ID VMPA_LOXIN Reviewed; 264 AA.
AC A0FKN6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Astacin-like metalloprotease toxin 1;
DE EC=3.4.24.-;
DE AltName: Full=Loxosceles astacin-like protease 1;
DE Short=LALP;
DE Short=LALP1;
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], FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Venom gland;
RX PubMed=17535156; DOI=10.1042/bj20070363;
RA da Silveira R.B., Wille A.C.M., Chaim O.M., Appel M.H., Silva D.T.,
RA Franco C.R.C., Toma L., Mangili O.C., Gremski W., Dietrich C.P.,
RA Nader H.B., Veiga S.S.;
RT "Identification, cloning, expression and functional characterization of an
RT astacin-like metalloprotease toxin from Loxosceles intermedia (brown
RT spider) venom.";
RL Biochem. J. 406:355-363(2007).
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. {ECO:0000269|PubMed:17535156}.
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.
CC {ECO:0000269|PubMed:17535156}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17535156}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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DR EMBL; EF028089; ABK20019.1; -; mRNA.
DR AlphaFoldDB; A0FKN6; -.
DR SMR; A0FKN6; -.
DR MEROPS; M12.333; -.
DR ArachnoServer; AS000017; Loxosceles astacin-like metalloprotease.
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; Collagenase (Catalytic Domain); 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 PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Toxin; Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..51
FT /evidence="ECO:0000250"
FT /id="PRO_5000148896"
FT CHAIN 52..264
FT /note="Astacin-like metalloprotease toxin 1"
FT /id="PRO_5000148897"
FT DOMAIN 52..249
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT ACT_SITE 144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 114..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 264 AA; 30384 MW; A3DA23213725E29D CRC64;
MIKYIGVFAF LVGGFCHDFE TVISNQDPIV DGMRLVEGDM LFDDGPLFTE RNAVKYDQQL
WPNGEIVYEI SPGLRQYEQI IREAMRTYED NTCIKFRRRT NEADYVNIHV GDRCYSRVGK
SFRGGPQPLS LGRGCTDFGT ILHELGHSVG FDHEHSRADR DEFLIIHKEN IKNGSEHNFD
KLWENNTRTI GPFDYDSIML YGAYAFSKDT RKFKTMEPVE PGLPMKSVIQ KGKLSYYDIV
KVNKLYKCPP VNPYPGGIRP YVNV
//
