VSPPA_LACMU
ID VSPPA_LACMU Reviewed; 258 AA.
AC Q27J47; P84036;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Venom plasminogen activator LV-PA;
DE EC=3.4.21.-;
DE AltName: Full=LMUT0402S;
DE AltName: Full=Plasminogen activating proteinase;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Lachesis muta muta (Bushmaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX NCBI_TaxID=8753;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-204 AND 223-258,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17034951; DOI=10.1016/j.bbagen.2006.08.023;
RA Sanchez E.F., Felicori L.F., Chavez-Olortegui C., Magalhaes H.B.,
RA Hermogenes A.L., Diniz M.R.V., Junqueira-de-Azevedo I.L.M., Magalhaes A.,
RA Richardson M.;
RT "Biochemical characterization and molecular cloning of a plasminogen
RT activator proteinase (LV-PA) from bushmaster snake venom.";
RL Biochim. Biophys. Acta 1760:1762-1771(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16582429; DOI=10.1534/genetics.106.056515;
RA Junqueira-de-Azevedo I.L.M., Ching A.T.C., Carvalho E., Faria F.,
RA Nishiyama M.Y. Jr., Ho P.L., Diniz M.R.V.;
RT "Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules and
RT scaffolds typical of cobra (Elapidae) venoms: implications for snake toxin
RT repertoire evolution.";
RL Genetics 173:877-889(2006).
RN [3]
RP PROTEIN SEQUENCE OF 25-64, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND GLYCOSYLATION.
RC STRAIN=Manaus; TISSUE=Venom;
RX PubMed=10871053; DOI=10.1006/abbi.2000.1781;
RA Sanchez E.F., Santos C.I., Magalhaes A., Diniz C.R., Figueiredo S.,
RA Gilroy J., Richardson M.;
RT "Isolation of a proteinase with plasminogen-activating activity from
RT Lachesis muta muta (bushmaster) snake venom.";
RL Arch. Biochem. Biophys. 378:131-141(2000).
CC -!- FUNCTION: Snake venom serine protease that activates plasminogen.
CC Weakly hydrolyzes the alpha chain of human fibrinogen without releasing
CC fibrinopeptide A. Does not hydrolyze plasma kallikrein or factor Xa.
CC Does not clot fibrinogen. Does not affect platelet function. Induces
CC hypotensive effects on rats. Shows a preferential cleavage at Lys-|-Xaa
CC over Arg-|-Xaa bonds. {ECO:0000269|PubMed:10871053,
CC ECO:0000269|PubMed:17034951}.
CC -!- ACTIVITY REGULATION: Inhibited by the serine protease inhibitors NPGB,
CC PMSF, p-aminobenzamidine and aprotinin. Not inhibited by soybean
CC trypsin inhibitor or EDTA. {ECO:0000269|PubMed:10871053}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=174 uM for H-D-Val-Leu-Arg-pNA (S-2266)
CC {ECO:0000269|PubMed:17034951};
CC KM=131 uM for H-D-Val-Leu-Lys-pNA (S-2251)
CC {ECO:0000269|PubMed:17034951};
CC KM=67 uM for N-p-Tos-Gly-Pro-Lys-pNA {ECO:0000269|PubMed:17034951};
CC KM=231 uM for H-D-Pro-Phe-Arg-pNA (S-2302)
CC {ECO:0000269|PubMed:17034951};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17034951}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17034951}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17034951}.
CC -!- PTM: N-glycosylated. PubMed:17034951 shows that it contains
CC approximately 10% carbohydrates, PubMed:10871053 shows that it contains
CC approximately 20% carbohydrates. {ECO:0000269|PubMed:10871053,
CC ECO:0000269|PubMed:17034951}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; DQ396477; ABD52886.1; -; mRNA.
DR AlphaFoldDB; Q27J47; -.
DR SMR; Q27J47; -.
DR MEROPS; S01.497; -.
DR SABIO-RK; Q27J47; -.
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 GO; GO:0008217; P:regulation of blood pressure; 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 Direct protein sequencing; Disulfide bond; Fibrinolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Hypotensive agent;
KW Plasminogen activation; Protease; Secreted; Serine protease; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:10871053,
FT ECO:0000269|PubMed:17034951"
FT /id="PRO_0000294998"
FT CHAIN 25..258
FT /note="Venom plasminogen activator LV-PA"
FT /id="PRO_0000088741"
FT DOMAIN 25..249
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 200..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 46
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="L -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..106
FT /note="NDE -> DEM (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="A -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="T -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..182
FT /note="AYSGWL -> IYPEFGLP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..187
FT /note="TT -> RV (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="E -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
