VSP2_GLOHA
ID VSP2_GLOHA Reviewed; 260 AA.
AC Q9YGI6;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Snake venom serine protease pallabin-2;
DE Short=SVSP;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=JZTHR7;
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=10205666; DOI=10.1080/15216549900201223;
RA Fan C., Qian Y., Gong Y., Yang S.;
RT "Cloning, sequence analysis and expression in E. coli of the cDNA of
RT thrombin like enzyme (pallabin) from Agkistrodon halys pallas.";
RL Biochem. Mol. Biol. Int. 47:217-225(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.
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}.
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DR EMBL; AJ006472; CAA07055.1; -; mRNA.
DR AlphaFoldDB; Q9YGI6; -.
DR SMR; Q9YGI6; -.
DR MEROPS; S01.332; -.
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; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000028375"
FT CHAIN 25..260
FT /note="Snake venom serine protease pallabin-2"
FT /id="PRO_0000028376"
FT DOMAIN 25..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 98..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 202..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 260 AA; 28684 MW; 51042C058B0EC097 CRC64;
MVLIKVLANL LILQLSYAQK SSELIIGGDE CNINEHRFLV ALYTSRTLFC GGTLINQEWV
LTAAHCNMED IQIKLGMHSK KVPNEDEQKR VPKEKFFCLS SKNYTLWDKD IMLIRLDSPV
KNSAHIAPLS LPSSPPSVGS VCRTMGWGRI SSTKETYPDV PHCVNINLLE YEMCRAPYPE
FELPATSRTL CAGILEGGKD TCVGDSGGPL ICNGQFQGIA SWGDDPCAQP HKPAAYTKVF
DHLDWIENII AGNTDASCPP
