VSPP_DEIAC
ID VSPP_DEIAC Reviewed; 258 AA.
AC Q9I8X1;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Snake venom serine protease Dav-PA;
DE Short=SVSP;
DE AltName: Full=AaV-SP-I;
DE AltName: Full=AaV-SP-II;
DE EC=3.4.21.-;
DE Flags: Precursor;
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].
RC TISSUE=Venom gland;
RX PubMed=11171091; DOI=10.1042/0264-6021:3540161;
RA Wang Y.-M., Wang S.-R., Tsai I.-H.;
RT "Serine protease isoforms of Deinagkistrodon acutus venom: cloning,
RT sequencing and phylogenetic analysis.";
RL Biochem. J. 354:161-168(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT AAV-SP-II ASP-70, X-RAY CRYSTALLOGRAPHY
RP (2.0 ANGSTROMS) OF 25-258, FUNCTION, ACTIVE SITE, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-44.
RX PubMed=15632114; DOI=10.1074/jbc.m412900200;
RA Zhu Z., Liang Z., Zhang T., Zhu Z., Xu W., Teng M., Niu L.;
RT "Crystal structures and amidolytic activities of two glycosylated snake
RT venom serine proteinases.";
RL J. Biol. Chem. 280:10524-10529(2005).
RN [3]
RP PROTEIN SEQUENCE OF 25-64, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CRYSTALLIZATION.
RC TISSUE=Venom;
RX PubMed=12595722; DOI=10.1107/s0907444902023375;
RA Zhu Z., Gong P., Teng M., Niu L.;
RT "Purification, N-terminal sequencing, partial characterization,
RT crystallization and preliminary crystallographic analysis of two
RT glycosylated serine proteinases from Agkistrodon acutus venom.";
RL Acta Crystallogr. D 59:547-550(2003).
CC -!- FUNCTION: Snake venom serine protease that has fibrinogenolytic
CC activities. Also possess esterolysis and amidolytic activities.
CC Selectively cleaves Arg-|-Xaa bonds. {ECO:0000269|PubMed:12595722,
CC ECO:0000269|PubMed:15632114}.
CC -!- ACTIVITY REGULATION: Inhibited by NPGB, leupeptin, aprotinin and PMSF,
CC but not by EDTA, SBTI, heparin and hirudin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.152 uM for TAME {ECO:0000269|PubMed:12595722,
CC ECO:0000269|PubMed:15632114};
CC KM=265 uM for D-Phe-L-Pip-Arg-p-NA (S-2238)
CC {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114};
CC KM=113 uM for D-Pro-Phe-Arg-p-NA (S-2302)
CC {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114};
CC KM=28 uM for N-p-Tosyl-Gly-Pro-Arg-p-NA {ECO:0000269|PubMed:12595722,
CC ECO:0000269|PubMed:15632114};
CC KM=202 uM for N-p-Tosyl-Gly-Pro-Lys-p-NA
CC {ECO:0000269|PubMed:12595722, ECO:0000269|PubMed:15632114};
CC Note=AaV-SP-II.;
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}.
CC -!- CAUTION: AaV-SP-I is sequenced from 25-48 and its carbohydrate contents
CC is 9%, whereas AaV-SP-II is sequenced from 25-64 and its carbohydrate
CC contents is 4%. {ECO:0000305}.
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DR EMBL; AF159058; AAF76378.1; -; mRNA.
DR PDB; 1OP0; X-ray; 2.00 A; A=25-258.
DR PDB; 1OP2; X-ray; 2.10 A; A=25-258.
DR PDBsum; 1OP0; -.
DR PDBsum; 1OP2; -.
DR AlphaFoldDB; Q9I8X1; -.
DR SMR; Q9I8X1; -.
DR MEROPS; S01.023; -.
DR iPTMnet; Q9I8X1; -.
DR BRENDA; 3.4.21.74; 191.
DR EvolutionaryTrace; Q9I8X1; -.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Fibrinogenolytic toxin; Glycoprotein; Hemostasis impairing toxin;
KW Hydrolase; Protease; Secreted; Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..24
FT /evidence="ECO:0000250"
FT /id="PRO_0000028363"
FT CHAIN 25..258
FT /note="Snake venom serine protease Dav-PA"
FT /id="PRO_0000028364"
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:0000269|PubMed:15632114"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15632114"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15632114"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15632114"
FT DISULFID 31..163
FT /evidence="ECO:0000269|PubMed:15632114,
FT ECO:0007744|PDB:1OP0, ECO:0007744|PDB:1OP2"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15632114, ECO:0007744|PDB:1OP0,
FT ECO:0007744|PDB:1OP2"
FT DISULFID 98..256
FT /evidence="ECO:0000269|PubMed:15632114,
FT ECO:0007744|PDB:1OP0, ECO:0007744|PDB:1OP2"
FT DISULFID 142..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15632114, ECO:0007744|PDB:1OP0,
FT ECO:0007744|PDB:1OP2"
FT DISULFID 174..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15632114, ECO:0007744|PDB:1OP0,
FT ECO:0007744|PDB:1OP2"
FT DISULFID 200..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15632114, ECO:0007744|PDB:1OP0,
FT ECO:0007744|PDB:1OP2"
FT VARIANT 70
FT /note="D -> N (in AaV-SP-II)"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1OP0"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1OP0"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:1OP0"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1OP0"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1OP0"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:1OP0"
SQ SEQUENCE 258 AA; 28033 MW; E8E1369C8919CCCB CRC64;
MVLIRVLANL LILQLSYAQK SSELVIGGNE CDINEHRFLV AFFNTTGFFC GGTLINPEWV
VTAAHCDSTD FQMQLGVHSK KVLNEDEQTR NPKEKFICPN KNNNEVLDKD IMLIKLDKPI
SNSKHIAPLS LPSSPPSVGS VCRIMGWGSI TPVKETFPDV PYCANINLLD HAVCQAGYPE
LLAEYRTLCA GIVQGGKDTC GGDSGGPLIC NGQFQGIVSY GAHPCGQGPK PGIYTNVFDY
TDWIQRNIAG NTDATCPP
