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Reviewed, UniProtKB/Swiss-Prot P04417 (PA21B_AGKHA)

Last modified June 16, 2009. Version 76. 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, basic
      Short name=PA2-I
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismAgkistrodon halys blomhoffi (Mamushi) (Gloydius blomhoffii)
Taxonomic identifier242054 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeGloydius

Protein attributes

Sequence length122 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.

Subunit structure

In contrast to the pancreatic enzymes, the molecules of venom phospholipases A2 are dimers of identical chains; the monomers appear to be inactive.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group II 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 – 122122Phospholipase A2, basic
PRO_0000161595

Sites

Active site471 By similarity
Active site891 By similarity
Metal binding271Calcium; via carbonyl oxygen By similarity
Metal binding291Calcium; via carbonyl oxygen By similarity
Metal binding311Calcium; via carbonyl oxygen By similarity
Metal binding481Calcium By similarity

Amino acid modifications

Disulfide bond26 ↔ 115 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 95 By similarity
Disulfide bond49 ↔ 122 By similarity
Disulfide bond50 ↔ 88 By similarity
Disulfide bond57 ↔ 81 By similarity
Disulfide bond75 ↔ 86 By similarity

Experimental info

Sequence uncertainty741

Sequences

Sequence LengthMass (Da)Tools
P04417-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: EA2C5EE5EEF44488

FASTA12213,982
        10         20         30         40         50         60 
HLLQFRKMIK KMTGKEPVIS YAFYGCYCGS GGRGKPKDAT DRCCFVHDCC YEKVTGCKPK 

        70         80         90        100        110        120 
WDDYTYSWKN GDIVCGGDDP CKKEICECDR AAAICFRDNL KTYKKRYMAY PDILCSSKSE 


KC 

« Hide

References

[1]"Amino acid sequence of a basic Agkistrodon halys blomhoffii phospholipase A2. Possible role of NH2-terminal lysines in action on phospholipids of Escherichia coli."
Forst S., Weiss J., Blackburn P., Frangione B., Goni F., Elsbach P.
Biochemistry 25:4309-4314(1986) [PubMed: 3530322] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

Sequence databases

PIRPSABA. A00766.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP04417.

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 namePA21B_AGKHA
AccessionPrimary (citable) accession number: P04417
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 76 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