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Database: UniProt
Entry: P83370
LinkDB: P83370
Original site: P83370 
ID   FAXD_HOPST              Reviewed;         455 AA.
AC   P83370; Q58L92;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   05-DEC-2018, entry version 109.
DE   RecName: Full=Venom prothrombin activator hopsarin-D;
DE            Short=vPA;
DE            EC=3.4.21.6;
DE   AltName: Full=Venom coagulation factor Xa-like protease;
DE   Contains:
DE     RecName: Full=Hopsarin-D light chain;
DE   Contains:
DE     RecName: Full=Hopsarin-D heavy chain;
DE   Flags: Precursor;
OS   Hoplocephalus stephensii (Stephens' banded snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Notechinae;
OC   Hoplocephalus.
OX   NCBI_TaxID=196418 {ECO:0000305};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15930152; DOI=10.1093/molbev/msi181;
RA   St Pierre L., Masci P.P., Filippovich I., Sorokina N., Marsh N.,
RA   Miller D.J., Lavin M.F.;
RT   "Comparative analysis of prothrombin activators from the venom of
RT   Australian elapids.";
RL   Mol. Biol. Evol. 22:1853-1864(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 41-181 AND 210-455, FUNCTION, CATALYTIC ACTIVITY,
RP   SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59;
RP   GLU-60; GLU-65; GLU-66; GLU-69; GLU-72 AND GLU-75, GLYCOSYLATION AT
RP   SER-92 AND ASN-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=12403650; DOI=10.1042/BJ20020889;
RA   Rao V.S., Joseph J.S., Kini R.M.;
RT   "Group D prothrombin activators from snake venom are structural
RT   homologues of mammalian blood coagulation factor Xa.";
RL   Biochem. J. 369:635-642(2003).
RN   [3]
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. The procoagulant activity of hopsarin-D is
CC       approximately 10-fold lower than that of trocarin-D and FXa.
CC       {ECO:0000269|PubMed:12403650}.
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         Evidence={ECO:0000269|PubMed:12403650};
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-linked. {ECO:0000269|PubMed:12403650}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12403650}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12403650}.
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 216 that is replaced by
CC       a Ser residue, resulting of a loss a disulfide bond. This may
CC       contribute to the lower procoagulant activity. {ECO:0000305}.
DR   EMBL; AY940208; AAX37264.1; -; mRNA.
DR   ProteinModelPortal; P83370; -.
DR   SMR; P83370; -.
DR   MEROPS; S01.426; -.
DR   iPTMnet; P83370; -.
DR   HOVERGEN; HBG013304; -.
DR   GO; GO:0005576; C:extracellular region; IDA: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; IDA: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; IDA:UniProtKB.
DR   GO; GO:0035807; P:positive regulation of blood coagulation in other organism; IDA: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; 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   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis impairing toxin;
KW   Hydrolase; Protease; Prothrombin activator; Repeat; Secreted;
KW   Serine protease; Signal; Toxin.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     40       {ECO:0000250}.
FT                                /FTId=PRO_0000409722.
FT   CHAIN        41    181       Hopsarin-D light chain.
FT                                /FTId=PRO_0000027816.
FT   PROPEP      182    209       Activation peptide.
FT                                {ECO:0000269|PubMed:12403650}.
FT                                /FTId=PRO_5000095361.
FT   CHAIN       210    455       Hopsarin-D heavy chain.
FT                                /FTId=PRO_0000027817.
FT   DOMAIN       41     86       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       86    121       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      210    453       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    251    251       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    308    308       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    405    405       Charge relay system. {ECO:0000250}.
FT   SITE        103    103       Not modified.
FT   MOD_RES      46     46       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      54     54       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      56     56       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      59     59       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      65     65       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      69     69       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      72     72       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   MOD_RES      75     75       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:12403650}.
FT   CARBOHYD     92     92       O-linked (Hex...) serine.
FT                                {ECO:0000269|PubMed:12403650}.
FT   CARBOHYD    254    254       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12403650}.
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    328       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    236    252       {ECO:0000250}.
FT   DISULFID    376    390       {ECO:0000250}.
FT   DISULFID    401    429       {ECO:0000250}.
FT   CONFLICT     78     78       E -> T (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     98     98       H -> R (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    260    270       Missing (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    402    402       E -> Q (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   455 AA;  51248 MW;  39B5F4442B995E4F CRC64;
     MAPQLLLCLI LTFLWSVPEA ESNVFLKSKV ANRFLQRTKR SNSLFEEIRP GNIERECIEE
     KCSKEEAREV FEDNEKTETF WNVYVDGDQC SSNPCHYHGT CKDGIGSYTC TCLPNYEGKN
     CEKVLFKSCR AFNGNCWHFC KRVQSETQCS CAESYRLGVD GHSCVAEGDF SCGRNIKARN
     KREASLPDFV QSQKATLLKK SDNPSPDIRI VNGMDSKLGE CPWQAVLINE KGEVFCGGTI
     LSPIHVLTAA HCINQTKSVS VIVGEIDISR KETRRLLSVD KIYVHTKFVP PNYYYGHQNF
     DRVAYDYDIA IIRMKTPIQF SENVVPACLP TADFANEVLM KQDSGIVSGF GRIRFKEPTS
     NTLKVITVPY VDRHTCMLSS DFRITQNMFC AGYDTLPQDA CEGDSGGPHI TAYGDTHFIT
     GIVSWGEGCA RKGKYGVYTK VSRFIPWIKK IMSLK
//
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