P00623 (PA2A_CROAD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Acidic phospholipase A2 beta Short name=svPLA2 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase
Organism	Crotalus adamanteus (Eastern diamondback rattlesnake)
Taxonomic identifier	8729 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

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 protein level

General annotation (Comments)

Function	PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Dimer. Ref.2
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
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	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	Ref.2
	Chain	17 – 138	122	Acidic phospholipase A2 beta		PRO_0000161642
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
Natural variations
	Natural variant	133	1	E → Q in the alpha form.
Experimental info
	Sequence conflict	72	1	D → N AA sequence Ref.2
	Sequence conflict	130	1	N → D AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P00623 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 71B48637E52C9E0A	FASTA	138	15,433
	10 20 30 40 50 60 MRTLWIVAVL LLGVEGSLVQ FETLIMKVAK RSGLLWYSAY GCYCGWGGHG RPQDATDRCC 70 80 90 100 110 120 FVHDCCYGKA TDCNPKTVSY TYSEENGEIV CGGDDPCGTQ ICECDKAAAI CFRDNIPSYD 130 NKYWLFPPKN CREEPEPC

References

[1]	"A high-throughput venom-gland transcriptome for the eastern diamondback rattlesnake (Crotalus adamanteus) and evidence for pervasive positive selection across toxin classes." Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B. Toxicon 57:657-671(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus adamanteus. A new classification of phospholipases A2 based upon structural determinants." Heinrikson R.L., Krueger E.T., Keim P.S. J. Biol. Chem. 252:4913-4921(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-138, SUBUNIT. Tissue: Venom.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases
EMBL GenBank DDBJ	HQ414104 mRNA. Translation: AEJ31982.1.
PIR	PSRSAE. A00763.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG008137.
Family and domain databases
Gene3D	1.20.90.10. 1 hit.
InterPro	IPR001211. PLipase_A2. IPR013090. PLipase_A2_AS. IPR016090. PLipase_A2_dom. [Graphical view]
PANTHER	PTHR11716. PTHR11716. 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...
Other
BindingDB	P00623.
ChEMBL	CHEMBL5711.

Entry information

Entry name

PA2A_CROAD

Accession

Primary (citable) accession number: P00623
Secondary accession number(s): F8S100

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program