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PA2AB_TRIPE
ID   PA2AB_TRIPE             Reviewed;         122 AA.
AC   Q2YHJ5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Acidic phospholipase A2 Tpu-E6b;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Trimeresurus puniceus (Flat-nosed pitviper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=197218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-23, FUNCTION, SUBUNIT,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15955061; DOI=10.1111/j.1742-4658.2005.04715.x;
RA   Wang Y.-M., Peng H.-F., Tsai I.-H.;
RT   "Unusual venom phospholipases A2 of two primitive tree vipers Trimeresurus
RT   puniceus and Trimeresurus borneensis.";
RL   FEBS J. 272:3015-3025(2005).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that weakly inhibits ADP-
CC       induced platelet aggregation when tested on platelet rich plasma from
CC       human and rabbit blood (15-25% of inhibition at 5-10 ug of enzyme).
CC       Exhibits moderate hydrolytic activities toward L-dipalmitoyl
CC       phosphatidylcholine. PLA2 catalyzes the calcium-dependent hydrolysis of
CC       the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:15955061}.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC         ProRule:PRU10036};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15955061}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=13978.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15955061};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY355175; AAR14169.1; -; mRNA.
DR   AlphaFoldDB; Q2YHJ5; -.
DR   SMR; Q2YHJ5; -.
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:UniProtKB-KW.
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.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..122
FT                   /note="Acidic phospholipase A2 Tpu-E6b"
FT                   /id="PRO_0000419059"
FT   ACT_SITE        47
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:O42191"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   BINDING         48
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   DISULFID        26..115
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   DISULFID        43..95
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   DISULFID        49..122
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   DISULFID        50..88
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   DISULFID        57..81
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:O42191"
SQ   SEQUENCE   122 AA;  13943 MW;  1A2178464F28FC15 CRC64;
     SLMQFETMIM KVAGRSGVWW YGSYGCYCGK GGQGQPQDAS DRCCFVHDCC YGKVNGCDPK
     DDFYTYSSEN GDVVCEEDNP CTKEICECDK AAAICFRDNM DTYQNKYWFY PTKYCKEESE
     PC
 
 
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