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Database: UniProt
Entry: Q58L96
LinkDB: Q58L96
Original site: Q58L96 
ID   FAXC_OXYSU              Reviewed;         467 AA.
AC   Q58L96;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=Venom prothrombin activator oscutarin-C catalytic subunit;
DE            Short=vPA;
DE            EC=3.4.21.6;
DE   AltName: Full=Factor VII activator;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   AltName: Full=Venom coagulation factor Xa-like protease;
DE   Contains:
DE     RecName: Full=Oscutarin-C catalytic subunit light chain;
DE   Contains:
DE     RecName: Full=Oscutarin-C catalytic subunit heavy chain;
DE   Flags: Precursor;
OS   Oxyuranus scutellatus (Coastal taipan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Acanthophiinae;
OC   Oxyuranus.
OX   NCBI_TaxID=8668;
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   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Oxyuranus scutellatus scutellatus; TISSUE=Venom;
RX   PubMed=6986908; DOI=10.1021/bi00546a029;
RA   Walker F.J., Owen W.G., Esmon C.T.;
RT   "Characterization of the prothrombin activator from the venom of
RT   Oxyuranus scutellatus scutellatus (taipan venom).";
RL   Biochemistry 19:1020-1023(1980).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   GAMMA-CARBOXYGLUTAMATION.
RC   TISSUE=Venom;
RX   PubMed=3531198;
RA   Speijer H., Govers-Riemslag J.W.P., Zwaal R.F.A., Rosing J.;
RT   "Prothrombin activation by an activator from the venom of Oxyuranus
RT   scutellatus (Taipan snake).";
RL   J. Biol. Chem. 261:13258-13267(1986).
RN   [4]
RP   FUNCTION AS FACTOR VII ACTIVATOR, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=1604437; DOI=10.1016/0049-3848(92)90230-8;
RA   Nakagaki T., Lin P., Kisiel W.;
RT   "Activation of human factor VII by the prothrombin activator from the
RT   venom of Oxyuranus scutellatus (Taipan snake).";
RL   Thromb. Res. 65:105-116(1992).
RN   [5]
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 (F2) activator that attacks the
CC       hemostatic system of prey. This catalytic subunit is functionally
CC       similar to blood coagulation factor Xa. For prothrombin
CC       activation, it requires a non-catalytic subunit present in the
CC       venom, which is similar to coagulation factor Va, to be fully
CC       active. In contrast to the 8 other snake venoms tested, this
CC       protein is the only one to also activate factor VII (F7). However,
CC       in contrast to prothrombin activation, the factor Va-like subunit
CC       is not essential for this activation. {ECO:0000269|PubMed:1604437,
CC       ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}.
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:3531198};
CC   -!- ACTIVITY REGULATION: Activated by calcium and negatively charged
CC       phospholipids. {ECO:0000269|PubMed:3531198}.
CC   -!- SUBUNIT: Heterodimer of a light and a heavy chains; disulfide-
CC       linked. Is associated with oscutarin-C non-catalytic subunit (AC
CC       Q58L91) in a non-covalent manner (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1604437,
CC       ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:1604437, ECO:0000269|PubMed:3531198,
CC       ECO:0000269|PubMed:6986908}.
CC   -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
CC       dependent carboxylation. These residues are essential for the
CC       binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463,
CC       ECO:0000269|PubMed:3531198}.
CC   -!- MISCELLANEOUS: Is classified in the group C of snake venom
CC       prothrombin activators, since it does not require the mammalian
CC       factor Va for the cleavage of prothrombin as the venom contains
CC       its own non-catalytic factor Va-like molecule.
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       Hence, catalytic and non-catalytic subunits are found naturally in
CC       venom as stable complexes.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AY940204; AAX37260.1; -; mRNA.
DR   ProteinModelPortal; Q58L96; -.
DR   SMR; Q58L96; -.
DR   MEROPS; S01.446; -.
DR   PRIDE; Q58L96; -.
DR   HOVERGEN; HBG013304; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; 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; 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; 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_0000409890.
FT   CHAIN        41    181       Oscutarin-C catalytic subunit light
FT                                chain.
FT                                /FTId=PRO_5000095344.
FT   PROPEP      182    209       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_5000095345.
FT   CHAIN       210    467       Oscutarin-C catalytic subunit heavy
FT                                chain.
FT                                /FTId=PRO_5000095346.
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      210    454       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    251    251       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    309    309       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    406    406       Charge relay system. {ECO:0000250}.
FT   SITE        209    210       Cleavage. {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    254    254       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    329       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    216    221       {ECO:0000250}.
FT   DISULFID    236    252       {ECO:0000250}.
FT   DISULFID    377    391       {ECO:0000250}.
FT   DISULFID    402    430       {ECO:0000250}.
SQ   SEQUENCE   467 AA;  52454 MW;  BB50EEB54F2B8F58 CRC64;
     MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR ANSLYEEFRS GNIERECIEE
     RCSKEEAREV FEDDEKTETF WNVYVDGDQC SSNPCHYRGT CKDGIGSYTC TCLSGYEGKN
     CERVLYKSCR VDNGNCWHFC KPVQNDIQCS CAEGYLLGED GHSCVAGGNF SCGRNIKTRN
     KREASLPDFV QSQNAILLKK SDNPSPDIRI VNGMDCKLGE CPWQAVLVDE KEDAFCGGTI
     LSPIYVLTAA HCINQTKMIS VVVGEINISR KNPGRLLSVD KIYVHQKFVP PKKGYEFYEK
     FDLVSYDYDI AILQMKTPIQ FSENVVPACL PTADFANQVL MKQDFGIVSG FGRIFEKGPQ
     SKTLKVLKVP YVDRHTCMLS SESPITPTMF CAGYDTLPRD ACQGDSGGPH ITAYRDTHFI
     TGIVSWGEGC AQTGKYGVYT KVSKFILWIK RIMRQKLPST ESSTGRL
//
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