ID VMPA1_TITSE Reviewed; 394 AA.
AC P86392; A0A076L876; V9Z8X8;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 4.
DT 28-JUN-2023, entry version 37.
DE RecName: Full=Venom metalloproteinase antarease TserMP_A;
DE Short=VMPA;
DE EC=3.4.24.-;
DE AltName: Full=Metalloserrulase 1 {ECO:0000303|PubMed:25091350};
DE Short=TsMS 1 {ECO:0000303|PubMed:25091350};
DE Flags: Precursor;
OS Tityus serrulatus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=6887;
RN [1] {ECO:0000312|EMBL:AIJ02109.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=25091350; DOI=10.1016/j.toxicon.2014.07.014;
RA Carmo A.O., Oliveira-Mendes B.B., Horta C.C., Magalhaes B.F., Dantas A.E.,
RA Chaves L.M., Chavez-Olortegui C., Kalapothakis E.;
RT "Molecular and functional characterization of metalloserrulases, new
RT metalloproteases from the Tityus serrulatus venom gland.";
RL Toxicon 90:45-55(2014).
RN [2] {ECO:0000312|EMBL:AHE40588.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 159-393.
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).
RN [3]
RP PROTEIN SEQUENCE OF 158-194 AND 203-393, FUNCTION, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=20026600; DOI=10.1074/jbc.m109.028365;
RA Fletcher P.L. Jr., Fletcher M.D., Weninger K., Anderson T.E., Martin B.M.;
RT "Vesicle-associated membrane protein (VAMP) cleavage by a new
RT metalloprotease from the Brazilian scorpion Tityus serrulatus.";
RL J. Biol. Chem. 285:7405-7416(2010).
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. {ECO:0000269|PubMed:20026600}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q3ZD74};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q3ZD74};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:20026600}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20026600}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20026600}.
CC -!- PTM: Contains 4 disulfide bonds. {ECO:0000305|PubMed:25091350}.
CC -!- MASS SPECTROMETRY: Mass=25500; Mass_error=100; Method=SELDI;
CC Evidence={ECO:0000269|PubMed:20026600};
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC {ECO:0000305}.
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DR EMBL; KM115016; AIJ02109.2; -; mRNA.
DR EMBL; KC693035; AHE40588.1; -; mRNA.
DR AlphaFoldDB; P86392; -.
DR SMR; P86392; -.
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; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF243; SOL NARAE, ISOFORM C; 1.
DR Pfam; PF13688; Reprolysin_5; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..157
FT /evidence="ECO:0000305|PubMed:20026600,
FT ECO:0000305|PubMed:25091350"
FT /id="PRO_0000455749"
FT CHAIN 158..394
FT /note="Venom metalloproteinase antarease TserMP_A"
FT /id="PRO_0000391698"
FT DOMAIN 162..391
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 DISULFID 295..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CONFLICT 340
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="K -> KV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 42975 MW; 6E428AA50F6CD603 CRC64;
MISYLASIFL LATVSAVPSG RVEVVFPSVE TSRSGVKTVK FTALDQDVEL KLRSAGEILG
KRFAIQDVDV ESLRRKIYRD SVNGAALLID EDGPLTIEGI VNSKLRIQPF ESGRITKDGI
IAHQIVEVID DKKSYDRVAV IPENVKRNAE NVSRMARDDD CIVVEYYIVT DSAFTKRFKS
NSALTNYVTV MFTGVQNLMD TLELGIGVRL LGVTTFTEKT EPSFIKDNLI PGPPAAFDPD
VLISAMSKYY CNHQTGLAKD TDLIFLITAR GMGDPREDGT VDINTAGIAN SAGVCKPCFK
SGIATDDSDY NERVDTLAHE SVHLLGSPHD GEGPNLVSLE GSPGAANCPA KAGYIMGNRN
DKNKYKFSPC TKKCVEYLLS KPTASCIFQQ CTDF
//
