ID   VSP1_MACLB              Reviewed;         260 AA.
AC   E0Y418;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Serine protease VLSP-1;
DE            EC=3.4.21.-;
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;
RA   Siigur E., Aaspollu A., Siigur J.;
RT   "Serine proteases from Vipera lebetina snake venom.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC       system of the prey. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The nucleotide accession number of this protein has been
CC       wrongly cited in a publication which is available in the nucleotide
CC       entry. {ECO:0000305}.
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DR   EMBL; GU570565; ADN04916.1; -; mRNA.
DR   AlphaFoldDB; E0Y418; -.
DR   SMR; E0Y418; -.
DR   MEROPS; S01.497; -.
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   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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000416397"
FT   CHAIN           25..260
FT                   /note="Serine protease VLSP-1"
FT                   /id="PRO_0000416398"
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        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
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   260 AA;  28702 MW;  E6C9B13CDD8F7E06 CRC64;
     MVLIRVLANL LVLHLSYAQK SSELVIGGDE CNINEHPFLA LMYNSTSMKF HCSGTLLNEE
     WVLTAAHCDM ENMQIYLGVH DKKNPNKDQQ TRVPKEMFFC LSNKSYTPWD KDIMLIRLNS
     PVTYSTHIAP FSLPSSPPTV GSVCRIMGWG AITSPNETYP DVPHCANIEI YDYSVCRKAY
     GGLPEKSRTL CAGVLQGGID TCLADSGGPL ICNGQFQGIV AWGRHPCAQP QLPAFYTKVF
     DYSDWIQSII AGNTAATCPS