Reviewed, UniProtKB/Swiss-Prot Q9PUH0 (PA214_AUSSU)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme S8-51     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase     ASPLA14
Organism	Austrelaps superbus (Australian copperhead)
Taxonomic identifier	29156 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Austrelaps

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits collagen-induced platelet aggregation By similarity.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Calcium Probable.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Toxin
PTM	Disulfide bond
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 – 19	19	Potential
	Propeptide	20 – 27	8	Potential		PRO_0000022811
	Chain	28 – 146	119	Phospholipase A2 isozyme S8-51		PRO_0000022812
Sites
	Active site	75	1	By similarity
	Active site	120	1	By similarity
	Metal binding	55	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	57	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	59	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	76	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	38 ↔ 98		By similarity
	Disulfide bond	54 ↔ 145		By similarity
	Disulfide bond	56 ↔ 72		By similarity
	Disulfide bond	71 ↔ 126		By similarity
	Disulfide bond	78 ↔ 119		By similarity
	Disulfide bond	87 ↔ 112		By similarity
	Disulfide bond	105 ↔ 117		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PUH0-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B3D1EBF6E2134D04	FASTA	146	16,212
	10 20 30 40 50 60 MYPAHLLVLL AVCVSLLGAA SIPPQPLNLV QFSYLIQCAN HGSRATWHYT DYGCYCGSGG 70 80 90 100 110 120 SGTPVDELDR CCQTHDNCYG EAEKKGCYPK MSAYDYYCGG DGPYCRNIRK ECQRFVCDCD 130 140 AIAAKCFARA PYNDANWDID TETRCQ

References

[1]

"Phospholipase A(2) with platelet aggregation inhibitor activity from Austrelaps superbus venom: protein purification and cDNA cloning." Singh S.B., Armugam A., Kini R.M., Jeyaseelan K. Arch. Biochem. Biophys. 375:289-303(2000) [PubMed: 10700385] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF184140 mRNA. Translation: AAD56563.1.
3D structure databases
HSSP	HSSP built from PDB template 1AE7 based on UniProtKB P00608.
SMR	Q9PUH0. Positions 28-146.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q9PUH0.
Enzyme and pathway databases
BRENDA	3.1.1.4. 298393.
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

PA214_AUSSU

Accession

Primary (citable) accession number: Q9PUH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)