ID   VSPA_DEIAC              Reviewed;         234 AA.
AC   Q9YGS1;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Thrombin-like enzyme acutin;
DE            Short=SVTLE acutin;
DE            EC=3.4.21.-;
DE   AltName: Full=Fibrinogen-clotting enzyme;
DE   AltName: Full=Snake venom serine protease;
DE            Short=SVSP;
DE   AltName: Full=Thrombin-like defibrase 1;
DE            Short=DFA1;
DE   Flags: Precursor; Fragment;
OS   Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX   NCBI_TaxID=36307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-16, AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=10049722; DOI=10.1006/bbrc.1999.0203;
RA   Pan H., Du X., Yang G., Zhou Y., Wu X.;
RT   "cDNA cloning and expression of acutin, a thrombin-like enzyme from
RT   Agkistrodon acutus.";
RL   Biochem. Biophys. Res. Commun. 255:412-415(1999).
CC   -!- FUNCTION: Thrombin-like snake venom serine protease. Has arginyl
CC       esterase and fibrinogen clotting activities.
CC       {ECO:0000269|PubMed:10049722}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not have phospholipase, fibrinolytic and
CC       hemorrhagic activities. {ECO:0000305|PubMed:10049722}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF089847; AAD19350.1; -; mRNA.
DR   PIR; JG0169; JG0169.
DR   AlphaFoldDB; Q9YGS1; -.
DR   SMR; Q9YGS1; -.
DR   MEROPS; S01.023; -.
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   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW   Protease; Secreted; Serine protease; Toxin; Zymogen.
FT   PROPEP          <1..1
FT                   /id="PRO_0000416383"
FT   CHAIN           2..234
FT                   /note="Thrombin-like enzyme acutin"
FT                   /id="PRO_0000416384"
FT   DOMAIN          2..225
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        42
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        87
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        180
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        8..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        27..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        75..232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        119..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        151..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        176..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        6
FT                   /note="D -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   234 AA;  25408 MW;  3F1C3653E00BCA39 CRC64;
     MVIGGDECDI NEHRFLVAFF NTTGFFCGGT LINPEWVVTA AHCDSTNFQM QLGVHSKKVL
     NEDEQTRNPK EKFICPNKNN NEVLDKDIML IKLDKPISNS KHIAPLSLPS SPPSVGSVCR
     IMGWGSITPV KETFPDVPYC ANINLLDHAV CQTGYPSCWR NTTLCAGFLE GGKDTCGGDS
     GGPLICNGQF QGIVSYGAHS CGQGPKPGIY TNVFDYTDWI QRNIAGNTDA TCPP