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Reviewed, UniProtKB/Swiss-Prot Q8UW08 (PA20_LAPHA)

Last modified November 24, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Phospholipase A2
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismLapemis hardwickii (Hardwick's sea snake)
Taxonomic identifier8781 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaHydrophiidaeLapemis

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland Probable.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 276 By similarity
PRO_0000022876
Chain28 – 146119Phospholipase A2
PRO_0000022877

Sites

Active site751 By similarity
Active site1201 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 ↔ 98 By similarity
Disulfide bond54 ↔ 145 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 126 By similarity
Disulfide bond78 ↔ 119 By similarity
Disulfide bond87 ↔ 112 By similarity
Disulfide bond105 ↔ 117 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8UW08-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: FDD58BF5BD8E38C1

FASTA14616,114
        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAA SIPPLPLNLV QFSYVITCAN HGRRSSLDYA DYGCYCGAGG 

        70         80         90        100        110        120 
SGTPVDELDR CCQIHDDCYG EAEKQGCYPK MLIYDYYCGS DGPYCRNVKK KCNRMVCDCD 

       130        140 
VAAAKCFARN AYNNANYNID TNKRCK 

« Hide

References

[1]"A novel PLA2-like cDNA clone from sea snake venom."
Wei J., Yang W., Zhao G., Zhong X., Xu A.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF205378 mRNA. Translation: AAL54920.1.

3D structure databases

SMRQ8UW08. Positions 28-146.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ8UW08.

Enzyme and pathway databases

BRENDA3.1.1.4. 274608.

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.
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...

Entry information

Entry namePA20_LAPHA
AccessionPrimary (citable) accession number: Q8UW08
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2002
Last modified: November 24, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

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