Skip Header

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

P25498 (PA21B_NAJOX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase A2 isozyme E
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismNaja oxiana (Central Asian cobra) (Oxus cobra)
Taxonomic identifier8657 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Naja

Protein attributes

Sequence length119 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

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.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
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

Chain1 – 119119Phospholipase A2 isozyme E
PRO_0000161670

Sites

Active site471 By similarity
Active site931 By similarity
Metal binding271Calcium; via carbonyl oxygen By similarity
Metal binding291Calcium; via carbonyl oxygen By similarity
Metal binding311Calcium; via carbonyl oxygen By similarity
Metal binding481Calcium By similarity

Amino acid modifications

Disulfide bond11 ↔ 71 By similarity
Disulfide bond26 ↔ 118 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 99 By similarity
Disulfide bond50 ↔ 92 By similarity
Disulfide bond60 ↔ 85 By similarity
Disulfide bond78 ↔ 90 By similarity

Sequences

Sequence LengthMass (Da)Tools
P25498 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: CC856D62685AA172

FASTA11913,229
        10         20         30         40         50         60 
NLYQFKNMIK CTVPSRSWLD FANYGCYCGR GGSGTPVDDL DRCCQIHDNC YNEAGKISGC 

        70         80         90        100        110 
WPYFKTYSYE CSQGTLTCKG DNNSCAASVC DCDRLAAICF AGAPYNNDNY NINLKARCQ

« Hide

References

[1]"Complete amino acid sequence of phospholipase A2 (isozyme E3) from the venom of middle Asian cobra Naja naja oxiana."
Ovchinnikov Y.A., Miroshnikov A.I., Nazimov I.V., Apsalaon U.R., Soldatova L.N.
Bioorg. Khim. 5:805-813(1979)
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRJN0403.

3D structure databases

ProteinModelPortalP25498.
SMRP25498. Positions 1-119.
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 namePA21B_NAJOX
AccessionPrimary (citable) accession number: P25498
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 19, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents