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Reviewed, UniProtKB/Swiss-Prot P81243 (PA21B_BOTJA)

Last modified June 16, 2009. Version 57. 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
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    BJ-PLA2
OrganismBothrops jararaca (Jararaca)
Taxonomic identifier8724 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

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Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

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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: 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

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

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Sequences

Sequence LengthMass (Da)Tools
P81243-1 [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

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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.

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Cross-references

3D structure databases

HSSPHSSP built from PDB template 1BK9 based on UniProtKB P14418.
SMRP81243. Positions 2-124.
ModBaseSearch...

Phylogenomic databases

HOVERGENP81243.

Enzyme and pathway databases

BRENDA3.1.1.4. 19086.

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.
ProDomPD000303. PhospholipaseA2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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_BOTJA
AccessionPrimary (citable) accession number: P81243
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: June 16, 2009
This is version 57 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