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Reviewed, UniProtKB/Swiss-Prot P59359 (PA21B_AUSSU)

Last modified November 24, 2009. Version 43. 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 S2-22
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismAustrelaps superbus (Australian copperhead)
Taxonomic identifier29156 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeAcanthophiinaeAustrelaps

Protein attributes

Sequence length145 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_0000022785
Chain28 – 145118Phospholipase A2 isozyme S2-22
PRO_0000022786

Sites

Active site751 By similarity
Active site1211 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 ↔ 99 By similarity
Disulfide bond54 ↔ 144 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 127 By similarity
Disulfide bond78 ↔ 120 By similarity
Disulfide bond88 ↔ 113 By similarity
Disulfide bond106 ↔ 118 By similarity

Sequences

Sequence LengthMass (Da)Tools
P59359-1 [UniParc].

Last modified February 28, 2003. Version 1.
Checksum: D38F999D2C7B5C82

FASTA14516,133
        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAS DIPPQPLNLV QFSNMIQCAN HGRRPTSNYM DYGCYCGKGG 

        70         80         90        100        110        120 
SGTPVDELDR CCKIHDDCYG EAEKSQKCAP YWTWYTWKCG SDGPQCDDSK TGCQRFVCDC 

       130        140 
DATAAKCFAK APYNKENYNI KTRCQ 

« 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
AY178051 mRNA. Translation: AAO21118.1.

3D structure databases

SMRP59359. Positions 28-145.
ModBaseSearch...

Phylogenomic databases

HOVERGENP59359.

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 namePA21B_AUSSU
AccessionPrimary (citable) accession number: P59359
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: February 28, 2003
Last modified: November 24, 2009
This is version 43 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