VSPF5_MACLB
ID VSPF5_MACLB Reviewed; 259 AA.
AC Q9PT41;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Factor V activator;
DE Short=FVA;
DE Short=VLFVA;
DE EC=3.4.21.95;
DE AltName: Full=Lebetina viper venom FV activator;
DE Short=LVV-V;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=8709;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=10462474; DOI=10.1006/bbrc.1999.1200;
RA Siigur E., Aaspollu A., Siigur J.;
RT "Molecular cloning and sequence analysis of a cDNA for factor V activating
RT enzyme.";
RL Biochem. Biophys. Res. Commun. 262:328-332(1999).
RN [2]
RP PROTEIN SEQUENCE OF 25-54, FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=9920400; DOI=10.1016/s0167-4838(98)00232-5;
RA Siigur E., Samel M., Tonismagi K., Subbi J., Reintamm T., Siigur J.;
RT "Isolation, properties and N-terminal amino acid sequence of a factor V
RT activator from Vipera lebetina (Levantine viper) snake venom.";
RL Biochim. Biophys. Acta 1429:239-248(1998).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND 3D-STRUCTURE MODELING.
RC STRAIN=Turanica; 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).
RN [4]
RP FUNCTION, GLYCOSYLATION, AND SIALIC ACID CONTENT.
RX PubMed=11910177; DOI=10.1159/000048055;
RA Siigur J., Aaspollu A., Tonismagi K., Trummal K., Samel M., Vija H.,
RA Subbi J., Siigur E.;
RT "Proteases from Vipera lebetina venom affecting coagulation and
RT fibrinolysis.";
RL Haemostasis 31:123-132(2001).
CC -!- FUNCTION: Venom serine protease that converts factor V (F5) to the
CC active form Va in the presence of calcium ions and phospholipids. It
CC cleaves the Arg(1545)-Ser(1546) linkage in the human factor V molecule.
CC Has hydrolytic activities against BAEE (1.2 U/mg), TAME, and Pro-Phe-
CC Arg-MCA (4.9 U/mg). Shows coagulant activity.
CC {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:16807918,
CC ECO:0000269|PubMed:9920400}.
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) (98%), PMSF (93%), benzamidine (67%), and
CC diisopropylfluorophosphate (DFP). Is not inhibited by BPTI,
CC antithrombin and EDTA. {ECO:0000269|PubMed:16807918,
CC ECO:0000269|PubMed:9920400}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9920400}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated. Contains 4.4% of hexoses, 4.4% of hexosamines and
CC 3.1% of sialic acids. {ECO:0000269|PubMed:11910177}.
CC -!- MASS SPECTROMETRY: Mass=28400; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9920400};
CC -!- MISCELLANEOUS: Does not hydrolyze casein or asocasein, prothrombin,
CC fibrinogen and fibrin. Does not induce or inhibit platelet aggregation
CC (PubMed:9920400). {ECO:0000305|PubMed:9920400}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF163973; AAF03233.1; -; mRNA.
DR AlphaFoldDB; Q9PT41; -.
DR SMR; Q9PT41; -.
DR MEROPS; S01.429; -.
DR BRENDA; 3.4.21.95; 6665.
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; 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; 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; Sialic acid; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:9920400"
FT /id="PRO_0000028423"
FT CHAIN 25..259
FT /note="Factor V activator"
FT /id="PRO_0000028424"
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:0000250"
FT ACT_SITE 112
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 52..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 100..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 144..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 176..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 202..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 259 AA; 28595 MW; 5F2256F1B576B12B CRC64;
MVLIRVLANL LVLQLSYAQK SSELVVGGDE CDINEHPFLV ALYTSSSSTV HCAGTLINQE
WVLTAVHCDR KNIRIKLGMH SKNIRNEDEQ IRVPRRKFFC LNTKFPNGKD KDIMLIRLRR
PVKNSAHIAP ISLPSSPSSP RSRCRIMGWG KISTTEETYP DVPHCAKIFI VKHAWCEALY
PWVPADSRTL CAGILQGGKD TCEGDSGGPL ICNGQIQGIV SGGSDPCGQR LKPAVYTKVF
DYTDWIQSII AGNTTATCP
