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Reviewed, UniProtKB/Swiss-Prot Q9DF33 (PA22_OPHHA)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, acidic 2
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    APLA2-2
OrganismOphiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifier8665 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Ophiophagus

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Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Displays edema-inducing and moderate anticoagulant activities.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland Probable.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 276 Potential
PRO_0000022944
Chain28 – 146119Phospholipase A2, acidic 2
PRO_0000022945

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 ↔ 146 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

Secondary structure

1 ...................... 146
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9DF33-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 354F45F6B67690A7

FASTA14615,901
        10         20         30         40         50         60 
MNPAHLLVLS AVCVSLLGAS SIPPQPLHLV QFNGMIRCTI PGSIPWWDYS DYGCYCGSGG 

        70         80         90        100        110        120 
SGTPVDELDR CCQVHDNCYT QAQQLTECSP YSKRYSYDCS EGTLTCKADN DECAAFVCDC 

       130        140 
DRVAAICFAG APYNKENINI DTTTRC

« Hide

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References

[1]"Cloning and characterization of cDNAs encoding two acidic isoforms of phospholipase A2 in Guangxi King Cobra (Ophiophagus hannah)."
Wang Q.Y., Shu Y.Y.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF302907 mRNA. Translation: AAG23963.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1M8TX-ray2.10A/B/C/D/E/F28-146[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9DF33.

Enzyme and pathway databases

BRENDA3.1.1.4. 19088.

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.
ProDomPD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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 namePA22_OPHHA
AccessionPrimary (citable) accession number: Q9DF33
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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