ID   VSPKA_GLOHA             Reviewed;          15 AA.
AC   P0DJG5;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Snake venom serine protease AHP-Ka;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=8714;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=22162083; DOI=10.1002/jsfa.4733;
RA   Zhang Y., Xu W., Ma B., Huang K., Song M., Zhang N., Zhang Y., Wang Y.,
RA   Dai Y., Luo Y.;
RT   "Isolation and characterisation of a kallikrein-like enzyme from
RT   Agkistrodon halys pallas snake venom.";
RL   J. Sci. Food Agric. 92:1497-1503(2012).
CC   -!- FUNCTION: Snake venom serine protease that hydrolyzes specific
CC       chromogenic substrate S-2302 suggesting that AHP-Ka is a plasma
CC       kallikrein. Has esterase activity on alpha-N-benzoyl-L-arginine ethyl
CC       ester hydrochloride (BAEE) and amidolytic activity.
CC       {ECO:0000269|PubMed:22162083}.
CC   -!- ACTIVITY REGULATION: Inhibited by PMSF, Fe(3+), Fe(2+), Cu(2+), Cd(2+),
CC       Mn(2+), and Al(3+). Not inhibited by Ca(2+) and Mg(2+) and EDTA.
CC       {ECO:0000269|PubMed:22162083}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-8. {ECO:0000269|PubMed:22162083};
CC       Temperature dependence:
CC         Optimum temperature is 30-40 degrees Celsius.
CC         {ECO:0000269|PubMed:22162083};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22162083}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: N-glycosylated. Cleavage of N-glycans reduces the catalytic
CC       enzymatic efficiency.
CC   -!- MASS SPECTROMETRY: Mass=26243; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22162083};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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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   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease; Toxin.
FT   CHAIN           1..>15
FT                   /note="Snake venom serine protease AHP-Ka"
FT                   /id="PRO_0000417006"
FT   DOMAIN          1..>15
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        7..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1716 MW;  03F3910227D52FDA CRC64;
     VIGGDECNIN EHRFL