VMPA2_TITPA
ID VMPA2_TITPA Reviewed; 235 AA.
AC V9ZAX6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Venom metalloproteinase antarease-like TpachMP_B;
DE Short=VMPA;
DE EC=3.4.24.-;
DE Flags: Fragment;
OS Tityus pachyurus (Colombian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=288781;
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 -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC {ECO:0000305}.
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DR EMBL; KC693038; AHE40591.1; -; mRNA.
DR AlphaFoldDB; V9ZAX6; -.
DR SMR; V9ZAX6; -.
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; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..>235
FT /note="Venom metalloproteinase antarease-like TpachMP_B"
FT /id="PRO_0000429178"
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"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 137..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT NON_TER 235
SQ SEQUENCE 235 AA; 25792 MW; 7BB0334332DDC20F CRC64;
DDCIVVEYYI VTDSRFTQRF DSDQAVTDYV TVMFTGVQNL IETLNLDIKV RLLGVTPYHK
ESEPSFIDDS LLPGHETYVD ARKIVRNMKF YFCNHNTGLA KSADIIILLI TRKMGVLDPG
DTDISEIAGA SSISSVCQRC NNVGACVDNS DHNERADTVA HESVHLLGSP HDGEGPNGLG
LPNSPGAANC PDSDGYIMGT RNEQNGKKFS ECTKQCVKYL LSLPRASCVY ENCSK