ID   FAXD_NOTSN              Reviewed;          20 AA.
AC   P0CY52;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Venom prothrombin activator notanarin-D;
DE            Short=vPA;
DE            EC=3.4.21.6;
DE   AltName: Full=Venom coagulation factor Xa-like protease;
DE   Contains:
DE     RecName: Full=Notanarin-D light chain;
DE   Contains:
DE     RecName: Full=Notanarin-D heavy chain;
DE   Flags: Precursor; Fragments;
OS   Notechis scutatus niger (Peninsula tiger snake) (Notechis ater niger).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Notechis.
OX   NCBI_TaxID=1027870;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, GAMMA-CARBOXYGLUTAMATION AT GLU-6 AND GLU-7, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=12403650; DOI=10.1042/bj20020889;
RA   Rao V.S., Joseph J.S., Kini R.M.;
RT   "Group D prothrombin activators from snake venom are structural homologues
RT   of mammalian blood coagulation factor Xa.";
RL   Biochem. J. 369:635-642(2003).
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. {ECO:0000269|PubMed:12403650}.
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:0000269|PubMed:12403650}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12403650}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12403650}.
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:12403650}.
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. The venom of this species
CC       does not contains its own coagulation factor V-like.
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   AlphaFoldDB; P0CY52; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Prothrombin activator; Secreted; Toxin.
FT   CHAIN           1..>10
FT                   /note="Notanarin-D light chain"
FT                   /id="PRO_0000409891"
FT   CHAIN           11..>20
FT                   /note="Notanarin-D heavy chain"
FT                   /id="PRO_0000409892"
FT   DOMAIN          1..>10
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          11..>20
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   MOD_RES         6
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:12403650"
FT   MOD_RES         7
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:12403650"
FT   UNSURE          17
FT                   /note="Assigned by comparison with orthologs"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000305"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2209 MW;  C480714CC4EDDC33 CRC64;
     SNSLFEEVRP IVNGMDCKLG