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Reviewed, UniProtKB/Swiss-Prot P00599 (PA21B_NAJME)

Last modified June 16, 2009. Version 75. 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 isozyme DE-I
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismNaja melanoleuca (Forest cobra) (Black-lipped cobra)
Taxonomic identifier8643 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Naja

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Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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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: 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

Chain1 – 118118Phospholipase A2 isozyme DE-I
PRO_0000161663

Sites

Active site471 By similarity
Active site921 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 ↔ 72 By similarity
Disulfide bond26 ↔ 117 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 98 By similarity
Disulfide bond50 ↔ 91 By similarity
Disulfide bond60 ↔ 84 By similarity
Disulfide bond78 ↔ 89 By similarity

Secondary structure

1 ...................... 118
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00599-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0B2792570FF5D94D

FASTA11813,473
        10         20         30         40         50         60 
NLYQFKNMIH CTVPNRPWWH FANYGCYCGR GGKGTPVDDL DRCCQIHDKC YDEAEKISGC 

        70         80         90        100        110 
WPYIKTYTYE SCQGTLTCKD GGKCAASVCD CDRVAANCFA RATYNDKNYN IDFNARCQ

« Hide

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References

[1]"The amino acid sequence of phospholipase A, fractions DE-I and DE-II."
Joubert F.J.
Biochim. Biophys. Acta 379:345-359(1975) [PubMed: 1122292] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Naja melanoleuca (forest cobra) venom. Purification and some properties of phospholipases A."
Joubert F.J., van der Walt S.J.
Biochim. Biophys. Acta 379:317-328(1975) [PubMed: 1122290] [Abstract]
Cited for: DISULFIDE BONDS.

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Cross-references

Sequence databases

PIRPSNJ1W. A00741.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OO1model-A1-118[»]
SMRP00599. Positions 1-118.
ModBaseSearch...

Phylogenomic databases

HOVERGENP00599.

Enzyme and pathway databases

BRENDA3.1.1.4. 95991.

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 namePA21B_NAJME
AccessionPrimary (citable) accession number: P00599
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 75 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