VSPC1_CROAT
ID VSPC1_CROAT Reviewed; 75 AA.
AC Q7LZF5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Thrombin-like enzyme catroxobin-1;
DE Short=SVTLE;
DE EC=3.4.21.-;
DE AltName: Full=Catroxobin I;
DE AltName: Full=Fibrinogen-clotting enzyme;
DE AltName: Full=Snake venom serine protease;
DE Short=SVSP;
DE Flags: Fragments;
OS Crotalus atrox (Western diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8730;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=2617466; DOI=10.1016/0049-3848(89)90158-8;
RA Pirkle H., Theodor I., Lopez R.;
RT "Catroxobin, a weakly thrombin-like enzyme from the venom of Crotalus
RT atrox. NH2-terminal and active site amino acid sequences.";
RL Thromb. Res. 56:159-168(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-23, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19371136; DOI=10.1021/pr900249q;
RA Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT "Exploring the venom proteome of the western diamondback rattlesnake,
RT Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT approaches.";
RL J. Proteome Res. 8:3055-3067(2009).
CC -!- FUNCTION: Thrombin-like snake venom serine protease. Clots fibrinogen
CC (FGA and FGB) very slowly, releasing fibrinopeptide A and a small
CC amount of fibrinopeptide B. {ECO:0000269|PubMed:2617466}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2617466}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:2617466}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR PIR; A37002; A37002.
DR AlphaFoldDB; Q7LZF5; -.
DR SMR; Q7LZF5; -.
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 Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR SUPFAM; SSF50494; SSF50494; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW Serine protease; Toxin.
FT CHAIN 1..>75
FT /note="Thrombin-like enzyme catroxobin-1"
FT /id="PRO_0000296306"
FT DOMAIN 1..75
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 41
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 60
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 26..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT NON_CONS 42..43
FT /evidence="ECO:0000305"
FT NON_TER 75
SQ SEQUENCE 75 AA; 7593 MW; 0B5DD9FF7C019E77 CRC64;
VVGGDECNIN EHRSLVAIFV STEFDCGGDL INVEWVLTAA HCTLCAGIPE GGLDTCGGDS
GGPLICDGKP DGITS
