VSPA_DABSI
ID VSPA_DABSI Reviewed; 236 AA.
AC P18964;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Factor V activator RVV-V alpha;
DE EC=3.4.21.95;
DE AltName: Full=Russel's viper venom FV activator alpha;
DE Short=RVV-V alpha;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
OS Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=343250;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=3053712; DOI=10.1016/s0021-9258(19)77860-0;
RA Tokunaga F., Nagasawa K., Tamura S., Miyata T., Iwanaga S., Kisiel W.;
RT "The factor V-activating enzyme (RVV-V) from Russell's viper venom.
RT Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their
RT complete amino acid sequences.";
RL J. Biol. Chem. 263:17471-17481(1988).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=16807918; DOI=10.1002/prot.21051;
RA Segers K., Rosing J., Nicolaes G.A.;
RT "Structural models of the snake venom factor V activators from Daboia
RT russelli and Daboia lebetina.";
RL Proteins 64:968-984(2006).
CC -!- FUNCTION: Venom serine protease that activates factor V (F5) in a
CC calcium-independent manner. It cleaves the Arg(1545)-Ser(1546) linkage
CC in the human factor V molecule. Induces the coagulation of mammalian
CC plasma. {ECO:0000269|PubMed:16807918, ECO:0000269|PubMed:3053712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fully activates human clotting factor V by a single cleavage
CC at the 1545-Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but
CC not rabbit, factor V is cleaved, and no other proteins of the
CC clotting system are attacked. Esterase activity is observed on Bz-
CC Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-
CC NHPhNO2.; EC=3.4.21.95;
CC -!- ACTIVITY REGULATION: Inhibited by D-Phe-Pro-Arg-chloromethyl ketone
CC (FPRCK) (97%), PMSF (76%), and benzamidine (50%). Is not inhibited by
CC BPTI, antithrombin and EDTA. {ECO:0000269|PubMed:16807918}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: There are three isoproteins of RVV-V, designated RVV-V
CC alpha, V-beta, and V-gamma.
CC -!- MISCELLANEOUS: Has no proteolytic effect on factor VIII, factor XIII,
CC fibrinogen, and prothrombin. {ECO:0000305|PubMed:16807918}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; A32121; A32121.
DR AlphaFoldDB; P18964; -.
DR SMR; P18964; -.
DR MEROPS; S01.184; -.
DR iPTMnet; P18964; -.
DR BRENDA; 3.4.21.95; 6667.
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; Toxin.
FT CHAIN 1..236
FT /note="Factor V activator RVV-V alpha"
FT /id="PRO_0000088738"
FT DOMAIN 1..227
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 88
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3053712"
FT DISULFID 7..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 28..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 76..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 120..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 152..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 178..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 236 AA; 26182 MW; 24ECBD93CB442502 CRC64;
VVGGDECNIN EHPFLVALYT STSSTIHCGG ALINREWVLT AAHCDRRNIR IKLGMHSKNI
RNEDEQIRVP RGKYFCLNTK FPNGLDKDIM LIRLRRPVTY STHIAPVSLP SRSRGVGSRC
RIMGWGKIST TEDTYPDVPH CTNIFIVKHK WCEPLYPWVP ADSRTLCAGI LKGGRDTCHG
DSGGPLICNG QIQGIVAGGS EPCGQHLKPA VYTKVFDYNN WIQNIIAGNR TVTCPP
