFNames=AAES_153561 {ECO:0000313|EMBL:KQK74902.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74902.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK74902.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74902.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK74902.1}.
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DR EMBL; LMAW01002989; KQK74902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3T2V1; -.
DR STRING; 12930.A0A0Q3T2V1; -.
DR Proteomes; UP000051836; 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:UP000051836};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..283
FT /note="Tissue factor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006207755"
FT TRANSMEM 243..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..105
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF01108"
FT DOMAIN 124..230
FT /note="Interferon/interleukin receptor"
FT /evidence="ECO:0000259|Pfam:PF09294"
SQ SEQUENCE 283 AA; 31798 MW; 274E79D55EB91611 CRC64;
MLHAAARGPA LLLSALLWSL ATAGNPELPT AVNITWSSIN FKTILRWQPK PSGYLYTVEI
HGQTSNTRKK CILTAETECD VTDLLRNVRE TYTAHILSVA SSGTDNFEEP PFAVSEKFTP
YSQTVLGKPE IQNYTQKGSK LTVMFQDPLT PYTFPNGSFQ SIRDIFQNDL EYKIYYWKDQ
SSGKKDAITK SHEFEERVDS SKNYCFYIQG IIPSRRENRN GQESMVLCTS IGRNVLHEYG
AEFFIIIAVI VIAVIASAVV LSVILCKRKK AKAAREKEPL NGI
//
