ID   VSPCA_AGKBI             Reviewed;          20 AA.
AC   P33588;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein C activator;
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragment;
OS   Agkistrodon bilineatus (Cantil) (Tropical moccasin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8718;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=2385829; DOI=10.1016/0049-3848(90)90305-v;
RA   Nakagaki T., Kazim A.L., Kisiel W.;
RT   "Isolation and characterization of a protein C activator from tropical
RT   moccasin venom.";
RL   Thromb. Res. 58:593-602(1990).
CC   -!- FUNCTION: Snake venom serine protease that selectively cleaves the
CC       heavy chain of protein C (PROC). This activation is thrombomodulin-
CC       independent. {ECO:0000269|PubMed:2385829}.
CC   -!- ACTIVITY REGULATION: Inhibited by calcium.
CC       {ECO:0000269|PubMed:2385829}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.7 uM for human protein C {ECO:0000269|PubMed:2385829};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:2385829}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   PIR; A60489; A60489.
DR   AlphaFoldDB; P33588; -.
DR   MEROPS; S01.178; -.
DR   SABIO-RK; P33588; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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 inhibiting toxin; Direct protein sequencing;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW   Serine protease; Toxin.
FT   CHAIN           1..>20
FT                   /note="Protein C activator"
FT                   /id="PRO_0000088724"
FT   DOMAIN          1..>20
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2191 MW;  6E99F8B4CC53EFE1 CRC64;
     VVGGDECNIN EHRSLALMYA