PA2B1_AGKPL
ID PA2B1_AGKPL Reviewed; 139 AA.
AC C0HKC3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Basic phospholipase A2 APL-D49 {ECO:0000303|PubMed:28633930};
DE Short=svPLA2 {ECO:0000250|UniProtKB:P51972};
DE EC=3.1.1.4 {ECO:0000269|PubMed:28633930};
DE AltName: Full=Apl-D49 {ECO:0000303|PubMed:28633930};
DE AltName: Full=AplP3 {ECO:0000303|PubMed:28633930};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P51972};
DE Flags: Precursor;
OS Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias
OS leucostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=459671 {ECO:0000303|PubMed:28633930};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland {ECO:0000303|PubMed:18502463};
RX PubMed=18502463; DOI=10.1016/j.toxicon.2008.03.028;
RA Jia Y., Cantu B.A., Sanchez E.E., Perez J.C.;
RT "Complementary DNA sequencing and identification of mRNAs from the venomous
RT gland of Agkistrodon piscivorus leucostoma.";
RL Toxicon 51:1457-1466(2008).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 17-28, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom {ECO:0000303|PubMed:28633930};
RX PubMed=28633930; DOI=10.1016/j.toxicon.2017.06.010;
RA Jia Y., Ermolinsky B., Garza A., Provenzano D.;
RT "Phospholipase A2 in the venom of three cottonmouth snakes.";
RL Toxicon 135:84-92(2017).
RN [3]
RP FUNCTION.
RX PubMed=29928892; DOI=10.1016/j.toxicon.2018.06.062;
RA Jia Y., Villarreal J.;
RT "Phospholipases A2 purified from cottonmouth snake venoms display no
RT antibacterial effect against four representative bacterial species.";
RL Toxicon 151:1-4(2018).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that does not show
CC antibacterial activity (PubMed:29928892). PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
CC (PubMed:28633930). {ECO:0000269|PubMed:28633930,
CC ECO:0000269|PubMed:29928892}.
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,
CC ECO:0000269|PubMed:28633930};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14418};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14418};
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000250|UniProtKB:P51972}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18502463}.
CC -!- PTM: Acylation causes dimerization. {ECO:0000250|UniProtKB:P51972}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; EV854875; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; C0HKC3; -.
DR SMR; C0HKC3; -.
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: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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lipoprotein; Metal-binding; Palmitate;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:28633930"
FT CHAIN 17..139
FT /note="Basic phospholipase A2 APL-D49"
FT /evidence="ECO:0000305|PubMed:28633930"
FT /id="PRO_0000442174"
FT ACT_SITE 63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10036"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT LIPID 23
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT LIPID 26
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT DISULFID 42..139
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT DISULFID 65..139
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:P51972"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:P51972"
SQ SEQUENCE 139 AA; 15787 MW; A7F52704FE6F26CF CRC64;
MRTLWIMAVL LLGVEGNLFQ FEKLIKKMTG KSGMLWYSAY GCYCGWGGQG RPKDATDRCC
FVHDCCYGKV TGCNPKMDIY TYSVENGNIV CGGTNPCKKQ ICECDRAAAI CFRDNLKTYD
SKTYWKYPKK NCKEESEPC
