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P15445 (PA2_NAJNA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospholipase A2, acidic

EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Phospholipase A2 2
Short name=PLA22
OrganismNaja naja (Indian cobra)
Taxonomic identifier35670 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeElapinaeNaja

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. Like most other acidic phospholipases, this protein is not neurotoxic.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Homotrimer.

Subcellular location

Secreted Ref.3.

Tissue specificity

Expressed by the venom gland. Ref.3

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 term3D-structure
Direct 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, acidic
PRO_0000161669

Sites

Active site471
Active site931
Metal binding271Calcium; via carbonyl oxygen
Metal binding291Calcium; via carbonyl oxygen
Metal binding311Calcium; via carbonyl oxygen
Metal binding481Calcium Ref.4

Amino acid modifications

Disulfide bond11 ↔ 71 Ref.4
Disulfide bond26 ↔ 118 Ref.4
Disulfide bond28 ↔ 44 Ref.4
Disulfide bond43 ↔ 99 Ref.4
Disulfide bond50 ↔ 92 Ref.4
Disulfide bond60 ↔ 85 Ref.4
Disulfide bond78 ↔ 90 Ref.4

Secondary structure

...................... 119
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15445 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: B725291AAB522966

FASTA11913,346
        10         20         30         40         50         60 
NLYQFKNMIK CTVPSRSWWD FADYGCYCGR GGSGTPVDDL DRCCQVHDNC YNEAEKISGC 

        70         80         90        100        110 
WPYFKTYSYE CSQGTLTCKG DNNACAASVC DCDRLAAICF AGAPYNDNNY NIDLKARCQ 

« Hide

References

[1]"Amino acid sequence and circular dichroism of Indian cobra (Naja naja naja) venom acidic phospholipase A2."
Davidson F.F., Dennis E.A.
Biochim. Biophys. Acta 1037:7-15(1990) [PubMed: 2294972] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Phospholipase A2 from cobra (Naja naja naja) venom. Primary structure and subspecies variation."
Shafqat J., Beg O.U., Joernvall H., Zaidi Z.H.
Protein Seq. Data Anal. 2:451-452(1989) [PubMed: 2626425] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[3]"Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka."
Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G., Athauda S.B., Moriyama A.
Biomed. Res. 31:71-81(2010) [PubMed: 20203422] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Venom.
[4]"Crystal structure of phospholipase A2 from Indian cobra reveals a trimeric association."
Fremont D.H., Anderson D.H., Wilson I.A., Dennis E.A., Xuong N.-H.
Proc. Natl. Acad. Sci. U.S.A. 90:342-346(1993) [PubMed: 8419939] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRS07528.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3DX-ray1.80A1-119[»]
1A3FX-ray2.65A/B/C1-119[»]
1OWSX-ray2.30A3-118[»]
B4-119[»]
1PSHX-ray2.30A/B/C1-119[»]
2WQ5X-ray1.65A1-119[»]
ProteinModelPortalP15445.
SMRP15445. 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 namePA2_NAJNA
AccessionPrimary (citable) accession number: P15445
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 19, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families