FAXC_OXYSU
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 03-AUG-2022, entry version 110.
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; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; 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 Oxyuranus
RT scutellatus scutellatus (taipan venom).";
RL Biochemistry 19:1020-1023(1980).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND GAMMA-CARBOXYGLUTAMATION.
RC TISSUE=Venom;
RX PubMed=3531198; DOI=10.1016/s0021-9258(18)69299-3;
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 venom
RT 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 from
RT snake venoms.";
RL Thromb. Haemost. 86:710-711(2001).
CC -!- FUNCTION: Snake prothrombin (F2) activator that attacks the hemostatic
CC system of prey. This catalytic subunit is functionally similar to blood
CC coagulation factor Xa. For prothrombin activation, it requires a non-
CC catalytic subunit present in the venom, which is similar to coagulation
CC factor Va, to be fully active. In contrast to the 8 other snake venoms
CC tested, this protein is the only one to also activate factor VII (F7).
CC However, in contrast to prothrombin activation, the factor Va-like
CC subunit is not essential for this activation.
CC {ECO:0000269|PubMed:1604437, ECO:0000269|PubMed:3531198,
CC ECO:0000269|PubMed:6986908}.
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 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-linked.
CC Is associated with oscutarin-C non-catalytic subunit (AC Q58L91) in a
CC 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 dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3531198}.
CC -!- MISCELLANEOUS: Is classified in the group C of snake venom prothrombin
CC activators, since it does not require the mammalian factor Va for the
CC cleavage of prothrombin as the venom contains its own non-catalytic
CC factor Va-like molecule.
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. Hence, catalytic and non-
CC catalytic subunits are found naturally in venom as stable complexes.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AY940204; AAX37260.1; -; mRNA.
DR AlphaFoldDB; Q58L96; -.
DR SMR; Q58L96; -.
DR MEROPS; S01.446; -.
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 another organism; IDA:UniProtKB.
DR GO; GO:0035807; P:positive regulation of blood coagulation in another organism; IDA: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; 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
FT /evidence="ECO:0000255"
FT PROPEP 21..40
FT /evidence="ECO:0000250"
FT /id="PRO_0000409890"
FT CHAIN 41..181
FT /note="Oscutarin-C catalytic subunit light chain"
FT /id="PRO_5000095344"
FT PROPEP 182..209
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_5000095345"
FT CHAIN 210..467
FT /note="Oscutarin-C catalytic subunit heavy chain"
FT /id="PRO_5000095346"
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 210..454
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 309
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 406
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 209..210
FT /note="Cleavage"
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 254
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..329
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 216..221
FT /evidence="ECO:0000250"
FT DISULFID 236..252
FT /evidence="ECO:0000250"
FT DISULFID 377..391
FT /evidence="ECO:0000250"
FT DISULFID 402..430
FT /evidence="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
