VSPUA_GLOUS
ID VSPUA_GLOUS Reviewed; 233 AA.
AC Q8UUJ1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Snake venom serine protease ussurase;
DE Short=SVSP;
DE EC=3.4.21.-;
OS Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=35671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Daolin D., Xiaodong D., Wenfang W., Anguo L., Mei X.;
RT "Cloning and analysis of cDNA for thrombin-like enzyme, ussurin and
RT ussurase, from Agkistrodon halys ussuriensis snake venom.";
RL She Zhi 13:1-9(2001).
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=AAL48222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF444251; AAL48222.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8UUJ1; -.
DR SMR; Q8UUJ1; -.
DR MEROPS; S01.350; -.
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; Toxin.
FT CHAIN 1..233
FT /note="Snake venom serine protease ussurase"
FT /id="PRO_0000295823"
FT DOMAIN 1..224
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 40
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 25..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 73..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 117..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 149..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 233 AA; 26017 MW; DC49A826164FECF7 CRC64;
VIGGVECNIN EHGFLALLYS RRFQCGGTLI NEEWVLTAAH CDMRNMYIYL GVHNVSVQYD
DEQRRYPKKK YFCLSSRNYN QWDKDIMLIR LNRPVRNSAH IAPLSLPSNP PSVGSVCRVM
GWGTITSPQE TLPDVPHCAN INILDYEVCR AAYPELPVTR RTLCAGILEG GKDSCNGDSG
GPLICNGQFQ GIAYWGADTC AQPREPGLYT KVFDYTDWIQ SIISGNTDAT CPQ
