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 04-NOV-2026, entry version 123. 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, ACTIVE SITE, AND DISULFIDE 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 AlphaFoldDB; P18965; -. DR SMR; P18965; -. DR MEROPS; S01.184; -. DR GlyCosmos; P18965; 1 site, No reported glycans. DR iPTMnet; P18965; -. DR BRENDA; 3.4.21.95; 6667. DR EvolutionaryTrace; P18965; -. DR GO; GO:0005576; C:extracellular region; EXP:UniProtKB. DR GO; GO:0030141; C:secretory granule; IEA:TreeGrafter. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0035821; P:modulation of process of another organism; IEA:UniProtKB-ARBA. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd00190; Tryp_SPc; 1. DR FunFam; 2.40.10.10:FF:000010; Kallikrein related peptidase 11; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24271:SF47; KALLIKREIN-1; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 HELIX 130..134 FT /evidence="ECO:0007829|PDB:3S9A" 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 //