ID   VMXP_PHIPA              Reviewed;          10 AA.
AC   P85103;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Snake venom metalloproteinase patagonfibrase;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Fragment;
OS   Philodryas patagoniensis (Ringless green snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Philodryas.
OX   NCBI_TaxID=120310;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom {ECO:0000269|Ref.1};
RA   Peichoto M.E., Batista I.F.C., Acosta O., Mitiko A., Tanaka-Azevedo A.M.,
RA   Santoro M.L.;
RT   "Partial amino acid sequence and some features of patagonfibrase, a
RT   hemorrhagic metalloprotease isolated from Philodryas patagoniensis snake
RT   venom.";
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2] {ECO:0000305}
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17306461; DOI=10.1016/j.bbagen.2006.12.014;
RA   Peichoto M.E., Teibler P., Mackessy S.P., Leiva L., Acosta O.,
RA   Goncalves L.R., Tanaka-Azevedo A.M., Santoro M.L.;
RT   "Purification and characterization of patagonfibrase, a metalloproteinase
RT   showing alpha-fibrinogenolytic and hemorrhagic activities, from Philodryas
RT   patagoniensis snake venom.";
RL   Biochim. Biophys. Acta 1770:810-819(2007).
CC   -!- FUNCTION: Snake venom zinc metalloprotease that hydrolyzes the alpha
CC       chain of fibrinogen (FGA) but not the beta or gamma chains. Has
CC       caseinolytic activity. Induces hemorrhage after intradermal injection
CC       into mice. Intramuscular injection into the gastrocnemius muscle of
CC       mice causes hemorrhage, edema, myonecrosis, increase in serum creatine
CC       kinase levels and multifocal lung hemorrhage. Inhibits collagen-induced
CC       platelet aggregation, but not thrombin- or ristocetin-induced platelet
CC       aggregation. {ECO:0000269|PubMed:17306461}.
CC   -!- ACTIVITY REGULATION: Inhibited by DTT, EDTA and L-cysteine, but not by
CC       the serine protease inhibitor PMSF. Activated by calcium, unaffected by
CC       magnesium, inhibited by zinc. {ECO:0000269|PubMed:17306461}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5 with azocasein as substrate. Incubation at a pH of
CC         below 6.0 or above 9.5 results in an abrupt decrease in activity.
CC         {ECO:0000269|PubMed:17306461};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius with azocasein as
CC         substrate. Incubation at 55 degrees Celsius for 90 minutes reduces
CC         activity to 20% of its maximum. {ECO:0000269|PubMed:17306461};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17306461}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17306461}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:17306461}.
CC   -!- MASS SPECTROMETRY: Mass=53224; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17306461};
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hemorrhagic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin.
FT   CHAIN           <1..>10
FT                   /note="Snake venom metalloproteinase patagonfibrase"
FT                   /id="PRO_0000284773"
FT   BINDING         10
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   10 AA;  1011 MW;  80560B6DC2C05AB1 CRC64;
     LSTDIVAPPV