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Reviewed, UniProtKB/Swiss-Prot P0C8M1 (PA21_BOTMO)

Last modified June 16, 2009. Version 5. 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 BmTX-I
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismBothrops moojeni (Lance-headed viper) (Caissaca)
Taxonomic identifier98334 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

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Protein attributes

Sequence length121 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. Shows PA2 activity in the presence of a synthetic substrate. In vitro, blocks the neuromuscular transmission in young chick biventer cervicis preparations. In mice, induces myonecrosis and a systemic interleukin-6 response upon intramuscular injection. Also induces edema and exerts a strong proinflammatory effect. Ref.1

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit. Ref.1

Enzyme regulation

Inhibited by magnesium, cadmium and manganese ions. Also inhibited by crotapotin. Ref.1

Subcellular location

Secreted. Ref.1

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 35-45 degrees Celsius.

Mass spectrometry

Molecular mass is 14238.71 Da from positions 1 - 121. Determined by MALDI. Ref.1

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Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Myotoxin
Neurotoxin
Toxin
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

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 – 121121Phospholipase A2 BmTX-I
PRO_0000359436

Sites

Active site481 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 binding491Calcium By similarity

Amino acid modifications

Disulfide bond26 ↔ 114 By similarity
Disulfide bond28 ↔ 45 By similarity
Disulfide bond44 ↔ 95 By similarity
Disulfide bond50 ↔ 121 By similarity
Disulfide bond51 ↔ 88 By similarity
Disulfide bond58 ↔ 82 By similarity
Disulfide bond76 ↔ 86 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P0C8M1-1 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: 4441455A8D14F766

FASTA12114,081
        10         20         30         40         50         60 
DLWQFNKMIK KEVGKLPFPF YGAYGCYCGW GGRGEKPKDG TDRCCFVHDC CYKKLTGCPK 

        70         80         90        100        110        120 
WDDRYSYSWK DITIVCGEDL PCEEICECDR AAAVCFYENL GTYNKKYMKH LKPCKKADYP 


C

« Hide

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References

[1]"Biological and biochemical characterization of new basic phospholipase A(2) BmTX-I isolated from Bothrops moojeni snake venom."
Calgarotto A.K., Damico D.C.S., Ponce-Soto L.A., Baldasso P.A., Da Silva S.L., Souza G.H.M.F., Eberlin M.N., Marangoni S.
Toxicon 51:1509-1519(2008) [PubMed: 18501940] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
Tissue: Venom.

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Cross-references

3D structure databases

ModBaseSearch...

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 namePA21_BOTMO
AccessionPrimary (citable) accession number: P0C8M1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: June 16, 2009
This is version 5 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

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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