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Reviewed, UniProtKB/Swiss-Prot Q45Z30 (PA21_TROCA)

Last modified June 16, 2009. Version 28. 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, acidic 1
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase 1
      Short name=PLA-1
OrganismTropidechis carinatus (Australian rough-scaled snake)
Taxonomic identifier100989 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeNotechinaeTropidechis

Protein attributes

Sequence length151 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.

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
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Toxin
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

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 – 2727 Potential
Chain28 – 151124Phospholipase A2, acidic 1
PRO_0000043276

Sites

Active site751 By similarity
Active site1261 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 ↔ 104 By similarity
Disulfide bond54 ↔ 151 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 132 By similarity
Disulfide bond78 ↔ 125 By similarity
Disulfide bond88 ↔ 118 By similarity
Disulfide bond111 ↔ 123 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q45Z30-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 663C0EF2DEB9935A

FASTA15116,921
        10         20         30         40         50         60 
MYPAHLLVLL AVCVSLLGAA SIPARPLNLY QFGNMIQCAN HGRRPTRHYM DYGCYCGKGG 

        70         80         90        100        110        120 
SGTPVDELDR CCQTHDDCYG EAEKLPACNY MMSGPYYNTY SYECNDGELT CKDNNDECKA 

       130        140        150 
FICNCDRTAA ICFARTPYND ANWNIDTKTR C 

« Hide

References

[1]"Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species."
St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.
Cell. Mol. Life Sci. 62:2679-2693(2005) [PubMed: 16261251] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

Cross-references

Sequence databases

DQ085836 mRNA. Translation: AAZ22654.1.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENQ45Z30.

Enzyme and pathway databases

BRENDA3.1.1.4. 295067.

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...

Entry information

Entry namePA21_TROCA
AccessionPrimary (citable) accession number: Q45Z30
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: September 13, 2005
Last modified: June 16, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

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