Reviewed, UniProtKB/Swiss-Prot Q91506 (PA21B_TRIMU)

Names and origin

Protein names	Recommended name:     Phospholipase A2 1     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase
Organism	Trimeresurus mucrosquamatus (Taiwan habu) (Protobothrops mucrosquamatus)
Taxonomic identifier	103944 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Protobothrops

Protein attributes

Sequence length	122 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Catalytic activity	Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	SecretedBy 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
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
	Chain	1 – 122	122	Phospholipase A2 1		PRO_0000161705
Sites
	Active site	47	1	By similarity
	Active site	88	1	By similarity
	Metal binding	27	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	29	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	31	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	48	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	26 ↔ 115		By similarity
	Disulfide bond	28 ↔ 44		By similarity
	Disulfide bond	43 ↔ 94		By similarity
	Disulfide bond	49 ↔ 122		By similarity
	Disulfide bond	50 ↔ 87		By similarity
	Disulfide bond	57 ↔ 81		By similarity
	Disulfide bond	75 ↔ 85		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q91506-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CA62DAAE5D284626	FASTA	122	13,615
	10 20 30 40 50 60 NLWQFENMIM KVAKKSGILS YSAYGCYCGW GGRGTPKDAT DRCCFVHDCC YGKVTGCNPK 70 80 90 100 110 120 LGKYTYSSEN GDIICGGDGP CKEVCECDRA AAICFRDNLD TYDRKTYWKY PASNCQEDSE PC

References

[1]	"Cloning and sequencing of an phospholipase A2 from Taiwan habu." Tsai I.-H. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X77088 mRNA. Translation: CAA54363.1.
PIR	S46979.
3D structure databases
HSSP	HSSP built from PDB template 1VAP based on UniProtKB P51972.
SMR	Q91506. Positions 1-122.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q91506.
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

PA21B_TRIMU

Accession

Primary (citable) accession number: Q91506

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)