PA2B1_HEMHA
ID PA2B1_HEMHA Reviewed; 119 AA.
AC P00595;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Basic phospholipase A2 DE-1;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Hemachatus haemachatus (Rinkhals) (Sepedon haemachatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Hemachatus.
OX NCBI_TaxID=8626;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=1236145; DOI=10.1111/j.1432-1033.1975.tb04025.x;
RA Joubert F.J.;
RT "Hemachatus haemachatus (Ringhals) venom. Purification, some properties and
RT amino-acid sequence of phospholipase A (fraction DE-I).";
RL Eur. J. Biochem. 52:539-544(1975).
RN [2]
RP SITE.
RX PubMed=7222060; DOI=10.1016/0041-0101(80)90081-1;
RA Yang C.C., King K.;
RT "Chemical modification of the histidine residue in phospholipase A2 from
RT the Hemachatus haemachatus snake venom.";
RL Toxicon 18:529-547(1980).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- TOXIC DOSE: LD(50) is 8.6 mg/kg by intravenous injection.
CC -!- MISCELLANEOUS: Two forms of phospholipase A2 are found in Ringhals
CC venom.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PIR; A00738; PSRIA.
DR AlphaFoldDB; P00595; -.
DR SMR; P00595; -.
DR PRIDE; P00595; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Toxin.
FT CHAIN 1..119
FT /note="Basic phospholipase A2 DE-1"
FT /id="PRO_0000161649"
FT ACT_SITE 93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035,
FT ECO:0000255|PROSITE-ProRule:PRU10036"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 47
FT /note="Activity and toxicity lost upon alkylation, Ca(2+)
FT markedly slows inactivation"
FT DISULFID 11..71
FT /evidence="ECO:0000250"
FT DISULFID 26..118
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..99
FT /evidence="ECO:0000250"
FT DISULFID 50..92
FT /evidence="ECO:0000250"
FT DISULFID 60..85
FT /evidence="ECO:0000250"
FT DISULFID 78..90
FT /evidence="ECO:0000250"
SQ SEQUENCE 119 AA; 13519 MW; 4DEDD044EFA97035 CRC64;
NLYQFKNMIK CTVPSRSWWH FANYGCYCGR GGSGTPVDDL DRCCQTHDNC YSDAEKISGC
RPYFKTYSYD CTKGKLTCKE GNNECAAFVC KCDRLAAICF AGAHYNDNNN YIDLARHCQ
