ID   VSPA2_CROAT             Reviewed;          15 AA.
AC   Q9PRW3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Alpha-fibrinogenase A2;
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   Flags: Fragment;
OS   Crotalus atrox (Western diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8730;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=8024586; DOI=10.1006/bbrc.1994.1861;
RA   Hung C.C., Chiou S.H.;
RT   "Isolation of multiple isoforms of alpha-fibrinogenase from the Western
RT   diamondback rattlesnake, Crotalus atrox: N-terminal sequence homology with
RT   ancrod, an antithrombotic agent from Malayan viper.";
RL   Biochem. Biophys. Res. Commun. 201:1414-1423(1994).
CC   -!- FUNCTION: Snake venom serine protease that cleaves fibrinogen Aalpha
CC       chain (FGA), partially cleaves Bbeta chain (FGB) and has no activity on
CC       gamma chain. Is more potent than A3 alpha-fibrinogenases and less
CC       potent than A1. {ECO:0000269|PubMed:8024586}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF, bovine aprotinin (APR), and
CC       soybean trypsin inhibitor (STI). Is not inhibited by EDTA, beta-
CC       mercaptoethanol, and high temperature (85 degrees Celsius).
CC       {ECO:0000269|PubMed:8024586}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8024586}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8024586}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:8024586}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   PIR; PC2215; PC2215.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
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   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW   Toxin.
FT   CHAIN           1..>15
FT                   /note="Alpha-fibrinogenase A2"
FT                   /id="PRO_0000406905"
FT   DISULFID        7..?
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1640 MW;  03EFE10227CA12DA CRC64;
     VPGGDECNIN EHRSL