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VMPA_LOXIN
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   03-AUG-2022, entry version 55.
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; -; 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   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
 
 
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