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Reviewed, UniProtKB/Swiss-Prot Q9PUG7 (PA217_AUSSU)

Last modified November 24, 2009. Version 49. 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 isozyme S17-58
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    ASPLA17
OrganismAustrelaps superbus (Australian copperhead)
Taxonomic identifier29156 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeAcanthophiinaeAustrelaps

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits collagen-induced platelet aggregation By similarity.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Calcium Probable.

Subcellular location

Secreted By similarity.

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
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Toxin
   PTMDisulfide bond
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 278 Potential
PRO_0000022817
Chain28 – 152125Phospholipase A2 isozyme S17-58
PRO_0000022818

Sites

Active site751 By similarity
Active site1261 By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding571Calcium; via carbonyl oxygen By similarity
Metal binding591Calcium; via carbonyl oxygen By similarity
Metal binding761Calcium By similarity

Amino acid modifications

Disulfide bond38 ↔ 104 By similarity
Disulfide bond54 ↔ 151 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 132 By similarity
Disulfide bond78 ↔ 125 By similarity
Disulfide bond88 ↔ 118 By similarity
Disulfide bond111 ↔ 123 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PUG7-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 0F2BD5BDDCF04FCB

FASTA15216,641
        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAS NIPLPSLDFE QFGKMIQCTI PCEESCLAYM DYGCYCGPGG 

        70         80         90        100        110        120 
SGTPSDELDR CCQTHDNCYA EAGKLPACKA MLSEPYNDTY SYSCIERQLT CNDDNDECKA 

       130        140        150 
FICNCDRAAV ICFSGAPYND SNYDIGTIEH CK 

« Hide

References

[1]"Phospholipase A(2) with platelet aggregation inhibitor activity from Austrelaps superbus venom: protein purification and cDNA cloning."
Singh S.B., Armugam A., Kini R.M., Jeyaseelan K.
Arch. Biochem. Biophys. 375:289-303(2000) [PubMed: 10700385] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF184143 mRNA. Translation: AAD56410.1.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENQ9PUG7.

Enzyme and pathway databases

BRENDA3.1.1.4. 298393.

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 namePA217_AUSSU
AccessionPrimary (citable) accession number: Q9PUG7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: November 24, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

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