ID   VSP4_LACMR              Reviewed;          53 AA.
AC   C0HLA3;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Snake venom serine protease LmrSP-4 {ECO:0000303|PubMed:31131000};
DE            Short=SVSP {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000269|PubMed:31131000};
DE   Flags: Fragment;
OS   Lachesis muta rhombeata (Bushmaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX   NCBI_TaxID=60219;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=31131000; DOI=10.1590/1678-9199-jvatitd-1470-18;
RA   Wiezel G.A., Bordon K.C., Silva R.R., Gomes M.S., Cabral H.,
RA   Rodrigues V.M., Ueberheide B., Arantes E.C.;
RT   "Subproteome of Lachesis muta rhombeata venom and preliminary studies on
RT   LmrSP-4, a novel snake venom serine proteinase.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 25:E147018-E147018(2019).
CC   -!- FUNCTION: Snake venom serine protease that has fibrinogenolytic
CC       activity. Hydrolyzes the alpha-chain of fibrinogen (FGA), without
CC       affecting the beta- and the gamma-chains. Also displays hydrolytic
CC       activity towards S-2302 (plasma kalikrein substrate) and S-2251
CC       (substrate for plasmin), but has no hydrolytic activity with S-2238
CC       (thrombin substrate) or S-2222 (factor Xa).
CC       {ECO:0000269|PubMed:31131000}.
CC   -!- ACTIVITY REGULATION: Inhibited by the small molecule serine protease
CC       inhibitors phenylmethylsulfonyl fluoride (PMSF) and benzamidine.
CC       {ECO:0000269|PubMed:31131000}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 7-8 (at 40 degrees Celsius).
CC         {ECO:0000269|PubMed:31131000};
CC       Temperature dependence:
CC         Optimum temperature is between 40 and 55 degrees Celsius (at pH 7).
CC         Activity decreases at 60 degrees Celsius.
CC         {ECO:0000269|PubMed:31131000};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q27J47}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31131000}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31131000}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:31131000}.
CC   -!- MASS SPECTROMETRY: Mass=28190; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:31131000};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HLA3; -.
DR   SMR; C0HLA3; -.
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   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00089; Trypsin; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Glycoprotein; Hemostasis impairing toxin; Hydrolase; Protease; Secreted;
KW   Serine protease; Toxin.
FT   CHAIN           1..>53
FT                   /note="Snake venom serine protease LmrSP-4"
FT                   /evidence="ECO:0000269|PubMed:31131000"
FT                   /id="PRO_0000447684"
FT   ACT_SITE        41
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10078"
FT   DISULFID        26..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         53
FT                   /evidence="ECO:0000305|PubMed:31131000"
SQ   SEQUENCE   53 AA;  5845 MW;  9C82E53ACF832046 CRC64;
     VFGGDECNIN EHRSLVVLFD SDGFLCAGTL INKEWVLTAA HCDSENFQMQ LGV