Reviewed, UniProtKB/Swiss-Prot Q90WA8 (PA22_BUNFA)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme 2     EC=3.1.1.4 Alternative name(s):     Phospholipase A2 isozyme II     KBf-2     KBf II     Phosphatidylcholine 2-acylhydrolase
Organism	Bungarus fasciatus (Banded krait)
Taxonomic identifier	8613 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length	145 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 By similarity.
Catalytic activity	Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group I subfamily.
Mass spectrometry	Molecular weight is 13003±1 Da from positions 18 - 135. Determined by ESI. In KBf-2. Ref.2

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
Technical term	Direct protein sequencing
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			PRO_0000022831
	Chain	28 – 145	118	Phospholipase A2 isozyme 2		PRO_0000022832
Sites
	Active site	73	1	By similarity
	Active site	119	1	By similarity
	Metal binding	53	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	55	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	56	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	74	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	38 ↔ 97		By similarity
	Disulfide bond	52 ↔ 144		By similarity
	Disulfide bond	54 ↔ 70		By similarity
	Disulfide bond	69 ↔ 125		By similarity
	Disulfide bond	76 ↔ 118		By similarity
	Disulfide bond	86 ↔ 111		By similarity
	Disulfide bond	104 ↔ 116		By similarity
Natural variations
	Natural variant	18	1	A → G
	Natural variant	114	1	T → N
	Natural variant	124	1	L → I

Sequences

	Sequence		Length	Mass (Da)
	Q90WA8-1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: 5599DA79109D0700	FASTA	145	15,769
	10 20 30 40 50 60 MNPAHLLVLL AVCVSLLAAA NIPPQSLNLL QFKNMIECAG TRTWMAYVKY GCYCGPGGTG 70 80 90 100 110 120 TPLDELDRCC QTHDQCYDNA KKFGNCIPYF KTYVYTCNKP DITCTGAKGS CGRTVCDCDR 130 140 AAALCFAAAP YNLANFGINK ETHCQ

References

[1]

"cDNA cloning and characterization of phospholipase A2 from the snake Bungarus fasciatus." Zha H., Zhang Y. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

[2]

"Sequences, geographic variations and molecular phylogeny of venom phospholipases and threefinger toxins of eastern India Bungarus fasciatus and kinetic analyses of its Pro31 phospholipases A2." Tsai I.-H., Tsai H.-Y., Saha A., Gomes A. FEBS J. 274:512-525(2007) [PubMed: 17166178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-145, PROTEIN SEQUENCE OF 28-47, MASS SPECTROMETRY. Tissue: Venom and Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ508412 mRNA. No translation available. AF387594 mRNA. Translation: AAK62361.1.
3D structure databases
HSSP	HSSP built from PDB template 1FE5 based on UniProtKB Q9DF52.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q90WA8.
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

PA22_BUNFA

Accession

Primary (citable) accession number: Q90WA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	June 26, 2007
Last modified:	November 25, 2008
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)