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Venom plasminogen activator LV-PA (EC 3.4.21.-) (LMUT0402S) (Plasminogen activating proteinase) (Snake venom serine protease) (SVSP)

 VSPPA_LACMU             Reviewed;         258 AA.
Q27J47; P84036;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 1.
12-SEP-2018, entry version 54.
RecName: Full=Venom plasminogen activator LV-PA;
EC=3.4.21.-;
AltName: Full=LMUT0402S;
AltName: Full=Plasminogen activating proteinase;
AltName: Full=Snake venom serine protease;
Short=SVSP;
Flags: Precursor;
Lachesis muta muta (Bushmaster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
NCBI_TaxID=8753;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-204 AND 223-258,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
TISSUE=Venom, and Venom gland;
PubMed=17034951; DOI=10.1016/j.bbagen.2006.08.023;
Sanchez E.F., Felicori L.F., Chavez-Olortegui C., Magalhaes H.B.,
Hermogenes A.L., Diniz M.R.V., Junqueira-de-Azevedo I.L.M.,
Magalhaes A., Richardson M.;
"Biochemical characterization and molecular cloning of a plasminogen
activator proteinase (LV-PA) from bushmaster snake venom.";
Biochim. Biophys. Acta 1760:1762-1771(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16582429; DOI=10.1534/genetics.106.056515;
Junqueira-de-Azevedo I.L.M., Ching A.T.C., Carvalho E., Faria F.,
Nishiyama M.Y. Jr., Ho P.L., Diniz M.R.V.;
"Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules
and scaffolds typical of cobra (Elapidae) venoms: implications for
snake toxin repertoire evolution.";
Genetics 173:877-889(2006).
[3]
PROTEIN SEQUENCE OF 25-64, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
REGULATION, AND GLYCOSYLATION.
STRAIN=Manaus; TISSUE=Venom;
PubMed=10871053; DOI=10.1006/abbi.2000.1781;
Sanchez E.F., Santos C.I., Magalhaes A., Diniz C.R., Figueiredo S.,
Gilroy J., Richardson M.;
"Isolation of a proteinase with plasminogen-activating activity from
Lachesis muta muta (bushmaster) snake venom.";
Arch. Biochem. Biophys. 378:131-141(2000).
-!- FUNCTION: Snake venom serine protease that activates plasminogen.
Weakly hydrolyzes the alpha chain of human fibrinogen without
releasing fibrinopeptide A. Does not hydrolyze plasma kallikrein
or factor Xa. Does not clot fibrinogen. Does not affect platelet
function. Induces hypotensive effects on rats. Shows a
preferential cleavage at Lys-|-Xaa over Arg-|-Xaa bonds.
{ECO:0000269|PubMed:10871053, ECO:0000269|PubMed:17034951}.
-!- ACTIVITY REGULATION: Inhibited by the serine protease inhibitors
NPGB, PMSF, p-aminobenzamidine and aprotinin. Not inhibited by
soybean trypsin inhibitor or EDTA. {ECO:0000269|PubMed:10871053}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=174 uM for H-D-Val-Leu-Arg-pNA (S-2266)
{ECO:0000269|PubMed:17034951};
KM=131 uM for H-D-Val-Leu-Lys-pNA (S-2251)
{ECO:0000269|PubMed:17034951};
KM=67 uM for N-p-Tos-Gly-Pro-Lys-pNA
{ECO:0000269|PubMed:17034951};
KM=231 uM for H-D-Pro-Phe-Arg-pNA (S-2302)
{ECO:0000269|PubMed:17034951};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17034951}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17034951}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:17034951}.
-!- PTM: N-glycosylated. PubMed:17034951 shows that it contains
approximately 10% carbohydrates, PubMed:10871053 shows that it
contains approximately 20% carbohydrates.
{ECO:0000269|PubMed:10871053, ECO:0000269|PubMed:17034951}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; DQ396477; ABD52886.1; -; mRNA.
ProteinModelPortal; Q27J47; -.
SMR; Q27J47; -.
MEROPS; S01.497; -.
HOVERGEN; HBG013304; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Fibrinolytic toxin;
Glycoprotein; Hemostasis impairing toxin; Hydrolase;
Hypotensive agent; Plasminogen activation; Protease; Secreted;
Serine protease; Signal; Toxin.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 24 {ECO:0000269|PubMed:10871053,
ECO:0000269|PubMed:17034951}.
/FTId=PRO_0000294998.
CHAIN 25 258 Venom plasminogen activator LV-PA.
/FTId=PRO_0000088741.
DOMAIN 25 249 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system. {ECO:0000250}.
ACT_SITE 110 110 Charge relay system. {ECO:0000250}.
ACT_SITE 204 204 Charge relay system. {ECO:0000250}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 66 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 142 210 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 174 189 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 200 225 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 46 46 S -> N (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 75 75 L -> V (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 104 106 NDE -> DEM (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 127 127 A -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 149 149 T -> K (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 177 182 AYSGWL -> IYPEFGLP (in Ref. 1; AA
sequence). {ECO:0000305}.
CONFLICT 186 187 TT -> RV (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 230 230 E -> K (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 258 AA; 28062 MW; 617E3B8CC154BEA0 CRC64;
MVLITVLANL LILQLSYAQK SSKLVFGGDE CNINEHRSLV VLFNSSGFLC AGTLINKEWV
LTAAHCDSEN FQMQLGVHSK KVPNKDEETR DPKEKFICPN RKKNDEKDKD IMLIRLNRPV
SNSEHIALLS LPSSPPSVGS VCRIMGWGTI SPTKEIYPDV PHCADINILD HAVCRAAYSG
WLATSTTLCA GILEGGKDSC HGDSGGPLIC NGQFQGIVSL GRHPCGHPDE PGVYTKVFDY
TDWIQSIIAG NTDAACPP


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