Q3C2C1 (PA22_ACAPL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 AP-PLA2-II EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase 2
Organism	Acanthaster planci (Crown-of-thorns starfish)
Taxonomic identifier	133434 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Echinodermata › Eleutherozoa › Asterozoa › Asteroidea › Valvatacea › Valvatida › Acanthasteridae › Acanthaster

Protein attributes

Sequence length	158 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. Has hemorrhagic and capillary permeability-increasing activities and hence is considered to be deeply involved in the local inflammation. Shows hemolytic activity only in the presence of phosphatidylcholine (PC). Ref.2
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Monomer.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
Biological process	Cytolysis Hemolysis Lipid degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Toxin
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism Inferred from electronic annotation. Source: UniProtKB-KW 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: 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	Potential
	Propeptide	17 – 23	7			PRO_0000272035
	Chain	24 – 158	135	Phospholipase A2 AP-PLA2-II		PRO_0000272036
Sites
	Active site	72	1	By similarity
	Active site	132	1	By similarity
	Metal binding	54	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	56	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	73	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	51 ↔ 158		By similarity
	Disulfide bond	53 ↔ 69		By similarity
	Disulfide bond	68 ↔ 138		By similarity
	Disulfide bond	75 ↔ 131		By similarity
	Disulfide bond	85 ↔ 124		By similarity
	Disulfide bond	109 ↔ 129		By similarity
Experimental info
	Sequence conflict	30	1	K → N AA sequence Ref.2
	Sequence conflict	65	1	T → L AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q3C2C1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: A013B58205747C22	FASTA	158	17,490
	10 20 30 40 50 60 MKTFLILAMA VALAKAQSTD EITNLVQFGK LVMCLGNIGY TEGLEYDGYG CFCGKGGKGT 70 80 90 100 110 120 PVDATDRCCE VHDNCYGQAV EEGKCWSVET YGTTYWYDQS TSGSCSIRCW EEGDYNSLVP 130 140 150 RKACKAAICE CDRKAAQCFA DNRPTFNRKY LNYAKDTC

References

[1]	"Molecular cloning of two toxic phospholipases A2 from the crown-of-thorns starfish Acanthaster planci venom." Ota E., Nagai H., Nagashima Y., Shiomi K. Comp. Biochem. Physiol. 143B:54-60(2006) [PubMed: 16275035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 131-158.
[2]	"Purification and properties of phospholipases A2 from the crown-of-thorns starfish (Acanthaster planci) venom." Shiomi K.A., Kazama A., Shimakura K., Nagashima Y. Toxicon 36:589-599(1998) [PubMed: 9643471] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-85, FUNCTION. Tissue: Spine.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB211368 mRNA. Translation: BAE46766.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZM6 based on UniProtKB P60045.
ProteinModelPortal	Q3C2C1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. False negative. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA22_ACAPL

Accession

Primary (citable) accession number: Q3C2C1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	November 22, 2005
Last modified:	October 19, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program