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Q9PUH4 (PA210_AUSSU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospholipase A2 isozyme S5-32M

EC=3.1.1.4
Alternative name(s):
ASPLA10
Phosphatidylcholine 2-acylhydrolase
OrganismAustrelaps superbus (Lowland copperhead snake) (Hoplocephalus superbus)
Taxonomic identifier29156 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeAcanthophiinaeAustrelaps

Protein attributes

Sequence length146 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

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: InterPro

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_0000022803
Chain28 – 146119Phospholipase A2 isozyme S5-32M
PRO_0000022804

Sites

Active site751 By similarity
Active site1201 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 ↔ 98 By similarity
Disulfide bond54 ↔ 145 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 126 By similarity
Disulfide bond78 ↔ 119 By similarity
Disulfide bond87 ↔ 112 By similarity
Disulfide bond105 ↔ 117 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PUH4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9C00CAEACDFDA180

FASTA14616,379
        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAA SIPPQPLNLV QFSYLIQCAN HGSRATWHYT DYGCYCGKGG 

        70         80         90        100        110        120 
SGTPVDELDR CCKIHDDCYG EAEKKGCYPK MSAYDYYCGE NGPYCRNIKK ECQRFVCDCD 

       130        140 
VEAAKCFARA PYNDANWNID TKKRCQ 

« 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF184136 mRNA. Translation: AAD56559.1.

3D structure databases

ProteinModelPortalQ9PUH4.
SMRQ9PUH4. Positions 28-146.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008137.

Family and domain databases

InterProIPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_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]
SUPFAMSSF48619. PhospholipaseA2. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA210_AUSSU
AccessionPrimary (citable) accession number: Q9PUH4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: October 19, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families