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P81243 (PA21B_BOTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 65. 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):
BJ-PLA2
Phosphatidylcholine 2-acylhydrolase
OrganismBothrops jararaca (Jararaca)
Taxonomic identifier8724 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits collagen- and ADP-induced platelet aggregation.

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 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: InterPro

phospholipase A2 activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 124124Phospholipase A2
PRO_0000161621

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 ↔ 117 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 97 By similarity
Disulfide bond49 ↔ 124 By similarity
Disulfide bond50 ↔ 90 By similarity
Disulfide bond57 ↔ 83 By similarity
Disulfide bond77 ↔ 88 By similarity

Sequences

Sequence LengthMass (Da)Tools
P81243 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: 5A4E33EE7745E3EA

FASTA12414,304
        10         20         30         40         50         60 
DLWQFGQMMN DVMREYVVFN YLYYGCYCGW GGIGKPRDAT DRCCFVHDCC YGKVTGCNPK 

        70         80         90        100        110        120 
TDSYTYTYSE ENGDVVCGGD DLCKKQICEC DRVAATCFRD NKDTYDTKYW LYGAKNCQEE 


SEPC

« Hide

References

[1]"A novel phospholipase A2, BJ-PLA2, from the venom of the snake Bothrops jararaca: purification, primary structure analysis, and its characterization as a platelet-aggregation-inhibiting factor."
Serrano S.M.T., Reichl A.P., Mentele R., Auerswald E.A., Santoro M.L., Sampaio C.A.M., Camargo A.C.M., Assakura M.T.
Arch. Biochem. Biophys. 367:26-32(1999) [PubMed: 10375395] [Abstract]
Cited for: PROTEIN SEQUENCE, CHARACTERIZATION.
Tissue: Venom.
+Additional computationally mapped references.

Cross-references

3D structure databases

ProteinModelPortalP81243.
SMRP81243. Positions 2-124.
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 namePA21B_BOTJA
AccessionPrimary (citable) accession number: P81243
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: October 19, 2011
This is version 65 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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