ID   VSPCA_AGKPL             Reviewed;         255 AA.
AC   E5L0E6;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Protein C activator {ECO:0000303|PubMed:21640745};
DE            Short=APL-C {ECO:0000303|PubMed:21640745};
DE            EC=3.4.21.-;
DE   AltName: Full=Snake venom serine protease {ECO:0000305};
DE            Short=SVSP {ECO:0000305};
DE   Flags: Precursor;
OS   Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias
OS   leucostoma).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=459671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21640745; DOI=10.1016/j.toxicon.2011.05.014;
RA   Sukkapan P., Jia Y., Nuchprayoon I., Perez J.C.;
RT   "Phylogenetic analysis of serine proteases from Russell's viper (Daboia
RT   russelli siamensis) and Agkistrodon piscivorus leucostoma venom.";
RL   Toxicon 58:168-178(2011).
CC   -!- FUNCTION: Snake venom serine protease that selectively cleaves the
CC       heavy chain of protein C (PROC). This activation is thrombomodulin-
CC       independent. {ECO:0000250|UniProtKB:P09872}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09872}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
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; HQ270467; ADP88562.1; -; mRNA.
DR   AlphaFoldDB; E5L0E6; -.
DR   SMR; E5L0E6; -.
DR   MEROPS; S01.466; -.
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; 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; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation cascade inhibiting toxin; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250|UniProtKB:Q8UVX1"
FT                   /id="PRO_0000432332"
FT   CHAIN           25..255
FT                   /note="Protein C activator"
FT                   /id="PRO_0000432333"
FT   DOMAIN          25..246
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        64
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   DISULFID        31..162
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   DISULFID        49..65
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   DISULFID        97..253
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   DISULFID        141..207
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   DISULFID        173..186
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
FT   DISULFID        197..222
FT                   /evidence="ECO:0000250|UniProtKB:P09872"
SQ   SEQUENCE   255 AA;  27811 MW;  BC6BCE5CC5DE7E74 CRC64;
     MVLIRVLANL LILHLSYAQK SSELVIGGDE CNINEHRFLA LVYANGSLCG GTLINQEWVL
     TARHCDRGNM RIYLGMHNLK VLNKDALRRF PKEKYFCLNI RNDTIWDKDI MLIRLNRPVR
     NSAHIAPLSL PSNPPSVGSV CRVMGWGTIT SPNATLPDVP HCANINILDY AVCQAAYRGL
     AATTLCSGIL EGGKDTCKGD SGGPLICNGQ FQGILSVGGN PCAQPRKPGV YTKVFDYTDW
     IQSIISGNTD AACPP