ID   VMPA1_TITTR             Reviewed;         394 AA.
AC   V9ZAY0;
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 TtrivMP_A;
DE            Short=VMPA;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
OS   Tityus trivittatus (Argentinean scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=369776;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
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   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {ECO:0000305}.
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DR   EMBL; KC693043; AHE40596.1; -; mRNA.
DR   AlphaFoldDB; V9ZAY0; -.
DR   SMR; V9ZAY0; -.
DR   PRIDE; V9ZAY0; -.
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; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..158
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000429179"
FT   CHAIN           159..394
FT                   /note="Venom metalloproteinase antarease-like TtrivMP_A"
FT                   /id="PRO_0000429180"
FT   DOMAIN          162..390
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        295..386
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   394 AA;  43062 MW;  92D0417D306A10D0 CRC64;
     MISYLASIFL LATVSAVPSG RVEVVFPSVE TSRSGVKTVK FTALDQNVEL KLRSAGEILG
     KHFAIQDVDV ESLRRKIYRD SVNGAALLID EDGPLTIEGI VNSKLRIQPF ESGRIIKDGM
     IAHQIVEVID DKKSYDRVAV IHENVKRNAE NVSRMAEEND CIVVEYYIVT DSAFTKRFKS
     NSALTNYVTV MFTGVQNLMD TLELGIGVRL LGVTAFNEET EPSFIKDNLI PGPPEAFEPD
     VLITAMSQYY CNHQTGLAKD TDLIFLITAR GMGDPREDGT VDINTAGIAN SAGVCKPCLK
     AGIATDDSNY NERVDTLAHE SVHLLGSPHD GEGPDQVSVE GSPGAANCPA KAGYIMGNRK
     DPNKYKFSPC TKKCVEYLLS KPTAFCIFEQ CSDF