Reviewed, UniProtKB/Swiss-Prot P0CAS7 (PA217_CRODU)

Names and origin

Protein names	Recommended name:     Phospholipase A2 F17     EC=3.1.1.4 Alternative name(s):     CdtF17     Phosphatidylcholine 2-acylhydrolase
Organism	Crotalus durissus terrificus (South American rattlesnake)
Taxonomic identifier	8732 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 monomeric form, has anticoagulant activity and inhibits bactericial growth of the Gram-negative bacteria Xanthomonas axonopodis pv. passiflorae. Ref.1
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit. Ref.1
Enzyme regulation	Activated by heparin. Inhibited by its chaperone crotapotin. Ref.1
Subunit structure	When this PA2 is associated with crotapotin (F5 or F7), it forms the crotoxin protein.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the phospholipase A2 family. Group II subfamily.
Biophysicochemical properties	Kinetic parameters: KM=31.2 mM for 4-nitro-3-(octanoyloxy)benzoic acid Vmax=8.2 nmol/min/mg enzyme pH dependence: Optimum pH is 7.9. Temperature dependence: Optimum temperature is 10-30 degrees Celsius.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Antibiotic Antimicrobial Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to bacterium 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: 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 – 121	121	Phospholipase A2 F17		PRO_0000376924
Sites
	Active site	46	1	By similarity
	Active site	88	1	By similarity
	Metal binding	26	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	28	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	30	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	47	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	25 ↔ 114		By similarity
	Disulfide bond	27 ↔ 43		By similarity
	Disulfide bond	42 ↔ 94		By similarity
	Disulfide bond	48 ↔ 121		By similarity
	Disulfide bond	49 ↔ 87		By similarity
	Disulfide bond	56 ↔ 80		By similarity
	Disulfide bond	74 ↔ 85		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0CAS7-1 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: E06F8697975E036D	FASTA	121	14,368
	10 20 30 40 50 60 HLLQFNKMLK FETRKNAVPF YAFGCYCGWG GQRRPKDATD RCCFVHDCCY EKVTKCNTKW 70 80 90 100 110 120 DFYRYSLKSG YITCGKGTWC KEQICECDRV AAECLRRSLS TYKNEYMFYP DSRCREPSET C

References

[1]

"Structural and functional characterization of basic PLA2 isolated from Crotalus durissus terrificus venom." Oliveira D.G., Toyama M.H., Novello J.C., Beriam L.O.S., Marangoni S. J. Protein Chem. 21:161-168(2002) [PubMed: 12018617] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. 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

PA217_CRODU

Accession

Primary (citable) accession number: P0CAS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	September 22, 2009
This is version 4 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)