Reviewed, UniProtKB/Swiss-Prot Q8QG87 (PA21_BOTIN)

Names and origin

Protein names	Recommended name:     Phospholipase A2 BITP01A     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase     BinTX-I
Organism	Bothrops insularis (Island jararaca) (Queimada jararaca)
Taxonomic identifier	8723 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length	138 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Induces edema in mice, produces neuromuscular blockade in chick biventer cervicis, increases CK release and produces myonecrosis. Ref.2
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	Secreted. Ref.2
Tissue specificity	Expressed by the venom gland. Ref.2
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily.
Mass spectrometry	Molecular mass is 13975 Da from positions 17 - 138. Determined by ESI. Ref.2

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Toxin
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Ref.2
	Chain	17 – 138	122	Phospholipase A2 BITP01A		PRO_0000022820
Sites
	Active site	63	1	By similarity
	Active site	105	1	By similarity
	Metal binding	43	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	45	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	47	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	64	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	42 ↔ 131		By similarity
	Disulfide bond	44 ↔ 60		By similarity
	Disulfide bond	59 ↔ 111		By similarity
	Disulfide bond	65 ↔ 138		By similarity
	Disulfide bond	66 ↔ 104		By similarity
	Disulfide bond	73 ↔ 97		By similarity
	Disulfide bond	91 ↔ 102		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8QG87-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: DFB41FD618A1CE54	FASTA	138	15,759
	10 20 30 40 50 60 MRTLWIMAVL LVGVEGNLWQ FGKMMNYVMG QSVVYKYFYY GCYCGWGGIG QPRDATDRCC 70 80 90 100 110 120 FVHDCCYGKV TGCDPKTDSY TYSKENGDVV CGGDDPCKKQ ICECDRVAAT CFRDNKDTYD 130 MKYWLYGAKN CQEESEPC

References

[1]	"A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs)." Junqueira-de-Azevedo I.L.M., Ho P.L. Gene 299:279-291(2002) [PubMed: 12459276] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Purification, sequencing and structural analysis of two acidic phospholipases A2 from the venom of Bothrops insularis (jararaca ilhoa)." Cogo J.C., Lilla S., Souza G.H.M.F., Hyslop S., de Nucci G. Biochimie 88:1947-1959(2006) [PubMed: 17140721] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-138, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY. Tissue: Venom.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF490535 mRNA. Translation: AAM09694.1.
3D structure databases
HSSP	HSSP built from PDB template 1M8R based on UniProtKB P14418.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q8QG87.
Enzyme and pathway databases
BRENDA	3.1.1.4. 289960.
Family and domain databases
InterPro	IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. IPR001211. Phospholipase_A2_euk. [Graphical view]
Gene3D	G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHER	PTHR11716. Phospholipase_A2. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PRINTS	PR00389. PHPHLIPASEA2.
ProDom	PD000303. PhospholipaseA2. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00085. PA2c. 1 hit. [Graphical view]
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21_BOTIN

Accession

Primary (citable) accession number: Q8QG87

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)