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Database: UniProt
Entry: A6MFK7
LinkDB: A6MFK7
Original site: A6MFK7 
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   05-DEC-2018, entry version 77.
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;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX   NCBI_TaxID=412038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 134-140; 163-174;
RP   348-359; 372-380 AND 427-434, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND 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
RT   from 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
CC         in prothrombin to form thrombin.; EC=3.4.21.6;
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-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
CC       glutamate residues allows the modified protein to bind calcium.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Is classified in the group D of snake venom
CC       prothrombin activators, since it requires the mammalian factor Va
CC       for maximal activity for the cleavage of prothrombin.
CC   -!- MISCELLANEOUS: In contrast to blood coagulation factors that
CC       circulate as inactive zymogen in plasma, venom prothrombin
CC       activators are always found in the active form in the venom.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- CAUTION: Lacks the Cys residue in position 255 that is replaced by
CC       a Gly residue, resulting of a loss a disulfide bond. This may
CC       contribute to a probable lower procoagulant activity.
CC       {ECO:0000305}.
DR   EMBL; DQ917518; ABK63547.1; -; mRNA.
DR   ProteinModelPortal; A6MFK7; -.
DR   MEROPS; S01.396; -.
DR   PRIDE; A6MFK7; -.
DR   HOVERGEN; HBG013304; -.
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 other organism; ISS:UniProtKB.
DR   GO; GO:0035807; P:positive regulation of blood coagulation in other organism; ISS:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
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; IPR013032; EGF-like_CS.
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; 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;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease;
KW   Prothrombin activator; Repeat; Secreted; Serine protease; Signal;
KW   Toxin.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     40       {ECO:0000250}.
FT                                /FTId=PRO_0000409894.
FT   CHAIN        41    181       Vestarin-D1 light chain.
FT                                /FTId=PRO_5000254111.
FT   PROPEP      182    228       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000409895.
FT   CHAIN       229    473       Vestarin-D1 heavy chain.
FT                                /FTId=PRO_0000409896.
FT   DOMAIN       41     86       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       86    122       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      129    164       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      229    460       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    270    270       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    315    315       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    412    412       Charge relay system. {ECO:0000250}.
FT   MOD_RES      46     46       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      54     54       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      56     56       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      59     59       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      65     65       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      69     69       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      72     72       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      75     75       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   CARBOHYD     92     92       O-linked (Hex...) serine. {ECO:0000250}.
FT   CARBOHYD    273    273       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57     62       {ECO:0000250}.
FT   DISULFID     90    101       {ECO:0000250}.
FT   DISULFID     95    110       {ECO:0000250}.
FT   DISULFID    112    121       {ECO:0000250}.
FT   DISULFID    129    140       {ECO:0000250}.
FT   DISULFID    136    149       {ECO:0000250}.
FT   DISULFID    151    164       {ECO:0000250}.
FT   DISULFID    172    335       Interchain (between light and heavy
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DISULFID    235    240       {ECO:0000250}.
FT   DISULFID    383    397       {ECO:0000250}.
FT   DISULFID    408    436       {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
//
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