FAXD1_DEMVE
ID FAXD1_DEMVE Reviewed; 473 AA.
AC A6MFK7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Venom prothrombin activator vestarin-D1;
DE Short=vPA;
DE EC=3.4.21.6;
DE AltName: Full=Venom coagulation factor Xa-like protease;
DE Contains:
DE RecName: Full=Vestarin-D1 light chain;
DE Contains:
DE RecName: Full=Vestarin-D1 heavy chain;
DE Flags: Precursor;
OS Demansia vestigiata (Lesser black whip snake) (Demansia atra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX NCBI_TaxID=412038;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 134-140; 163-174; 348-359;
RP 372-380 AND 427-434, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17608513; DOI=10.1021/pr0701613;
RA St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J.,
RA de Jersey J., Masci P.P., Lavin M.F.;
RT "Diversity of toxic components from the venom of the evolutionarily
RT distinct black whip snake, Demansia vestigiata.";
RL J. Proteome Res. 6:3093-3107(2007).
RN [2]
RP NOMENCLATURE.
RX PubMed=11522026;
RA Manjunatha Kini R., Morita T., Rosing J.;
RT "Classification and nomenclature of prothrombin activators isolated from
RT snake venoms.";
RL Thromb. Haemost. 86:710-711(2001).
CC -!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
CC system of prey. This protein is functionally similar to blood
CC coagulation factor Xa (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
CC prothrombin to form thrombin.; EC=3.4.21.6;
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-
CC linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17608513}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17608513}.
CC -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC residues allows the modified protein to bind calcium. {ECO:0000250}.
CC -!- MISCELLANEOUS: Is classified in the group D of snake venom prothrombin
CC activators, since it requires the mammalian factor Va for maximal
CC activity for the cleavage of prothrombin.
CC -!- MISCELLANEOUS: In contrast to blood coagulation factors that circulate
CC as inactive zymogen in plasma, venom prothrombin activators are always
CC found in the active form in the venom.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Lacks the Cys residue in position 255 that is replaced by a
CC Gly residue, resulting of a loss a disulfide bond. This may contribute
CC to a probable lower procoagulant activity. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ917518; ABK63547.1; -; mRNA.
DR AlphaFoldDB; A6MFK7; -.
DR SMR; A6MFK7; -.
DR MEROPS; S01.396; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in another organism; ISS:UniProtKB.
DR GO; GO:0035807; P:positive regulation of blood coagulation in another organism; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Calcium;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Prothrombin activator;
KW Repeat; Secreted; Serine protease; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..40
FT /evidence="ECO:0000250"
FT /id="PRO_0000409894"
FT CHAIN 41..181
FT /note="Vestarin-D1 light chain"
FT /id="PRO_5000254111"
FT PROPEP 182..228
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409895"
FT CHAIN 229..473
FT /note="Vestarin-D1 heavy chain"
FT /id="PRO_0000409896"
FT DOMAIN 41..86
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 86..122
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 129..164
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 229..460
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 412
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT CARBOHYD 92
FT /note="O-linked (Hex...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..62
FT /evidence="ECO:0000250"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
FT DISULFID 95..110
FT /evidence="ECO:0000250"
FT DISULFID 112..121
FT /evidence="ECO:0000250"
FT DISULFID 129..140
FT /evidence="ECO:0000250"
FT DISULFID 136..149
FT /evidence="ECO:0000250"
FT DISULFID 151..164
FT /evidence="ECO:0000250"
FT DISULFID 172..335
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00463"
FT DISULFID 235..240
FT /evidence="ECO:0000250"
FT DISULFID 383..397
FT /evidence="ECO:0000250"
FT DISULFID 408..436
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 52732 MW; 4C625C1975A8FBEC CRC64;
MAPQLLLCLI QTFLWSLPEA ESNVFLKSNV ANRFLQRTKR ANSGFEEIYP ANFERECVEE
RCSKEEAREV FEDDEKTEAF WTVYVDGDQC LSNPCHYGGT CKDGIGSYTC TCLAGYEGKN
CEHDLLKSCR VDNGNCWHFC KPVQNDTQCS CAEGYRLGDN GFSCIAEGEF SCGRNIKSRN
KREASLPDFQ TDFSDDYDAI DENNLIETVQ SQSATLLKKS DNPNPDIRIV NGLDCKLGEC
PWQAVLIDEK GTAFGGGTIL SPYFVLTAAH CINKTKSIAV VVGQVDISRK ETRRLLSVDK
VYTHPKYVHV TNDYDIAIIQ LKTPIQFSEN VVPACLPTAD FANHVLMKQD FGIVSGFGRI
EEKGPTSNIL KVVMVPYVDR HTCILSTKIP ITRNMFCAGY GNQPEDACEG DSGGPHITAY
KDTHFLTGIV SWGEGCGRDG KYGIYTKVSN FLPWIKTIMR RKQPSTESST GRL
