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Database: UniProt
Entry: Q58L95
LinkDB: Q58L95
Original site: Q58L95 
ID   FAXC_OXYMI              Reviewed;         467 AA.
AC   Q58L95;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-DEC-2018, entry version 103.
DE   RecName: Full=Venom prothrombin activator omicarin-C catalytic subunit;
DE            Short=vPA;
DE            EC=3.4.21.6;
DE   AltName: Full=Venom coagulation factor Xa-like protease;
DE   Contains:
DE     RecName: Full=Omicarin-C catalytic subunit light chain;
DE   Contains:
DE     RecName: Full=Omicarin-C catalytic subunit heavy chain;
DE   Flags: Precursor;
OS   Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Acanthophiinae;
OC   Oxyuranus.
OX   NCBI_TaxID=111177;
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   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 catalytic subunit is functionally similar to
CC       blood coagulation factor Xa. It requires a non-catalytic subunit
CC       present in the venom, which is similar to coagulation factor Va,
CC       to be fully active (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   -!- ACTIVITY REGULATION: Activated by calcium and negatively charged
CC       phospholipids. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of a light and a heavy chains; disulfide-
CC       linked. Is associated with omicarin-C non-catalytic subunit (AC
CC       Q58L90) in a non-covalent manner (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
CC       dependent carboxylation. These residues are essential for the
CC       binding of calcium.
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; AY940205; AAX37261.1; -; mRNA.
DR   ProteinModelPortal; Q58L95; -.
DR   MEROPS; S01.446; -.
DR   PRIDE; Q58L95; -.
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   2: Evidence at transcript 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_0000409889.
FT   CHAIN        41    181       Omicarin-C catalytic subunit light chain.
FT                                /FTId=PRO_5000095348.
FT   PROPEP      182    209       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_5000095349.
FT   CHAIN       210    467       Omicarin-C catalytic subunit heavy chain.
FT                                /FTId=PRO_5000095350.
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;  52467 MW;  7A2F9BD327A74DD4 CRC64;
     MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR ANSLFEEFRS GNIERECIEE
     RCSKEEAREV FEDDEKTETF WNVYVDGDQC SSNPCHYRGT CKDGIGSYTC TCLFGYEGKN
     CERVLYKSCR VDNGNCWHFC KPVQNDIQCS CAEGYLLGED GHSCVAGGNF SCGRNIKTRN
     KREASLPDFV QSQNATLLKK SDNPSPDIRI VNGMDCKLGE CPWQAVLVDE KEGVFCGGTI
     LSPIYVLTAA HCINQTEKIS VVVGEIDKSR VETGHLLSVD KIYVHKKFVP PKKGYKFYEK
     FDLVSYDYDI AIIQMKTPIQ FSENVVPACL PTADFANQVL MKQDFGIISG FGRIFEKGPK
     SNTLKVLKVP YVDRHTCMVS SESPITPTMF CAGYDTLPRD ACQGDSGGPH ITAYRDTHFI
     TGIVSWGEGC AKKGKYGIYT KVSKFILWIK RIMRQKLPST ESSTGRL
//
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