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Reviewed, UniProtKB/Swiss-Prot Q9W7J4 (PA21B_PSETE)

Last modified January 19, 2010. Version 53. 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 1
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Pt-PLA1
OrganismPseudonaja textilis (Eastern brown snake)
Taxonomic identifier8673 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeAcanthophiinaePseudonaja

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Shows moderate PA2 activity and exhibits procoagulant property. Ref.1

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
   Biological processBlood coagulation
Lipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

lipid 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 – 1919 Potential
Propeptide20 – 278
PRO_0000022948
Chain28 – 154127Phospholipase A2 1
PRO_0000022949

Sites

Active site751 By similarity
Active site1261 By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding571Calcium; via carbonyl oxygen By similarity
Metal binding581Calcium; via carbonyl oxygen By similarity
Metal binding761Calcium By similarity

Amino acid modifications

Disulfide bond38 ↔ 104 By similarity
Disulfide bond54 ↔ 153 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
Q9W7J4-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 1A50E3D04492E2C5

FASTA15416,844
        10         20         30         40         50         60 
MHPAHLLVLL GVCVSLLGAA RIPPLPLSLD DFSNLITCAN RGSRSWLDYA HYGCFCGSGG 

        70         80         90        100        110        120 
SGTPVDDLDR CCQVHDNCFG DAEKLPACNY LFSGPYWNPY SYKCNEGEIT CTDDNDECAA 

       130        140        150 
FICNCDRTAA ICFAGATYND ENFMVTIKKK NICQ 

« Hide

References

[1]"Group IB phospholipase A2 from Pseudonaja textilis."
Armugam A., Gong N.L., Li X.J., Siew P.Y., Chai S.C., Nair R., Jeyaseelan K.
Arch. Biochem. Biophys. 421:10-20(2004) [PubMed: 14678780] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-39, FUNCTION.
Tissue: Venom and Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF082983 mRNA. Translation: AAD40975.1.
AY027494 Genomic DNA. Translation: AAK15775.1.

3D structure databases

SMRQ9W7J4. Positions 29-145.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9W7J4.

Enzyme and pathway databases

BRENDA3.1.1.4. 274617.

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 namePA21B_PSETE
AccessionPrimary (citable) accession number: Q9W7J4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1999
Last modified: January 19, 2010
This is version 53 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