VSP_BOMIG
ID VSP_BOMIG Reviewed; 360 AA.
AC B5U2W0;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Venom serine protease Bi-VSP;
DE EC=3.4.21.-;
DE AltName: Full=Thrombin-like enzyme;
DE Flags: Precursor;
OS Bombus ignitus (Bumblebee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Bombus; Bombus.
OX NCBI_TaxID=130704;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20454652; DOI=10.1371/journal.pone.0010393;
RA Choo Y.M., Lee K.S., Yoon H.J., Kim B.Y., Sohn M.R., Roh J.Y., Je Y.H.,
RA Kim N.J., Kim I., Woo S.D., Sohn H.D., Jin B.R.;
RT "Dual function of a bee venom serine protease: prophenoloxidase-activating
RT factor in arthropods and fibrin(ogen)olytic enzyme in mammals.";
RL PLoS ONE 5:E10393-E10393(2010).
RN [2]
RP FUNCTION.
RX PubMed=22359676; DOI=10.1371/journal.pone.0032269;
RA Choo Y.M., Lee K.S., Yoon H.J., Qiu Y., Wan H., Sohn M.R., Sohn H.D.,
RA Jin B.R.;
RT "Antifibrinolytic role of a bee venom serine protease inhibitor that acts
RT as a plasmin inhibitor.";
RL PLoS ONE 7:E32269-E32269(2012).
CC -!- FUNCTION: Multifunctional venom serine protease. In insects, it acts as
CC an arthropod prophenoloxidase-activating factor, thereby triggering the
CC phenoloxidase cascade. When injected into larvae, it induces a lethal
CC melanization response in target insects by modulating the innate immune
CC response. In mammals, it converts fibrinogen into fibrin, activates
CC prothrombin, and also degrades fibrin. In mammal, it may act in a
CC cooperative manner with the serine protease inhibitor Bi-KTI (AC
CC G3LH89) to promote the spread of bee venom under anti-bleeding
CC conditions. {ECO:0000269|PubMed:20454652, ECO:0000269|PubMed:22359676}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236}.
CC -!- MISCELLANEOUS: Does not activate plasminogen.
CC {ECO:0000305|PubMed:20454652}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236}.
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DR EMBL; FJ159442; ACI01044.1; -; Genomic_DNA.
DR EMBL; FJ159443; ACI01045.1; -; mRNA.
DR AlphaFoldDB; B5U2W0; -.
DR SMR; B5U2W0; -.
DR MEROPS; S01.511; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
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 Gene3D; 3.30.1640.30; -; 1.
DR InterPro; IPR022700; CLIP.
DR InterPro; IPR038565; CLIP_sf.
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; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51888; CLIP; 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 Blood coagulation cascade activating toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Fibrinolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Protease; Prothrombin activator; Secreted; Serine protease; Signal; Toxin;
KW Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..113
FT /id="PRO_0000429470"
FT CHAIN 114..360
FT /note="Venom serine protease Bi-VSP"
FT /id="PRO_0000429471"
FT DOMAIN 28..79
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 114..360
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 311
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 39..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 45..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 104..230
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 147..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 278..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 307..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 360 AA; 39461 MW; D77EC2EF06BEC139 CRC64;
MTGSKMLFAC LALIAFLHPL VHVASAQECT TPNNKAGKCL GIRVCKPLLE MLQTQGHAAA
DFLRQSVCKY ENNNPIVCCP NEESREDRGI LVGNEYEPLR PPHCGFSNVS HTRVVGGKPA
VLGAWPWIAA LGFRYPRNPA LEPLWKCGGS LISSRHVLTA AHCAEINELY VVRIGDLNLV
RNDDGAHPVQ IEIESKIIHP DYISGVTKHD IAILKLVEEV PFSEYVYPIC LPVEDNLRNN
NFERYYPFVA GWGSLAHHGP GSDDLMEVQV PVISNTECKN SYARFAAAHV TDTVLCAGYT
QGGKDACQGD SGGPLMLPKK FTFYQIGVVS YGHKCAAAGY PGVYTRVTSY LDDFILPAMQ
