Reviewed, UniProtKB/Swiss-Prot P00625 (PA21B_TRIOK)

Names and origin

Protein names	Recommended name:     Phospholipase A2 PLA2-01     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase     Phospholipase A2 isozyme DE-I
Organism	Trimeresurus okinavensis (Hime-habu) (Ovophis okinavensis)
Taxonomic identifier	8769 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Ovophis

Protein attributes

Sequence length	139 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. Like most other acidic phospholipases, this protein is not neurotoxic.
Catalytic activity	Phosphatidylcholine + H2O = 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 II subfamily.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
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	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 – 16	16	Ref.2
	Chain	17 – 139	123	Phospholipase A2 PLA2-01 Ref.2		PRO_0000022966
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 ↔ 132		By similarity
	Disulfide bond	44 ↔ 60		By similarity
	Disulfide bond	59 ↔ 111		By similarity
	Disulfide bond	65 ↔ 139		By similarity
	Disulfide bond	66 ↔ 104		By similarity
	Disulfide bond	73 ↔ 97		By similarity
	Disulfide bond	91 ↔ 102		By similarity
Experimental info
	Sequence conflict	39 – 41	3	Missing in BAA08385. Ref.1
	Sequence conflict	83	1	S → T AA sequence Ref.2
	Sequence conflict	86	1	N → E AA sequence Ref.2
	Sequence conflict	90	1	T → S AA sequence Ref.2
	Sequence conflict	94 – 95	2	EN → ND AA sequence Ref.2
	Sequence conflict	117	1	D → N AA sequence Ref.2
	Sequence conflict	120	1	N → D AA sequence Ref.2
	Sequence conflict	135 – 136	2	ES → SE AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P00625-1 [UniParc]. Last modified November 28, 2002. Version 2. Checksum: E0FBB7B688925137	FASTA	139	15,584
	10 20 30 40 50 60 MRTLWIMAVL LLGVEGHLMQ FETLIMKIAG RSGVWWYGSY GCYCGAGGQG RPQDPSDRCC 70 80 90 100 110 120 FVHDCCYGKV TGCNTKDEFY TYSEENGAIT CGGENPCLKE VCECDLAAAI CFRDNLDTYN 130 SKKYWMFPAK NCLEESEPC

References

[1]	"Accelerated evolution of Trimeresurus okinavensis venom gland phospholipase A2 isozyme-encoding genes." Nobuhisa I., Nakashima K., Deshimaru M., Ogawa T., Shimohigashi Y., Fukumaki Y., Sakaki Y., Hattori S., Kihara H., Ohno M. Gene 172:267-272(1996) [PubMed: 8682315] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Liver and Venom gland.
[2]	"Snake venoms. Purification, some properties and amino acid sequence of a phospholipase A2 (DE-I) from Trimeresurus okinavensis (Hime-habu) venom." Joubert F.J., Haylett T. Hoppe-Seyler's Z. Physiol. Chem. 362:997-1006(1981) [PubMed: 7275018] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-139. Tissue: Venom.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D49388 mRNA. Translation: BAA08383.1. D49390 Genomic DNA. Translation: BAA08385.1. Sequence problems.
PIR	PSTV. JC4874.
3D structure databases
HSSP	HSSP built from PDB template 1BK9 based on UniProtKB P14418.
SMR	P00625. Positions 18-139.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00625.
Enzyme and pathway databases
BRENDA	3.1.1.4. 18554.
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_TRIOK

Accession

Primary (citable) accession number: P00625
Secondary accession number(s): P79836, Q92151

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 28, 2002
Last modified:	June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)