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P00606 (PA20_BUNMU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospholipase A2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismBungarus multicinctus (Many-banded krait)
Taxonomic identifier8616 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length145 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.

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
   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 278
PRO_0000022833
Chain28 – 145118Phospholipase A2
PRO_0000022834

Sites

Active site731 By similarity
Active site1191 By similarity
Metal binding531Calcium; via carbonyl oxygen By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding571Calcium; via carbonyl oxygen By similarity
Metal binding741Calcium By similarity

Amino acid modifications

Disulfide bond38 ↔ 97 By similarity
Disulfide bond52 ↔ 144 By similarity
Disulfide bond54 ↔ 70 By similarity
Disulfide bond69 ↔ 125 By similarity
Disulfide bond76 ↔ 118 By similarity
Disulfide bond86 ↔ 111 By similarity
Disulfide bond104 ↔ 116 By similarity

Sequences

Sequence LengthMass (Da)Tools
P00606 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: F7959376589967CA

FASTA14515,593
        10         20         30         40         50         60 
MNPAHLLILS AVCVSLLGAA NVPPQHLNLY QFKNMIVCAG TRPWIGYVNY GCYCGAGGSG 

        70         80         90        100        110        120 
TPVDELDRCC YVHDNCYGEA EKIPGCNPKT KTYSYTCTKP NLTCTDAAGT CARIVCDCDR 

       130        140 
TAAICFAAAP YNINNFMISS STHCQ

« Hide

References

[1]"Nucleotide sequence encoding for non-toxic phospholipase-A2 from Bungarus multicinctus."
Danse J.-M.
Nucleic Acids Res. 18:4608-4608(1990) [PubMed: 2388841] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Amino acid sequence of phospholipase A from Bungarus multicinctus venom."
Kondo K., Toda H., Narita K.
J. Biochem. 89:37-47(1981) [PubMed: 7217037] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-145.
Tissue: Venom.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X53406 mRNA. Translation: CAA37482.1.
PIRPSKF2U. S10981.

3D structure databases

ProteinModelPortalP00606.
SMRP00606. Positions 28-145.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008137.

Family and domain databases

InterProIPR016090. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR001211. PLipase_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]
SUPFAMSSF48619. PhospholipaseA2. 1 hit.
PROSITEPS00119. PA2_ASP. 1 hit.
PS00118. PA2_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePA20_BUNMU
AccessionPrimary (citable) accession number: P00606
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: October 19, 2011
This is version 82 of the entry and version 2 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

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