ID   VM3AL_BORPO             Reviewed;          31 AA.
AC   P0DJH4;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Zinc metalloproteinase alsophinase;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragment;
OS   Borikenophis portoricensis (Puerto Rican racer) (Alsophis portoricensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Borikenophis.
OX   NCBI_TaxID=1260276;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, MASS SPECTROMETRY, AND
RP   PYROGLUTAMATE FORMATION AT GLN-1.
RC   TISSUE=Venom;
RX   PubMed=22349739; DOI=10.1016/j.biochi.2012.02.006;
RA   Weldon C.L., Mackessy S.P.;
RT   "Alsophinase, a new P-III metalloproteinase with alpha-fibrinogenolytic and
RT   hemorrhagic activity from the venom of the rear-fanged puerto rican racer
RT   alsophis portoricensis (Serpentes: Dipsadidae).";
RL   Biochimie 94:1189-1198(2012).
CC   -!- FUNCTION: Snake venom zinc metalloprotease that has potent hemorrhagic
CC       activity, fibrinogenolytic activity on the alpha-subunit of human
CC       fibrinogen (FGA) in vitro and provokes necrosis in skin, muscle and
CC       lung tissues. May contribute to local edema and ecchymosis induced by
CC       venom. Hydrolyzes model substrate (beta-chain of insulin) at Ala(14)-
CC       Leu(15). {ECO:0000269|PubMed:22349739}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline.
CC       {ECO:0000269|PubMed:22349739}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 9 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=56003; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22349739};
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIa sub-subfamily. {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; Cell adhesion impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Fibrinogenolytic toxin; Hemorrhagic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Myotoxin; Protease; Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc.
FT   CHAIN           1..>31
FT                   /note="Zinc metalloproteinase alsophinase"
FT                   /id="PRO_0000417325"
FT   DOMAIN          9..>31
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:22349739"
FT   NON_TER         31
SQ   SEQUENCE   31 AA;  3732 MW;  82848C054693586E CRC64;
     QDTYLNAKKY IEFYLVVDNG MFXKYSXXFT V