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PA2A1_PSETE
ID   PA2A1_PSETE             Reviewed;         154 AA.
AC   Q9W7J4;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Acidic phospholipase A2 1;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=Pt-PLA1;
DE   Flags: Precursor;
OS   Pseudonaja textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX   NCBI_TaxID=8673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-39, AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=14678780; DOI=10.1016/j.abb.2003.09.045;
RA   Armugam A., Gong N.L., Li X.J., Siew P.Y., Chai S.C., Nair R.,
RA   Jeyaseelan K.;
RT   "Group IB phospholipase A2 from Pseudonaja textilis.";
RL   Arch. Biochem. Biophys. 421:10-20(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16284125; DOI=10.1074/mcp.m500270-mcp200;
RA   Birrell G.W., Earl S., Masci P.P., de Jersey J., Wallis T.P., Gorman J.J.,
RA   Lavin M.F.;
RT   "Molecular diversity in venom from the Australian Brown snake, Pseudonaja
RT   textilis.";
RL   Mol. Cell. Proteomics 5:379-389(2006).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows moderate
CC       enzymatic activity and exhibits procoagulant activity. PLA2 catalyzes
CC       the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC       phosphoglycerides. {ECO:0000269|PubMed:14678780}.
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.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF082983; AAD40975.1; -; mRNA.
DR   EMBL; AY027494; AAK15775.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9W7J4; -.
DR   SMR; Q9W7J4; -.
DR   PRIDE; Q9W7J4; -.
DR   Proteomes; UP000472273; Unplaced.
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   Blood coagulation cascade activating toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW   Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..27
FT                   /evidence="ECO:0000269|PubMed:14678780"
FT                   /id="PRO_0000022948"
FT   CHAIN           28..154
FT                   /note="Acidic phospholipase A2 1"
FT                   /id="PRO_0000022949"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..153
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        111..123
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   154 AA;  16844 MW;  1A50E3D04492E2C5 CRC64;
     MHPAHLLVLL GVCVSLLGAA RIPPLPLSLD DFSNLITCAN RGSRSWLDYA HYGCFCGSGG
     SGTPVDDLDR CCQVHDNCFG DAEKLPACNY LFSGPYWNPY SYKCNEGEIT CTDDNDECAA
     FICNCDRTAA ICFAGATYND ENFMVTIKKK NICQ
 
 
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