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VSPPE_GLOHA
ID   VSPPE_GLOHA             Reviewed;         236 AA.
AC   O93421;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Snake venom serine protease pallase;
DE            Short=SVSP pallase;
DE            EC=3.4.21.-;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=12142921;
RA   Pan H., Zhou Y.C., Yang G.Z., Wu X.F.;
RT   "Cloning and expression of cDNA for thrombin-like enzyme from Agkistrodon
RT   halys pallas snake venom.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 31:79-82(1999).
CC   -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC       system of the prey. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC34898.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF088996; AAC34898.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; O93421; -.
DR   SMR; O93421; -.
DR   MEROPS; S01.333; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 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   Disulfide bond; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW   Serine protease; Toxin.
FT   CHAIN           1..236
FT                   /note="Snake venom serine protease pallase"
FT                   /id="PRO_0000296196"
FT   DOMAIN          1..227
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        41
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        86
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        182
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        26..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        74..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        118..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        150..167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        178..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   236 AA;  26048 MW;  769BE7732E4F46F6 CRC64;
     VIGGDECNIN EHRFLVALYT SRTLFCGGTL INQEWVLTAA HCNMEDIQIK LGMHSKKVPN
     EDEQKRVPKE KFFCLSSKKL YLWDKDIMLI RLDSPVKNSA HIAPLSLPSS PPSVGSVCRT
     MGWGRISSTK ETYPDVPHCV NINLLEYEMC RAPYPEFELP ATSRTLCAGI LEGGKDTCVG
     DSGGPLICNG QFQGIASWGD HPCAQPHKPA AYTKVFDHLD WIENIIAGNT DASCPP
 
 
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