VSPG_DABSI
ID VSPG_DABSI Reviewed; 260 AA.
AC P18965; E5L0E2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Factor V activator RVV-V gamma;
DE EC=3.4.21.95;
DE AltName: Full=Russel's viper venom FV activator gamma;
DE Short=RVV-V gamma;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=21640745; DOI=10.1016/j.toxicon.2011.05.014;
RA Sukkapan P., Jia Y., Nuchprayoon I., Perez J.C.;
RT "Phylogenetic analysis of serine proteases from Russell's viper (Daboia
RT russelli siamensis) and Agkistrodon piscivorus leucostoma venom.";
RL Toxicon 58:168-178(2011).
RN [2]
RP PROTEIN SEQUENCE OF 25-260, FUNCTION, AND GLYCOSYLATION AT ASN-253.
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 [3]
RP CRYSTALLIZATION.
RX PubMed=20054136; DOI=10.1107/s1744309109046697;
RA Nakayama D., Ben Ammar Y., Takeda S.;
RT "Crystallization and preliminary X-ray crystallographic analysis of blood
RT coagulation factor V-activating proteinase (RVV-V) from Russell's viper
RT venom.";
RL Acta Crystallogr. F 65:1306-1308(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-260, ACTIVE SITE, AND DISULFIDE
RP BONDS.
RX PubMed=21871889; DOI=10.1016/j.febslet.2011.08.022;
RA Nakayama D., Ben Ammar Y., Miyata T., Takeda S.;
RT "Structural basis of coagulation factor V recognition for cleavage by RVV-
RT V.";
RL FEBS Lett. 585:3020-3025(2011).
CC -!- FUNCTION: Venom serine protease that selectively activates factor V
CC (F5) in a calcium-independent manner. It cleaves the Arg(1545)-
CC Ser(1546) linkage in the human factor V molecule. Induces the
CC coagulation of mammalian plasma. {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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3053712}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: There are three isoproteins of RVV-V, designated RVV-V
CC alpha, V-beta, and V-gamma. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ270463; ADP88558.1; -; mRNA.
DR PIR; B32121; B32121.
DR PDB; 3S9A; X-ray; 1.90 A; A=25-260.
DR PDB; 3S9B; X-ray; 1.90 A; A=25-260.
DR PDB; 3S9C; X-ray; 1.80 A; A=25-260.
DR PDB; 3SBK; X-ray; 2.55 A; A=25-260.
DR PDBsum; 3S9A; -.
DR PDBsum; 3S9B; -.
DR PDBsum; 3S9C; -.
DR PDBsum; 3SBK; -.
DR AlphaFoldDB; P18965; -.
DR SMR; P18965; -.
DR MEROPS; S01.184; -.
DR iPTMnet; P18965; -.
DR BRENDA; 3.4.21.95; 6667.
DR EvolutionaryTrace; P18965; -.
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 3D-structure; Blood coagulation cascade activating toxin;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:3053712"
FT /id="PRO_0000432323"
FT CHAIN 25..260
FT /note="Factor V activator RVV-V gamma"
FT /id="PRO_0000088739"
FT DOMAIN 25..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 67
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21871889"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21871889"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:21871889"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3053712"
FT DISULFID 31..165
FT /evidence="ECO:0000269|PubMed:21871889,
FT ECO:0007744|PDB:3S9A, ECO:0007744|PDB:3S9B,
FT ECO:0007744|PDB:3S9C, ECO:0007744|PDB:3SBK"
FT DISULFID 52..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21871889, ECO:0007744|PDB:3S9A,
FT ECO:0007744|PDB:3S9B, ECO:0007744|PDB:3S9C,
FT ECO:0007744|PDB:3SBK"
FT DISULFID 100..258
FT /evidence="ECO:0000269|PubMed:21871889,
FT ECO:0007744|PDB:3S9A, ECO:0007744|PDB:3S9B,
FT ECO:0007744|PDB:3S9C, ECO:0007744|PDB:3SBK"
FT DISULFID 144..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21871889, ECO:0007744|PDB:3S9A,
FT ECO:0007744|PDB:3S9B, ECO:0007744|PDB:3S9C,
FT ECO:0007744|PDB:3SBK"
FT DISULFID 176..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21871889, ECO:0007744|PDB:3S9A,
FT ECO:0007744|PDB:3S9B, ECO:0007744|PDB:3S9C,
FT ECO:0007744|PDB:3SBK"
FT DISULFID 202..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:21871889, ECO:0007744|PDB:3S9A,
FT ECO:0007744|PDB:3S9B, ECO:0007744|PDB:3S9C,
FT ECO:0007744|PDB:3SBK"
FT CONFLICT 203
FT /note="H -> K (in Ref. 1; ADP88558)"
FT /evidence="ECO:0000305"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 47..58
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3S9C"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3S9C"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3SBK"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:3S9C"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3S9C"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:3S9C"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3S9C"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3S9C"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:3S9C"
SQ SEQUENCE 260 AA; 28823 MW; CDFC23F40C0EC8F1 CRC64;
MVLIKVLANL LVLQLSYAQK SSELVVGGDE CNINEHPFLV ALYTSASSTI HCAGALINRE
WVLTAAHCDR RNIRIKLGMH SKNIRNEDEQ IRVPRGKYFC LNTKFPNGLD KDIMLIRLRR
PVTYSTHIAP VSLPSRSRGV GSRCRIMGWG KISTTEDTYP DVPHCTNIFI VKHKWCEPLY
PWVPADSRTL CAGILKGGRD TCHGDSGGPL ICNGEMHGIV AGGSEPCGQH LKPAVYTKVF
DYNNWIQSII AGNRTVTCPP
