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Q7T2Q4 (PA22_BUNFL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 41. 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 A2-2
EC=3.1.1.4
Alternative name(s):
PA2-II
Phosphatidylcholine 2-acylhydrolase
OrganismBungarus flaviceps flaviceps (Red-headed krait)
Taxonomic identifier8615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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
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 By similarity
PRO_0000271458
Chain28 – 147120Phospholipase A2-2
PRO_5000050836

Sites

Active site751 By similarity
Active site1211 By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding571Calcium; via carbonyl oxygen By similarity
Metal binding591Calcium; via carbonyl oxygen By similarity
Metal binding761Calcium By similarity

Amino acid modifications

Disulfide bond38 ↔ 99 By similarity
Disulfide bond54 ↔ 146 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 127 By similarity
Disulfide bond78 ↔ 120 By similarity
Disulfide bond88 ↔ 113 By similarity
Disulfide bond106 ↔ 118 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7T2Q4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 2A705D44885EDDDC

FASTA14715,875
        10         20         30         40         50         60 
MNPAHLLVLS AVCVSLLGAA IVPPQPLNLI QFSSLIQCAN GGSRATWHYA DYGCYCGKGG 

        70         80         90        100        110        120 
GGTPVDELDR CCQTHDNCYG EAEKLTKCSP YYKTYKYDCS EGKLTCNDAP GSCERSVCDC 

       130        140 
DRVAAICFAG APYNDKNFMI NTETNCQ

« Hide

References

[1]"Molecular cloning of the major lethal toxins from two kraits (Bungarus flaviceps and Bungarus candidus)."
Yanoshita R., Ogawa Y., Murayama N., Omori-Satoh T., Saguchi K., Higuchi S., Khow O., Chanhome L., Samejima Y., Sitprija V.
Toxicon 47:416-424(2006) [PubMed: 16458338] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB112360 mRNA. Translation: BAC77656.1.

3D structure databases

HSSPHSSP built from PDB template 1M8T based on UniProtKB Q9DF33.
ProteinModelPortalQ7T2Q4.
SMRQ7T2Q4. Positions 28-147.
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 namePA22_BUNFL
AccessionPrimary (citable) accession number: Q7T2Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2003
Last modified: October 19, 2011
This is version 41 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

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