VSPPA_AGKPL
ID VSPPA_AGKPL Reviewed; 258 AA.
AC E5L0E5;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Venom plasminogen activator {ECO:0000303|PubMed:21640745};
DE Short=APL-PA {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 activates plasminogen. Shows
CC a preferential cleavage at Arg-|-Xaa instead of Lys-|-Xaa bonds.
CC {ECO:0000250|UniProtKB:Q9YGJ8}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9YGJ8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9YGJ8}.
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; HQ270466; ADP88561.1; -; mRNA.
DR AlphaFoldDB; E5L0E5; -.
DR SMR; E5L0E5; -.
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: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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Plasminogen activation; Protease;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000432334"
FT CHAIN 25..258
FT /note="Venom plasminogen activator"
FT /id="PRO_0000432335"
FT DOMAIN 25..249
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 204
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..163
FT /evidence="ECO:0000250|UniProtKB:Q91516"
FT DISULFID 50..66
FT /evidence="ECO:0000250|UniProtKB:Q91516"
FT DISULFID 98..256
FT /evidence="ECO:0000250|UniProtKB:Q91516"
FT DISULFID 142..210
FT /evidence="ECO:0000250|UniProtKB:Q91516"
FT DISULFID 174..189
FT /evidence="ECO:0000250|UniProtKB:Q91516"
FT DISULFID 200..225
FT /evidence="ECO:0000250|UniProtKB:Q91516"
SQ SEQUENCE 258 AA; 28078 MW; 6E0EF8393715BD96 CRC64;
MVLIRVLANL LILQLSYAQK SSELVVGGDE CNINEHRSLV VFFNSSGFLC GGTSINQEWV
LTAAHCDSKN FQMLFGVHSK KILNEDEQTR DPKEKFICPN RKKDDERDKD IMLIRLDSPV
SNSEHIAPLS LPSSPPSVGS VCRIMGWGTI SPTKVTYPDV PHCANINILD HAVCRAAYPT
LLAESSTVCA GTQQEGKDTC GGDSGGPLIC NGQIQGIVSW RAHPCGQGLK PGVYTKVFDY
TDWIQSIISG NTDVTCPP