ID   VM2P3_PROMU             Reviewed;         411 AA.
AC   E9NW28;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Zinc metalloproteinase/disintegrin;
DE   Contains:
DE     RecName: Full=Snake venom metalloproteinase PMMP-3;
DE              Short=SVMP;
DE              EC=3.4.24.-;
DE   Flags: Precursor; Fragment;
OS   Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Sun Q.Y., Bao J.;
RT   "Purification, characterization and cloning of metalloproteinases from
RT   Trimeresurus mucrosquamatus Venom.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Snake venom metalloproteinase that impairs hemostasis in the
CC       envenomed animal. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {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 venom metalloproteinase (M12B) family. P-II
CC       subfamily. {ECO:0000305}.
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DR   EMBL; HQ731071; ADV71357.1; -; mRNA.
DR   AlphaFoldDB; E9NW28; -.
DR   SMR; E9NW28; -.
DR   MEROPS; M12.155; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..190
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000417633"
FT   CHAIN           191..395
FT                   /note="Snake venom metalloproteinase PMMP-3"
FT                   /id="PRO_0000417634"
FT   PROPEP          396..>411
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000423371"
FT   DOMAIN          197..395
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        352..374
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        354..357
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   NON_TER         411
SQ   SEQUENCE   411 AA;  46459 MW;  A52E1D5F234FFD8A CRC64;
     MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVS ALPKGAVQPK YEDTMQYELK
     ENGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIH NDADSTASIS
     ACDGLKGYFK LQGQTYLIEP LKLPDSEAHA VFKYENIEKE DEAPKMCGVT QNWESDESIK
     KASQLYLTPE QQRFPQRYVK LAIVVDYRMY IKYNRDSNKI TVRVHEMVNH VNEMYKPLNV
     AITLSLLRIW STRDLITVQS DSKVTLGSFG DWRKTVLLKQ QSHDCAHLLT DITFTKNVIG
     VAYKKGMCDP KLSVGLVQDY SSNVFVVAAI MTHELGHNLG MEHDEDENGK KCKCDTCIMS
     PAISDPPAQL FSDCSKNDYH TFLTNSKPQC ILNAPLRTDT VSTPVSGNEP L