Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P20254 (PA20_PSEAU)

Last modified November 24, 2009. Version 66. 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 isozyme PA-10A
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismPseudechis australis (Mulga snake) (King brown snake)
Taxonomic identifier8670 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeAcanthophiinaePseudechis

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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.

Miscellaneous

There are many protein components with phospholipase A2 activity in the Mulga snake venom and some of them are myotoxic.

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 termDirect 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 118118Phospholipase A2 isozyme PA-10A
PRO_0000161685

Sites

Active site481 By similarity
Active site921 By similarity
Metal binding281Calcium; via carbonyl oxygen By similarity
Metal binding301Calcium; via carbonyl oxygen By similarity
Metal binding321Calcium; via carbonyl oxygen By similarity
Metal binding491Calcium By similarity

Amino acid modifications

Disulfide bond11 ↔ 71 By similarity
Disulfide bond27 ↔ 117 By similarity
Disulfide bond29 ↔ 45 By similarity
Disulfide bond44 ↔ 98 By similarity
Disulfide bond51 ↔ 91 By similarity
Disulfide bond60 ↔ 84 By similarity
Disulfide bond78 ↔ 89 By similarity

Sequences

Sequence LengthMass (Da)Tools
P20254-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 884D1D3A6E2B5FCB

FASTA11813,027
        10         20         30         40         50         60 
NLIQFSNMIQ CANKGSRPSL HYADYGCYCG WGGSGTPVDE LDRCCKVHDD CYDQAGKKGC 

        70         80         90        100        110 
FPKLTLYSWD CTGNVPICNP KSKCKDFVCA CDAAAAKCFA KAPYNKANWN IDTKTRCK 

« Hide

References

[1]"Amino acid sequences of eight phospholipases A2 from the venom of Australian king brown snake, Pseudechis australis."
Takasaki C., Yutani F., Kajiyashiki T.
Toxicon 28:329-339(1990) [PubMed: 2343466] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

Sequence databases

PIRE34860.

3D structure databases

SMRP20254. Positions 1-118.
ModBaseSearch...

Phylogenomic databases

HOVERGENP20254.

Enzyme and pathway databases

BRENDA3.1.1.4. 276288.

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.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA20_PSEAU
AccessionPrimary (citable) accession number: P20254
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 24, 2009
This is version 66 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