ID   VSPF2_CALRH             Reviewed;         258 AA.
AC   P47797;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Thrombin-like enzyme ancrod-2;
DE            Short=SVTLE;
DE            EC=3.4.21.74;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   AltName: Full=Venombin A;
DE   Flags: Precursor;
OS   Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX   NCBI_TaxID=8717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=8373353; DOI=10.1042/bj2940387;
RA   Au L.-C., Lin S.-B., Chou J.-S., Teh G.-W., Chang K.-J., Shih C.-M.;
RT   "Molecular cloning and sequence analysis of the cDNA for ancrod, a
RT   thrombin-like enzyme from the venom of Calloselasma rhodostoma.";
RL   Biochem. J. 294:387-390(1993).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease. Cleaves fibrinogen
CC       (FGA) to split of fibrinopeptides AM, AO, and AY; the aberrant
CC       fibrinogen is then incapable of being cross-linked, forming easily
CC       dispersible clots.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form
CC         fibrin, and release fibrinopeptide A. The specificity of further
CC         degradation of fibrinogen varies with species origin of the enzyme.;
CC         EC=3.4.21.74;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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; L07308; AAA49195.1; -; mRNA.
DR   PIR; S36783; S36783.
DR   AlphaFoldDB; P47797; -.
DR   SMR; P47797; -.
DR   MEROPS; S01.178; -.
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   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.
PE   2: Evidence at transcript level;
KW   Blood coagulation cascade activating toxin; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028377"
FT   CHAIN           25..258
FT                   /note="Thrombin-like enzyme ancrod-2"
FT                   /id="PRO_0000028378"
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:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        112
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
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        102..256
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   258 AA;  29145 MW;  9181C7D1F2D689F4 CRC64;
     MVLIRVLANL VILQLSYAQK SSELVIGGDE CNINEHRFLV ALYDSTTRNF LCGGVLIHPE
     WVITAKHCNK KSMVLYLGKH KQSVKFDDEQ ERFPKEKHFI RCNKPRTRWG EDIMLIRLNK
     PVNNSEHIAP LSLPSNPPIV GSVCRVMGWG SINKYIDVLP DEPRCANINL YNYTVCRGVF
     PRIPKKSKIL CAGDLQGRLD SCHCDSGGPL ICSEEFHGIV YRGPNPCAQP DKPALYTNIF
     DHLHWILSIM AGNATCYP