Q8JFG0 (PA21B_VIPAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2, B chain EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase Vaspin chain B
Organism	Vipera aspis aspis (Aspic viper)
Taxonomic identifier	194601 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Vipera

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 transcript level

General annotation (Comments)

Function	PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. The vaspin complex shows postsynaptic neurotoxicity, while the isolated vaspin B chain is a presynaptic neurotoxin By similarity.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Heterodimer of a weakly toxic basic protein having phospholipase A2 activity (B chain) and a nontoxic acidic protein functioning as its inhibitor (A chain).
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Neurotoxin Postsynaptic neurotoxin Presynaptic neurotoxin Toxin
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	other organism postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW other organism presynaptic membrane 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	By similarity
	Chain	17 – 138	122	Phospholipase A2, B chain		PRO_0000022968
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)
	Q8JFG0 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 28C749D504D1EA3E	FASTA	138	15,610
	10 20 30 40 50 60 MRILWIVAVC LIGVEGNLFQ FAKMINGKLG AFSVWNYISY GCYCGWGGQG TPKDATDRCC 70 80 90 100 110 120 FVHDCCYGRV RGCNPKLAIY SYSFKKGNIV CGKNNGCLRD ICECDRVAAN CFHQNKNTYN 130 KNYRFLSSSR CRQTSEQC

References

[1]

"Toxicity evolution of Vipera aspis aspis venom: identification and molecular modeling of a novel phospholipase A(2) heterodimer neurotoxin." Jan V., Maroun R.C., Robbe-Vincent A., De Haro L., Choumet V. FEBS Lett. 527:263-268(2002) [PubMed: 12220671] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

[2]

"Sequences and structural organization of phospholipase A2 genes from Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom. Identification of the origin of a new viper population based on ammodytin I1 heterogeneity." Guillemin I., Bouchier C., Garrigues T., Wisner A., Choumet V. Eur. J. Biochem. 270:2697-2706(2003) [PubMed: 12823540] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ459807 mRNA. Translation: CAD30850.1. AY243576 Genomic DNA. Translation: AAO86504.1.
3D structure databases
ProteinModelPortal	Q8JFG0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG008137.
Family and domain databases
InterPro	IPR016090. PLipase_A2. IPR013090. PLipase_A2_AS. IPR001211. PLipase_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.
SMART	SM00085. PA2c. 1 hit. [Graphical view]
SUPFAM	SSF48619. PhospholipaseA2. 1 hit.
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21B_VIPAP

Accession

Primary (citable) accession number: Q8JFG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	October 1, 2002
Last modified:	November 16, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program