ID VSP12_BOTJA Reviewed; 255 AA.
AC Q5W960;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Snake venom serine protease HS112;
DE Short=SVSP;
DE EC=3.4.21.-;
DE Flags: Precursor;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=15876446; DOI=10.1016/j.toxicon.2005.03.011;
RA Saguchi K., Hagiwara-Saguchi Y., Murayama N., Ohi H., Fujita Y.,
RA Camargo A.C.M., Serrano S.M.T., Higuchi S.;
RT "Molecular cloning of serine proteinases from Bothrops jararaca venom
RT gland.";
RL Toxicon 46:72-83(2005).
CC -!- FUNCTION: Snake venom serine protease that may act in the hemostasis
CC system of the prey. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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}.
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DR EMBL; AB178321; BAD66927.1; -; mRNA.
DR AlphaFoldDB; Q5W960; -.
DR SMR; Q5W960; -.
DR MEROPS; S01.179; -.
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; Trypsin-like serine proteases; 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 PANTHER; PTHR24264:SF15; RIKEN CDNA 2210010C04 GENE; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; Hemostasis impairing toxin; Hydrolase;
KW Protease; 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_0000294988"
FT CHAIN 25..255
FT /note="Snake venom serine protease HS112"
FT /id="PRO_5000051171"
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"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 31..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 49..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 97..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 141..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 173..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 197..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 255 AA; 27988 MW; E0AF873428C8C33E CRC64;
MVLIRVIANL LILQLSYAQK SSELVIGGDE CDINEHRFLA FLYAGGYYCG GTLINQEWVL
SAAHCDKRII RIYLGMHTRS VPNDDEEIRY PKEKFICPNK KKNVITHKDI MLIRLNRPVK
NSEHIAPLSL PSNPPSVGSV CRIMGWGSIT TPDETSPNVP HCANINLFNN TVCREAYNGL
PAKTLCAGVL QGGIDTCGGD SGGPLICNGQ FQGILSWGGI PCAQPRKPAF YTKVFDYLPW
IQSIIAGNKT ATCPP
//
