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Database: UniProt
Entry: Q58L93
LinkDB: Q58L93
Original site: Q58L93 
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   05-DEC-2018, entry version 97.
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;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Acanthophiinae;
OC   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
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 (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   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-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
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}.
DR   EMBL; AY940207; AAX37263.1; -; mRNA.
DR   ProteinModelPortal; Q58L93; -.
DR   SMR; Q58L93; -.
DR   MEROPS; S01.396; -.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; 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       {ECO:0000255}.
FT   PROPEP       21     40       {ECO:0000250}.
FT                                /FTId=PRO_0000409900.
FT   CHAIN        41    181       Porpharin-D light chain.
FT                                /FTId=PRO_5000095356.
FT   PROPEP      182    209       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_5000095357.
FT   CHAIN       210    454       Porpharin-D heavy chain.
FT                                /FTId=PRO_5000095358.
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    441       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    251    251       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    296    296       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    393    393       Charge relay system. {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      75     75       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   CARBOHYD     92     92       O-linked (Hex...) serine. {ECO:0000250}.
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    316       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    364    378       {ECO:0000250}.
FT   DISULFID    389    417       {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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