PA2A1_TRIGA
ID PA2A1_TRIGA Reviewed; 138 AA.
AC P20476; P87480; P87481;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 112.
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=Phospholipase A2 isozyme I;
DE Short=PLA2-I;
DE Flags: Precursor;
OS Trimeresurus gramineus (Bamboo pit viper) (Indian green tree viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=8767;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Venom gland;
RX PubMed=7777556; DOI=10.1073/pnas.92.12.5605;
RA Nakashima K., Nobuhisa I., Deshimaru M., Nakai M., Ogawa T.,
RA Shimohigashi Y., Fukumaki Y., Hattori M., Sakaki Y., Hattori S., Ohno M.;
RT "Accelerated evolution in the protein-coding regions is universal in
RT crotalinae snake venom gland phospholipase A2 isozyme genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5605-5609(1995).
RN [2]
RP PROTEIN SEQUENCE OF 17-138.
RC TISSUE=Venom;
RX PubMed=2048135; DOI=10.1016/0041-0101(91)90100-6;
RA Oda N., Nakamura H., Sakamoto S., Liu S.-Y., Kihara H., Chang C.-C.,
RA Ohno M.;
RT "Amino acid sequence of a phospholipase A2 from the venom of Trimeresurus
RT gramineus (green habu snake).";
RL Toxicon 29:157-166(1991).
RN [3]
RP PROTEIN SEQUENCE OF 17-54.
RC TISSUE=Venom;
RX PubMed=3448089; DOI=10.1093/oxfordjournals.jbchem.a122190;
RA Oda N., Sakai H., Shieh T.C., Nakamura H., Sakamoto S., Kihara H.,
RA Chang C.-C., Ohno M.;
RT "Purification and characterization of phospholipase A2 from Trimeresurus
RT gramineus venom.";
RL J. Biochem. 102:1441-1449(1987).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has high lipolytic
CC activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides.
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 -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06552.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D31774; BAA06552.1; ALT_INIT; mRNA.
DR EMBL; D31780; BAA06558.1; -; Genomic_DNA.
DR PIR; A39557; A39557.
DR AlphaFoldDB; P20476; -.
DR SMR; P20476; -.
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; Metal-binding; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:2048135,
FT ECO:0000269|PubMed:3448089"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 1"
FT /id="PRO_0000022959"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:O42187"
SQ SEQUENCE 138 AA; 15519 MW; 1D1EF551CCB155ED CRC64;
MRTLWIMAVL LVGVEGHLMQ FETLIMKVAG RSGVWYYGSY GCFCGAGGQG RPQDASDRCC
FVHDCCYGKV NGCDPKKDFY TYSEENGAIV CGGDDPCKKE ICECDKDAAI CFRDNKDTYD
NKYWFFPAKN CQEESEPC
