VMPA3_LOXIN
ID VMPA3_LOXIN Reviewed; 243 AA.
AC C9D7R3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Astacin-like metalloprotease toxin 3;
DE EC=3.4.24.-;
DE AltName: Full=Loxosceles astacin-like protease 3;
DE Short=LALP3;
DE Flags: Precursor;
OS Loxosceles intermedia (Brown spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX NCBI_TaxID=58218;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19879318; DOI=10.1016/j.biochi.2009.10.003;
RA Trevisan-Silva D., Gremski L.H., Chaim O.M., da Silveira R.B.,
RA Meissner G.O., Mangili O.C., Barbaro K.C., Gremski W., Veiga S.S.,
RA Senff-Ribeiro A.;
RT "Astacin-like metalloproteases are a gene family of toxins present in the
RT venom of different species of the brown spider (genus Loxosceles).";
RL Biochimie 92:21-32(2010).
CC -!- FUNCTION: Zinc metalloprotease. Provoques deadhesion of endothelial
CC cells from cell cultures, and also degradation of fibronectin,
CC fibrinogen and gelatin in vitro. Its role in the venom is not fully
CC understood but it might act as a spreading factor that facilitates
CC diffusion of other venom toxins. Alternatively, it might be involved in
CC the proteolytic processing of other venom toxins or it might play a
CC role in extra-oral digestion of prey (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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DR EMBL; GQ227491; ACV52011.1; -; mRNA.
DR AlphaFoldDB; C9D7R3; -.
DR SMR; C9D7R3; -.
DR PRIDE; C9D7R3; -.
DR BRENDA; 3.4.24.21; 8287.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Toxin; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..43
FT /evidence="ECO:0000255"
FT /id="PRO_5000522739"
FT CHAIN 44..243
FT /note="Astacin-like metalloprotease toxin 3"
FT /id="PRO_5000522740"
FT DOMAIN 44..238
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT ACT_SITE 135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 107..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 243 AA; 27942 MW; B0559998E6CB7910 CRC64;
MTTMSFFTVL SVAVCLCIEA GVEGSRLNGR DMLMQEESPL MERNALKYDS RLWPDGVVIY
EFTSLRFYRK LIKRVMQHIA DNTCITFKER TNEKGYVNIY NGKLFTCFAD MGYYPFKQRL
SLGLGCRSFG AILHELGHVL GLYHEQQRPD RDDYVIVYKD NIQTGALRDY EKRFENNTRV
IGPFDYDSIM IYGETDARKS GSVTMKVKKP GATLVNASLK HELTALDIKK INTLYNCPGK
DKF
