ID   VSP1_BUNMU              Reviewed;         282 AA.
AC   A8QL57;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Snake venom serine protease BmSP;
DE            Short=SVSP;
DE            EC=3.4.21.-;
DE   Flags: Precursor; Fragment;
OS   Bungarus multicinctus (Many-banded krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17408712; DOI=10.1016/j.toxicon.2007.02.013;
RA   Jin Y., Lee W.H., Zhang Y.;
RT   "Molecular cloning of serine proteases from elapid snake venoms.";
RL   Toxicon 49:1200-1207(2007).
CC   -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC       system of the prey. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; EF080838; ABN72545.1; -; mRNA.
DR   AlphaFoldDB; A8QL57; -.
DR   SMR; A8QL57; -.
DR   MEROPS; S01.481; -.
DR   PRIDE; A8QL57; -.
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   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..56
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000417002"
FT   CHAIN           57..>282
FT                   /note="Snake venom serine protease BmSP"
FT                   /id="PRO_0000417003"
FT   DOMAIN          57..280
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        97
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        142
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        235
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        82..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        206..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        231..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         282
SQ   SEQUENCE   282 AA;  31010 MW;  F61135F59DB70F64 CRC64;
     MVLIGVLASL LILQLSYSKS LDDGAKESAY DDEIQQSSWG NSTVNTTLTE TVVIQLIMGG
     SECYKSKHPF LVYLYNSAGF FCSGTLLNHE WVLTAAHCNR DDIQLKLGVH NVHVHYEDEQ
     IRVPKEKLCC LSTKNCTQWS QDIMLIRLNS SVNNSKHIEP LSLPSRPPSM GSDCTVMGWG
     TITSPKVTYP KVPHCVDIKI LHNPVCQAAY PTMSRKNILC AGVLEGGKDS CKGDSGGPLI
     CDGQIQGIVS WGRFPCAQLL EPGVYTKVFD YIDWIKGIIA GN