VSP1_OPHHA
ID VSP1_OPHHA Reviewed; 260 AA.
AC A8QL56;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Alpha- and beta-fibrinogenase OhS1;
DE EC=3.4.21.-;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-47.
RC TISSUE=Venom, and 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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8079373; DOI=10.1016/0041-0101(94)90209-7;
RA Zhang Y., Lee W.H., Xiong Y.L., Wang W.Y., Zu S.W.;
RT "Characterization of OhS1, an arginine/lysine amidase from the venom of
RT king cobra (Ophiophagus hannah).";
RL Toxicon 32:615-623(1994).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Snake venom serine protease that possesses potent
CC fibrinogenolytic (on both alpha- (FGA) and beta-chains (FGB)) and
CC amidolytic activities. Selectively cleaves Arg-|-Xaa or Lys-|-Xaa
CC bonds. {ECO:0000269|PubMed:8079373}.
CC -!- ACTIVITY REGULATION: Completely inhibited by NPGB, PMSF,
CC diisopropylfluorophosphate (DFP), benzamidine and soybean trypsin
CC inhibitor. Not inhibited by EDTA. {ECO:0000269|PubMed:8079373}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8079373}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not hydrolyze casein. Does not clot fibrinogen or
CC act on factor X, prothrombin and plasminogen. Does not have hemorrhagic
CC activity (PubMed:8079373). {ECO:0000305|PubMed:8079373}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; EF080837; ABN72544.1; -; mRNA.
DR AlphaFoldDB; A8QL56; -.
DR SMR; A8QL56; -.
DR MEROPS; S01.481; -.
DR SABIO-RK; A8QL56; -.
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 Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|PubMed:17408712"
FT /id="PRO_0000417000"
FT CHAIN 25..260
FT /note="Alpha- and beta-fibrinogenase OhS1"
FT /id="PRO_0000417001"
FT DOMAIN 25..248
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 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 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
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..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 98..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 142..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 260 AA; 28656 MW; B2F4165133AC35AB CRC64;
MALIRVLASL LILQLSYAVT PFDRIIGGFE CNEYEHRSLV HLYNSSGFFC SGTLLNHEWV
LTAAHCNRDD IQIKLGVHNV SVNYEDEQIR VPKEKLCCHS TNNCTQLGQD IMLIRLNSSV
NYSEHIAPLS LPSNRPSMGS VCRVMGWGLL TSPEVTFPKV PHCVDINILH IQVCQAAYPS
MSENYLLCAG VLEGGKDSCK GDSGGPLICN REIQGIVSWG GFPCAQLLEP GVYTKVFDYI
DWIEGIIAGN TSVTCPSDNF
