ID   VSPPA_GLOBR             Reviewed;         258 AA.
AC   Q9YGJ8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Venom plasminogen activator Haly-PA;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
OS   Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS   brevicaudus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=259325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC   TISSUE=Venom gland;
RX   PubMed=9839665; DOI=10.1016/s0041-0101(98)00090-7;
RA   Park D.S., Kim H.D., Chung K.H., Kim D.-S., Yun Y.D.;
RT   "Expression and characterization of a novel plasminogen activator from
RT   Agkistrodon halys venom.";
RL   Toxicon 36:1807-1819(1998).
CC   -!- FUNCTION: Snake venom serine protease that activates plasminogen.
CC       Displays indirect fibrino(geno)lytic activity through conversion of
CC       plasminogen to plasmin. Shows a preferential cleavage at Arg-|-Xaa
CC       instead of Lys-|-Xaa bonds. {ECO:0000269|PubMed:9839665}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9839665}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:9839665}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:9839665}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AF017737; AAD01624.1; ALT_SEQ; mRNA.
DR   AlphaFoldDB; Q9YGJ8; -.
DR   SMR; Q9YGJ8; -.
DR   MEROPS; S01.186; -.
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   Disulfide bond; Fibrinolytic toxin; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Plasminogen activation; Protease;
KW   Secreted; Serine protease; Signal; Toxin; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000296372"
FT   CHAIN           25..258
FT                   /note="Venom plasminogen activator Haly-PA"
FT                   /id="PRO_5000053382"
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:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        98..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        200..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   258 AA;  27813 MW;  B5B341E689D23AFF CRC64;
     MALIRVLANL LILQLSYAQK SSELVVGGDE CNINEHRSLV VLFNSSGLIC SGTLINQEWV
     LTAAHCDSKN FQMLFGVHSK KILNEDEQTR DPKEKFICPN KKKDDEKDKD IMLIRLDSPV
     SNSEHIAPLS LPSSSPTVDS VCRIMGWGTI KPADETYPDV PHCANINILD HTVCRAAYPV
     LLAGSSTLCA GTQQGGKDTC VGDSGGPLIC NGQIQGIVSW GAHPCGQGSK PGVYTKVFDH
     LDWIKSIIAG NTAVTCPP