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P81478 (PA2A2_TRIGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. 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:
Acidic phospholipase A2 2
Short name=svPLA2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Phospholipase A2 isozyme II
Short name=PLA2-II
OrganismTrimeresurus gramineus (Bamboo pit viper) (Indian green tree viper)
Taxonomic identifier8767 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Trimeresurus

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Snake venom phospholipase A2 (PLA2) that has high lipolytic activity. PLA2 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 By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   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 – 122122Acidic phospholipase A2 2
PRO_0000161702

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 ↔ 115 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 95 By similarity
Disulfide bond49 ↔ 122 By similarity
Disulfide bond50 ↔ 88 By similarity
Disulfide bond57 ↔ 81 By similarity
Disulfide bond75 ↔ 86 By similarity

Sequences

Sequence LengthMass (Da)Tools
P81478 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: F08566FB270855CB

FASTA12213,793
        10         20         30         40         50         60 
NLLQFENMIR NVAGRSGIWW YSDYGCYCGK GGHGRPQDAS DRCCFVHDCC YGKVNGCNPK 

        70         80         90        100        110        120 
KAVYIYSLEN GDIVCGGDDP CRKEVCECDK AAAICFRDNK DTYDNKYWNI PSENCQEESE 


PC

« Hide

References

[1]"Sequence determination and characterization of a phospholipase A2 isozyme from Trimeresurus gramineus (green habu snake) venom."
Fukagawa T., Matsumoto H., Shimohigashi Y., Ogawa T., Oda N., Chang C.-C., Ohno M.
Toxicon 30:1331-1341(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

Sequence databases

PIRA44179.

3D structure databases

ProteinModelPortalP81478.
SMRP81478. Positions 1-122.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008137.

Family and domain databases

Gene3D1.20.90.10. 1 hit.
InterProIPR001211. PLipase_A2.
IPR013090. PLipase_A2_AS.
IPR016090. PLipase_A2_dom.
[Graphical view]
PANTHERPTHR11716. PTHR11716. 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 namePA2A2_TRIGA
AccessionPrimary (citable) accession number: P81478
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: May 1, 2013
This is version 73 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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