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FAXD_PSEPO
ID   FAXD_PSEPO              Reviewed;         454 AA.
AC   Q58L93;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Venom prothrombin activator porpharin-D;
DE            Short=vPA;
DE            EC=3.4.21.6;
DE   AltName: Full=Venom coagulation factor Xa-like protease;
DE   Contains:
DE     RecName: Full=Porpharin-D light chain;
DE   Contains:
DE     RecName: Full=Porpharin-D heavy chain;
DE   Flags: Precursor;
OS   Pseudechis porphyriacus (Red-bellied black snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX   NCBI_TaxID=8671;
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 from
RT   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 in
CC         prothrombin to form thrombin.; EC=3.4.21.6;
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-
CC       linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC       residues allows the modified protein to bind calcium. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Is classified in the group D of snake venom prothrombin
CC       activators, since it requires the mammalian factor Va for maximal
CC       activity for the cleavage of prothrombin.
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.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AY940207; AAX37263.1; -; mRNA.
DR   AlphaFoldDB; Q58L93; -.
DR   SMR; Q58L93; -.
DR   MEROPS; S01.396; -.
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 another organism; ISS:UniProtKB.
DR   GO; GO:0035807; P:positive regulation of blood coagulation in another organism; ISS: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; IPR009030; Growth_fac_rcpt_cys_sf.
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; SSF57184; SSF57184; 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   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
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..40
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000409900"
FT   CHAIN           41..181
FT                   /note="Porpharin-D light chain"
FT                   /id="PRO_5000095356"
FT   PROPEP          182..209
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000095357"
FT   CHAIN           210..454
FT                   /note="Porpharin-D heavy chain"
FT                   /id="PRO_5000095358"
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..441
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        296
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        393
FT                   /note="Charge relay system"
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         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   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..316
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        364..378
FT                   /evidence="ECO:0000250"
FT   DISULFID        389..417
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  50781 MW;  971596FB8730FFD1 CRC64;
     MAPQLLLCLI LTFLWSLPEA ESNVFLKSKE ANRFLQRTKR SNSLFEEFRP GNIERECIEE
     KCSKEEAREI FKDNEKTEAF WNVYVDGDQC SSNPCHYGGT CKDGIGSYTC TCLPNYEGKN
     CEHLLFKSCR FFNGNCWHFC KPVQNDTQCS CAESYRLGDD GHSCVAEGDF SCGRNIKARN
     KREASLPDFV QSQNATLLKK SDNPSPDIRI INGMDCKLGE CPWQAVLLDK EGDVFCGGTI
     LSPIYVLTAA HCITQSKHIS VVVGEIDISR KETRHLLSVD KAYVHTKFVL ATYDYDIAII
     QLKTPIQFSE NVVPACLPTA DFANQVLMKQ DFGIISGFGH TRSGGQTSNT LKVVTIPYVD
     RHTCMLSSDF RITPNMFCAG YDTLPRDACQ GDSGGPHITA YRDTHFITGI ISWGEGCAKK
     GKYGVYTKVS NFIPWIKAVM RKHQPSTESS TGRL
 
 
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