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Reviewed, UniProtKB/Swiss-Prot P0CAS6 (PA216_CRODU)

Last modified September 22, 2009. Version 3. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phospholipase A2 F16
    EC=3.1.1.4
Alternative name(s):
    CdtF16
    Phosphatidylcholine 2-acylhydrolase
OrganismCrotalus durissus terrificus (South American rattlesnake)
Taxonomic identifier8732 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

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Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. produces neuromuscular blockade in chick biventer cervicis preparations in the absence and presence of crotapotin. In contrast, in mouse phrenic nerve-diaphragm preparations, the neuromuscular blockade is dependent on crotapotin. Ref.1

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Enzyme regulation

Pre-incubation with heparin markedly reduces the neurotoxicity of this toxin. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.9.

Temperature dependence:

Optimum temperature is 25 degrees Celsius.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Neurotoxin
Toxin
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processlipid 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 componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase A2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Phospholipase A2 F16
PRO_0000376923

Sites

Active site471 By similarity
Active site891 By similarity
Metal binding271Calcium; via carbonyl oxygen By similarity
Metal binding291Calcium; via carbonyl oxygen By similarity
Metal binding311Calcium; via carbonyl oxygen By similarity
Metal binding481Calcium By similarity

Amino acid modifications

Disulfide bond26 ↔ 115 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 95 By similarity
Disulfide bond49 ↔ 122 By similarity
Disulfide bond50 ↔ 88 By similarity
Disulfide bond57 ↔ 81 By similarity
Disulfide bond75 ↔ 86 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P0CAS6-1 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 49A0BA3B85284C08

FASTA12214,332
        10         20         30         40         50         60 
SLLQFNKMIK FETRKNAVPF YAFYGCYCGW GGRRRPKDAT DRCCFVHDCC YEKVTKCNTK 

        70         80         90        100        110        120 
WDIYRYSLKS GYITCGKGTW CKEQICECDR VAAECLRRSL STYKNGYMFY PDSRCRGPSE 


TC

« Hide

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References

[1]"Biochemical, pharmacological and structural characterization of a new PLA2 from Crotalus durissus terrificus (South American rattlesnake) venom."
Hernandez-Oliveira S., Toyama M.H., Toyama D.O., Marangoni S., Hyslop S., Rodrigues-Simioni L.
Protein J. 24:233-242(2005) [PubMed: 16283546] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Venom.

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Cross-references

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR016090. Phospholipase_A2.
IPR013090. Phospholipase_A2_AS.
IPR001211. Phospholipase_A2_euk.
[Graphical view]
Gene3DG3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHERPTHR11716. Phospholipase_A2. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePA216_CRODU
AccessionPrimary (citable) accession number: P0CAS6
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents