VSPD_GLOUS
ID VSPD_GLOUS Reviewed; 234 AA.
AC Q7SZE2; P86171;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Bradykinin-releasing enzyme KR-E-1;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Thrombin-like enzyme defibrase;
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 Sun D.-J., Yang T.-S.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=18723043; DOI=10.1016/j.toxicon.2008.07.014;
RA Oyama E., Fukuda T., Takahashi H.;
RT "Amino acid sequence of a kinin-releasing enzyme, KR-E-1, from the venom of
RT Agkistrodon caliginosus (Kankoku-mamushi).";
RL Toxicon 52:651-654(2008).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=3201479; DOI=10.1016/0041-0101(88)90254-1;
RA Ohtani Y., Yabuki Y., Mimura M., Takahashi H.;
RT "Purification of a kininogenase from the venom of Agkistrodon caliginosus
RT (Kankoku-Mamushi).";
RL Toxicon 26:891-901(1988).
CC -!- FUNCTION: Bradykinin-releasing enzyme. Releases bradykinin from bovine
CC HMW kininogen. Has anticoagulant activity. Increases permeability of
CC capillaries by intradermal injection into rabbits.
CC {ECO:0000269|PubMed:3201479}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not show a thrombin-like activity.
CC {ECO:0000305|PubMed:18723043}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AY204242; AAP20637.1; -; mRNA.
DR AlphaFoldDB; Q7SZE2; -.
DR SMR; Q7SZE2; -.
DR MEROPS; S01.023; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB.
DR GO; GO:0002353; P:plasma kallikrein-kinin cascade; IDA:UniProtKB.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Secreted; Serine protease; Toxin.
FT CHAIN 1..234
FT /note="Bradykinin-releasing enzyme KR-E-1"
FT /id="PRO_0000295820"
FT DOMAIN 1..225
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 180
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 118..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 150..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 176..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 2
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="N -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="N -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..234
FT /note="DASCPP -> AATCSSF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 25352 MW; 0124C1485525F560 CRC64;
VIGGDECNIN EHRSLVAFFN STGFFCSGTL VNEEWVLSAA HCDSTNFQMK LGVHSKKVLN
EDEQTRNPKE KFICPNKKND EVLDKDIMLI KLDSRVSNSE HIAPLSLPSS PPSVGSVCHI
MGWGSITPIK ETYPDVPYCA NINLLDDEVC QAGYPELLAE YRTLCAGILE GGKDTCGGDS
GGPLICNGQF QGIVSYGAHP CGQSLKPGIY TKVFDYSDWI QSIIAGNTDA SCPP
