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PA22_BOTHY
ID   PA22_BOTHY              Reviewed;         123 AA.
AC   P0DUN1;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Basic myotoxic phospholipase A2 PhTX-II {ECO:0000303|PubMed:25365526};
DE            Short=svPLA2;
DE            EC=3.1.1.4 {ECO:0000269|PubMed:25365526};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Bothrocophias hyoprora (Amazonian hognose viper) (Porthidium hyoprora).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrocophias.
OX   NCBI_TaxID=230469;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, ACTIVITY REGULATION, COFACTOR,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=25365526; DOI=10.3390/toxins6113077;
RA   Huancahuire-Vega S., Ponce-Soto L.A., Marangoni S.;
RT   "PhTX-II a basic myotoxic phospholipase A(2) from Porthidium hyoprora snake
RT   venom, pharmacological characterization and amino acid sequence by mass
RT   spectrometry.";
RL   Toxins 6:3077-3097(2014).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces myotoxicity
CC       and local edema in mice (PubMed:25365526). In addition, it causes
CC       neuromuscular blockade in avian neuromuscular preparations with a
CC       significant direct action on skeletal muscle function
CC       (PubMed:25365526). Myotoxic action is exerted by both enzymatic and
CC       non-enzymatic mechanisms (PubMed:25365526). PLA2 catalyzes the calcium-
CC       dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
CC       (PubMed:25365526). {ECO:0000269|PubMed:25365526}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000269|PubMed:25365526};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:25365526};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: P-bromophenacyl bromide (BPB) completely inhibits
CC       the catalytic and edematogenic activities (PubMed:25365526). Enzymatic
CC       activity is also diminished by EDTA, heparin and crotapotins F2 and F3
CC       from C.d.collilineatus (PubMed:25365526). Inhibited by divalent cations
CC       different from calcium ions (cadmium, magnesium, manganese, zinc),
CC       since they act as competitive antagonists of this cofactor
CC       (PubMed:25365526). {ECO:0000269|PubMed:25365526}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=9.65 nmol/min/mg enzyme {ECO:0000269|PubMed:25365526};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:25365526};
CC       Temperature dependence:
CC         Optimum temperature is 40-45 degrees Celsius.
CC         {ECO:0000269|PubMed:25365526};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25365526}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25365526}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25365526}.
CC   -!- MASS SPECTROMETRY: Mass=14149.08; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:25365526};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DUN1; -.
DR   SMR; P0DUN1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR033112; PLipase_A2_Asp_AS.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   PANTHER; PTHR11716; PTHR11716; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Metal-binding; Myotoxin; Secreted; Toxin.
FT   CHAIN           1..123
FT                   /note="Basic myotoxic phospholipase A2 PhTX-II"
FT                   /evidence="ECO:0000269|PubMed:25365526"
FT                   /id="PRO_0000452840"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000250|UniProtKB:P06859"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250|UniProtKB:P06859"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        26..116
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        28..45
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        44..95
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        50..123
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        51..88
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        58..81
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
SQ   SEQUENCE   123 AA;  14159 MW;  9338BFB893C29D22 CRC64;
     NLLQFNKMIL KETGKNAIPF YAFYGCYCGW GGRGKPKDKT DDRCCFVHDC CYGKLTGCPK
     WDIYPYSLKS GYITCGKGTW CEEQICECDR AAAICFRENL DTYNKYGYMF YPDSRCKGPS
     EQC
 
 
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