VSPE2_GLOUS
ID VSPE2_GLOUS Reviewed; 258 AA.
AC O42207;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Thrombin-like enzyme CPI-enzyme 2;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Capillary permeability-increasing enzyme 2;
DE Flags: Precursor;
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;
RX PubMed=9839672; DOI=10.1016/s0041-0101(98)00109-3;
RA Hahn B.-S., Baek K., Kim W.-S., Lee C.-S., Chang I.-L., Kim Y.-S.;
RT "Molecular cloning of capillary permeability-increasing enzyme-2 from
RT Agkistrodon caliginosus (Korean viper).";
RL Toxicon 36:1887-1893(1998).
RN [2]
RP PROTEIN SEQUENCE OF 25-64, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=8303716; DOI=10.1016/0041-0101(93)90395-y;
RA Shimokawa K., Takahashi H.;
RT "Some properties of a capillary permeability-increasing enzyme-2 from the
RT venom of Agkistrodon caliginosus (Kankoku-mamushi).";
RL Toxicon 31:1221-1227(1993).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=8303715; DOI=10.1016/0041-0101(93)90394-x;
RA Shimokawa K., Takahashi H.;
RT "Purification of a capillary permeability-increasing enzyme-2 from the
RT venom of Agkistrodon caliginosus (Kankoku-mamushi).";
RL Toxicon 31:1213-1219(1993).
RN [4]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=9133714; DOI=10.1016/s0041-0101(96)00158-4;
RA Shimokawa K., Takahashi H.;
RT "Capillary permeability-increasing enzyme-2 from the venom of Agkistrodon
RT caliginosus (Kankoku-mamushi): activity resulting from the release of
RT peptides from fibrinogen.";
RL Toxicon 35:597-605(1997).
CC -!- FUNCTION: Thrombin-like snake venom serine protease that cleaves
CC fibrinogen beta (FGB) releasing fibrinopeptide B. Promotes capillary
CC permeability-increasing activity through the release of peptides from
CC the beta-chain of fibrinogen. {ECO:0000269|PubMed:8303715,
CC ECO:0000269|PubMed:8303716, ECO:0000269|PubMed:9133714}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF018568; AAB70575.1; -; mRNA.
DR AlphaFoldDB; O42207; -.
DR SMR; O42207; -.
DR MEROPS; S01.188; -.
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 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
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:0000269|PubMed:8303716"
FT /id="PRO_0000028371"
FT CHAIN 25..258
FT /note="Thrombin-like enzyme CPI-enzyme 2"
FT /id="PRO_0000028372"
FT DOMAIN 25..249
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 204
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
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..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 200..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 258 AA; 28523 MW; 55830E56E4D52397 CRC64;
MVLIRVLANL LILQLSYAQK SSELVIGGDE CNINEHRFLA LVFNSSGFLC SGTLINQEWV
LTAAHCDMEN MRIYLGVHNE SVQYDDEQTR VPEEKFFCLR SNNDTKWDKD IMLIRLDSPV
NNSAHIAPLN LPFNPPMLGS VCRIMGWGAI TSPNEIYSSV PHCANINVLH YSMCRAVYPG
MPAQTRILCA GIQTGGIDTC SGDSGGPLIC NGQFQGIVSW GRYPCAKPRA PGLYTRVFDY
TDWIENIIAG NTDASCPP
