Reviewed, UniProtKB/Swiss-Prot P0CAS3 (PA212_CRODR)

Names and origin

Protein names	Recommended name:     Phospholipase A2 Cdr-12     EC=3.1.1.4 Alternative name(s):     Phosphatidylcholine 2-acylhydrolase
Organism	Crotalus durissus ruruima (South American rattlesnake) (Mt. Roraima rattlesnake)
Taxonomic identifier	221570 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

Protein attributes

Sequence length	122 AA.
Sequence status	Complete.
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. In mice, this toxin induces myonecrosis and edema upon intramuscular injections. In vitro, causes a potent blockade of neuromuscular transmission in young chicken biventer cervicis preparation and produces cytotoxicity in murine C2C12 skeletal muscle myotubes and lack cytolytic activity upon myoblasts in vitro. Ref.1
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.
Mass spectrometry	Molecular mass is 14333.49 Da from positions 1 - 122. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Myotoxin Neurotoxin Toxin
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis 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
	Chain	1 – 122	122	Phospholipase A2 Cdr-12		PRO_0000376920
Sites
	Active site	47	1	By similarity
	Active site	89	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 ↔ 95		By similarity
	Disulfide bond	49 ↔ 122		By similarity
	Disulfide bond	50 ↔ 88		By similarity
	Disulfide bond	57 ↔ 81		By similarity
	Disulfide bond	75 ↔ 86		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0CAS3-1 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: 6908533F02C03AE4	FASTA	122	14,334
	10 20 30 40 50 60 SLLQFNKMIK FETRKNAIPF YAFYGCYCGW GGQGRPKDAT DRCCIVHDCC YGKLAKCNTK 70 80 90 100 110 120 WDFYRYSLRS GYFQCGKGTW CEQQICECDR VAAECLRRSL STYRYGYMIY PDSRCREPSE TC

References

[1]

"Biochemical, pharmacological and structural characterization of two PLA2 isoforms Cdr-12 and Cdr-13 from Crotalus durissus ruruima snake venom." Ponce-Soto L.A., Baldasso P.A., Romero-Vargas F.F., Winck F.V., Novello J.C., Marangoni S. Protein J. 26:39-49(2007) [PubMed: 17203396] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
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.
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

PA212_CRODR

Accession

Primary (citable) accession number: P0CAS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	September 22, 2009
This is version 3 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)