ID   VMPA1_TITFA             Reviewed;         236 AA.
AC   V9Z7R6;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Venom metalloproteinase antarease-like TfasMP_A;
DE            Short=VMPA;
DE            EC=3.4.24.-;
OS   Tityus fasciolatus (Central Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=203543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24361608; DOI=10.1016/j.bbagen.2013.12.012;
RA   Ortiz E., Rendon-Anaya M., Rego S.C., Schwartz E.F., Possani L.D.;
RT   "Antarease-like Zn-metalloproteases are ubiquitous in the venom of
RT   different scorpion genera.";
RL   Biochim. Biophys. Acta 1840:1738-1746(2014).
CC   -!- FUNCTION: Acts as a metalloprotease. Penetrates intact tissue and
CC       specifically cleaves the vesicle-associated membrane protein 2 (VAMP2)
CC       (part of the SNARE complex) involved in pancreatic secretion, thus
CC       disrupting the normal vesicular traffic (By similarity). {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   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains several disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {ECO:0000305}.
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DR   EMBL; KC693044; AHE40597.1; -; mRNA.
DR   AlphaFoldDB; V9Z7R6; -.
DR   SMR; V9Z7R6; -.
DR   MEROPS; M12.191; -.
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   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Toxin; Zinc.
FT   CHAIN           1..236
FT                   /note="Venom metalloproteinase antarease-like TfasMP_A"
FT                   /id="PRO_0000429181"
FT   DOMAIN          4..232
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   236 AA;  25505 MW;  548CD973DB4B9D49 CRC64;
     DDCIVVEYYI VTDSAFTKRF KSNSALTKYV TVMFTGVQNL MDTLELGIGV RLLGVTAFNE
     ETEPSFIIDN LISGPPEAFD PDVLITAMSE YYCNHQIGLA KNTDLIFLIT ARGMGDPRED
     GTVDINTAGI ANSAGVYKPC LKAGVATDDS DYNERVDTLA HESVHLLGSP HDGEGPDQVS
     LEGSPGAANC PAKAGYIMGN RNDKNKYKFS PCTKKCVEYL LSKPAASCIF EQCSGF