VSPY_MACLB
ID VSPY_MACLB Reviewed; 257 AA.
AC E0Y421;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Chymotrypsin-like protease VLCTLP;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE AltName: Full=Vipera Lebetina with chymotrypsin-like proteolytic activity;
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=12719779; DOI=10.1267/THRO03050826;
RA Siigur E., Aaspollu A., Siigur J.;
RT "Anticoagulant serine fibrinogenases from Vipera lebetina venom: structure-
RT function relationships.";
RL Thromb. Haemost. 89:826-831(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20950666; DOI=10.1016/j.biochi.2010.10.004;
RA Siigur E., Tonismagi K., Trummal K., Samel M., Vija H., Aaspollu A.,
RA Ronnholm G., Subbi J., Kalkkinen N., Siigur J.;
RT "A new tyrosine-specific chymotrypsin-like and angiotensin-degrading serine
RT proteinase from Vipera lebetina snake venom.";
RL Biochimie 93:321-330(2011).
CC -!- FUNCTION: Snake venom serine protease with tyrosine-specific
CC chymotrypsin-like activity. Hydrolyzes the N-acetyl-L-tyrosine ethyl
CC ester (ATEE). Has weak fibrinogenolytic activity. Weakly hydrolyzes
CC azocasein, Aalpha-chain (FGA) and more slowly Bbeta-chain (FGB) of
CC fibrinogen. Optimal substrates are angiotensins I and II (AGT).
CC {ECO:0000269|PubMed:20950666}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:20950666}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Partial deglycosylation has not effect on enzyme activity.
CC -!- MASS SPECTROMETRY: Mass=41926; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20950666};
CC -!- MISCELLANEOUS: Does not cleave the gamma chain of fibrinogen, does not
CC show fibrinolytic activity, and does not induce or inhibit platelet
CC aggregation. {ECO:0000305|PubMed:20950666}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: The nucleotide accession number corresponding to this protein
CC cited in PubMed:20950666 is wrongly indicated as being GU570565.
CC {ECO:0000305}.
CC -!- CAUTION: The sequence provided in PubMed:12719779 is indicated as being
CC Beta-fibrinogenase (VLBF). {ECO:0000305}.
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DR EMBL; GU570568; ADN04919.1; -; mRNA.
DR AlphaFoldDB; E0Y421; -.
DR SMR; E0Y421; -.
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 Disulfide bond; Fibrinogenolytic toxin; 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:0000250"
FT /id="PRO_0000416401"
FT CHAIN 25..257
FT /note="Chymotrypsin-like protease VLCTLP"
FT /id="PRO_0000416402"
FT DOMAIN 25..248
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 97..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 257 AA; 28278 MW; F4706E35E11B0610 CRC64;
MVLIRVLANL LLLQLSYAQK SSELVVGGDE CNINEHRSLV FLYNSSFGCG GTLINQQWVL
SAAHCDMENV QIYLGLHNLR LRNQDEQIRV AEEKFFCLSN KSYTKWDKDI MLIRLNSSVT
YNTHIAPLSL PSSPPRVGSV CRIMGWGAIT SPNETFPNVP HCANINILRY SVCRAAYRGL
PAQSRTLCAG ILQGGIGSCM GDSGGPLICN GEIQGIVSWG DDICAQPHKP VHYTKVFDYS
DWIQSIIAGN TTATCPL
