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Reviewed, UniProtKB/Swiss-Prot Q90WA7 (PA21B_BUNFA)

Last modified January 19, 2010. Version 48. 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

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Names and origin

Protein namesRecommended name:
    Phospholipase A2 isozyme 1
    EC=3.1.1.4
Alternative name(s):
    Phospholipase A2 isozyme I
    Phosphatidylcholine 2-acylhydrolase
OrganismBungarus fasciatus (Banded krait)
Taxonomic identifier8613 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

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Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides By similarity.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 278 By similarity
PRO_0000022829
Chain28 – 145118Phospholipase A2 isozyme 1
PRO_0000022830

Sites

Active site731 By similarity
Active site1191 By similarity
Metal binding531Calcium; via carbonyl oxygen By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding561Calcium; 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

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Sequences

Sequence LengthMass (Da)Tools
Q90WA7-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4C59AFFBDDD802CC

FASTA14515,853
        10         20         30         40         50         60 
MNPAHLLVLL AVCVSLLGAA NIPPQPLNLL QFKNMIQCAG SRLWVAYVKY GCYCGPGGTG 

        70         80         90        100        110        120 
TPLDQLDRCC QTHDHCYDNA KKFGNCIPYF KTYEYTCNKP DLTCTDAKGS CARNVCDCDR 

       130        140 
AAAICFAAAP YNLANFGINK ETHCQ

« Hide

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References

[1]"cDNA cloning and characterization of phospholipase A2 from the snake Bungarus fasciatus."
Zha H., Zhang Y.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF387595 mRNA. Translation: AAK62362.1.

3D structure databases

SMRQ90WA7. Positions 28-145.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ90WA7.

Enzyme and pathway databases

BRENDA3.1.1.4. 97947.

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...

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Entry information

Entry namePA21B_BUNFA
AccessionPrimary (citable) accession number: Q90WA7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: December 1, 2001
Last modified: January 19, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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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