Reviewed, UniProtKB/Swiss-Prot Q75S48 (PA21_BUNCA)

Names and origin

Protein names	Recommended name:     Phospholipase A2-1     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase     PA2-I
Organism	Bungarus candidus (Malayan krait)
Taxonomic identifier	92438 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length	152 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.
Catalytic activity	Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	SecretedBy 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
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: InterPro phospholipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro phospholipase A2 activity Inferred from electronic annotation. Source: InterPro
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	By similarity		PRO_0000271454
	Chain	28 – 152	125	Phospholipase A2-1		PRO_5000051030
Sites
	Active site	75	1	By similarity
	Active site	126	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 ↔ 104		By similarity
	Disulfide bond	54 ↔ 151		By similarity
	Disulfide bond	56 ↔ 72		By similarity
	Disulfide bond	71 ↔ 132		By similarity
	Disulfide bond	78 ↔ 125		By similarity
	Disulfide bond	88 ↔ 118		By similarity
	Disulfide bond	111 ↔ 123		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q75S48-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4E1FF5C59401F763	FASTA	152	16,855
	10 20 30 40 50 60 MNPAYFLVLA AVCVSLLGAA NIPPQPLSFY RYTEMIQCTI RGSLTYLDYM DYGCYCGTGS 70 80 90 100 110 120 RGTPVDELDR CCQTHDNCYA EAEEHPKCSS LVKSPYMNLY SYTCSGGTIT CNADNDECGA 130 140 150 FICNCDRTAA LCFAKAPYNE ENKEIDISKR CQ

References

[1]

"Molecular cloning of the major lethal toxins from two kraits (Bungarus flaviceps and Bungarus candidus)." Yanoshita R., Ogawa Y., Murayama N., Omori-Satoh T., Saguchi K., Higuchi S., Khow O., Chanhome L., Samejima Y., Sitprija V. Toxicon 47:416-424(2006) [PubMed: 16458338] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB158302 mRNA. Translation: BAD06270.1.
3D structure databases
HSSP	HSSP built from PDB template 1A3D based on UniProtKB P15445.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q75S48.
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_BUNCA

Accession

Primary (citable) accession number: Q75S48

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	July 5, 2004
Last modified:	November 25, 2008
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)