Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P81237 (PA22_ACAAN)

Last modified January 19, 2010. Version 56. 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

Names and origin

Protein namesRecommended name:
    Phospholipase A2
    EC=3.1.1.4
Alternative name(s):
    Acanthin II
    Phosphatidylcholine 2-acylhydrolase
OrganismAcanthophis antarcticus (Common death adder)
Taxonomic identifier8605 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeAcanthophiinaeAcanthophis

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Exhibits antiplatelet activity.

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 I subfamily.

Ontologies

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

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118Phospholipase A2
PRO_0000161592

Sites

Active site481 By similarity
Active site921 By similarity
Metal binding281Calcium; via carbonyl oxygen By similarity
Metal binding301Calcium; via carbonyl oxygen By similarity
Metal binding321Calcium; via carbonyl oxygen By similarity
Metal binding491Calcium By similarity

Amino acid modifications

Disulfide bond11 ↔ 71 By similarity
Disulfide bond27 ↔ 117 By similarity
Disulfide bond29 ↔ 45 By similarity
Disulfide bond44 ↔ 98 By similarity
Disulfide bond51 ↔ 91 By similarity
Disulfide bond60 ↔ 84 By similarity
Disulfide bond78 ↔ 89 By similarity

Sequences

Sequence LengthMass (Da)Tools
P81237-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: E1477D186C06B3EB

FASTA11812,884
        10         20         30         40         50         60 
NLYQFGGMIQ CANKGARSWL SYVNYGCYCG WGGSGTPVDE LDRCCQIHDN CYGEAEKKRC 

        70         80         90        100        110 
GPKMTLYSWE CANDVPVCNS KSACEGFVCD CDAAAAKCFA KAPYNKNNIG IGSKTRCQ 

« Hide

References

[1]"Purification, characterization, and amino acid sequence determination of acanthins, potent inhibitors of platelet aggregation from Acanthophis antarcticus (common death adder) venom."
Chow G., Subburaju S., Kini R.M.
Arch. Biochem. Biophys. 354:232-238(1998) [PubMed: 9637731] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

3D structure databases

SMRP81237. Positions 1-118.
ModBaseSearch...

Phylogenomic databases

HOVERGENP81237.

Enzyme and pathway databases

BRENDA3.1.1.4. 291618.

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...

Entry information

Entry namePA22_ACAAN
AccessionPrimary (citable) accession number: P81237
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 19, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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