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Reviewed, UniProtKB/Swiss-Prot P60043 (PA21B_NAJSG)

Last modified June 16, 2009. Version 49. 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 isoform 1
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismNaja sagittifera (Andaman cobra)
Taxonomic identifier195058 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Naja

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Protein attributes

Sequence length126 AA.
Sequence statusFragment.
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.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Heterodimer formed between two homologous isoforms: isoform 1 and isoform 2.

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
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

Propeptide‹1 – 7›7
PRO_0000022924
Chain8 – 126119Phospholipase A2 isoform 1
PRO_0000022925

Sites

Active site541 By similarity
Active site1001 By similarity
Metal binding341Calcium; via carbonyl oxygen By similarity
Metal binding361Calcium; via carbonyl oxygen By similarity
Metal binding381Calcium; via carbonyl oxygen By similarity
Metal binding551Calcium By similarity

Amino acid modifications

Disulfide bond18 ↔ 78
Disulfide bond33 ↔ 125
Disulfide bond35 ↔ 51
Disulfide bond50 ↔ 106
Disulfide bond57 ↔ 99
Disulfide bond67 ↔ 92
Disulfide bond85 ↔ 97

Experimental info

Non-terminal residue11

Secondary structure

1 ...................... 126
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P60043-1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 07D0BFA119F6A8B2

FASTA12614,003
        10         20         30         40         50         60 
SNRPMPLNTY QFKNMIQCTV PKRSWWDFAD YGCYCGRGGS GTPIDDLDRC CQVHDNCYNS 

        70         80         90        100        110        120 
AREQGGCRPK QKTYSYECKA GTLSCSGSNN SCAATVCDCD RLAAICFAGA PYNDNNYNID 


LKARCQ

« Hide

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References

[1]"Phospholipase A2 isoform from Indian cobra."
Paramasivam M., Saravanan K., Hariprasad R.G., Jabeen T., Sharma S., Singh T.P., Srinivasan A.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]Jabeen T., Varma A.K., Paramasivam M., Singh N., Singh R.K., Sharma S., Srinivasan A., Singh T.P.
Submitted (AUG-2002) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 8-126 IN COMPLEX WITH ISOFORM 2.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY422775 mRNA. Translation: AAR00253.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MH2X-ray2.70A8-126[»]
1MH7X-ray2.00A10-126[»]
1MH8X-ray1.86A10-126[»]
1S6BX-ray1.60A8-126[»]
1XXWX-ray2.70A8-125[»]
2RD4X-ray2.97A8-126[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP60043.

Enzyme and pathway databases

BRENDA3.1.1.4. 294523.

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_NAJSG
AccessionPrimary (citable) accession number: P60043
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: May 10, 2004
Last modified: June 16, 2009
This is version 49 of the entry and version 2 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