Skip Header

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

Reviewed, UniProtKB/Swiss-Prot P80966 (PA21B_OPHHA)

Last modified November 24, 2009. Version 70. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Phospholipase A2, acidic 1
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    APLA2-1
    OHV A-PLA2
      Short name=OHV-APLA2
OrganismOphiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifier8665 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Ophiophagus

Hide | Top

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Exhibits cardiotoxicity, myotoxicity, antiplatelet activity, and edema-inducing 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.

Hide | Top

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionCardiotoxin
Hydrolase
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 276
PRO_0000022942
Chain28 – 151124Phospholipase A2, acidic 1
PRO_0000022943

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

Secondary structure

1 ........................ 151
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P80966-1 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: F1E021B886BC4BEB

FASTA15116,444
        10         20         30         40         50         60 
MNPAHLLVLS AVCVSLLGAS SIPPQPLHLI QFGNMIQCTV PGFLSWIKYA DYGCYCGAGG 

        70         80         90        100        110        120 
SGTPVDKLDR CCQVHDNCYT QAQKLPACSS IMDSPYVKIY SYDCSERTVT CKADNDECAA 

       130        140        150 
FICNCDRVAA HCFAASPYNN NNYNIDTTTR C

« Hide

Hide | Top

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.
[2]"Complete amino acid sequence of an acidic, cardiotoxic phospholipase A2 from the venom of Ophiophagus hannah (King Cobra): a novel cobra venom enzyme with 'pancreatic loop'."
Huang M.Z., Gopalakrishnakone P., Chung M.C.M., Kini R.M.
Arch. Biochem. Biophys. 338:150-156(1997) [PubMed: 9028866] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-151.
Tissue: Venom.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF302908 mRNA. Translation: AAG23964.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GP7X-ray2.60A/B/C1-151[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP80966.

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.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry namePA21B_OPHHA
AccessionPrimary (citable) accession number: P80966
Secondary accession number(s): Q9DF32
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 30, 2002
Last modified: November 24, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Hide | Top

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