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P20249 (PA2A_GLOBL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acidic phospholipase A2

Short name=PA2-II
Short name=svPLA2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismGloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi)
Taxonomic identifier242054 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeGloydius

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PLA2 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.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

Is not neurotoxic.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   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: InterPro

phospholipase A2 activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Acidic phospholipase A2
PRO_0000161596

Sites

Active site471
Active site891
Metal binding271Calcium; via carbonyl oxygen
Metal binding291Calcium; via carbonyl oxygen
Metal binding301Calcium; via carbonyl oxygen
Metal binding481Calcium

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
P20249 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 9728BC3E27CC5474

FASTA12213,664
        10         20         30         40         50         60 
SLMQFETLIM KIAGRSGIWY YGSYGCYCGA GGQGRPQDAS DRCCFVHDCC YGKVTGCDPK 

        70         80         90        100        110        120 
LDVYTYTEEN GAIVCGGDDP CKKQICECDK DAAICFRDNI DTYDNKYWFF PAKNCQEESE 


PC 

« Hide

References

[1]"Revised amino acid sequence, crystallization, and preliminary X-ray diffraction analysis of acidic phospholipase A2 from the venom of Agkistrodon halys blomhoffii."
Tomoo K., Ohishi H., Ishida T., Inoue M., Ikeda K., Aoki Y., Samejima Y.
J. Biol. Chem. 264:3636-3638(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Complete amino acid sequence of phospholipase A2-II isolated from Agkistrodon halys blomhoffii venom."
Samejima Y., Iwanaga S., Suzuki T.
FEBS Lett. 47:348-351(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE.
Tissue: Venom.
[3]"Structure of acidic phospholipase A2 for the venom of Agkistrodon halys blomhoffii at 2.8-A resolution."
Tomoo K., Ohishi H., Doi M., Ishida T., Inoue M., Ikeda K., Hata Y., Samejima Y.
Biochem. Biophys. Res. Commun. 184:137-143(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Cross-references

3D structure databases

ProteinModelPortalP20249.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008137.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 1 hit.
PfamPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
PRINTSPR00389. PHPHLIPASEA2.
SMARTSM00085. PA2c. 1 hit.
[Graphical view]
SUPFAMSSF48619. SSF48619. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA2A_GLOBL
AccessionPrimary (citable) accession number: P20249
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 16, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families