Skip Header

Contribute Send feedback
Read comments (?) or add your own

P07037 (PA2A2_ASPSC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acidic phospholipase A2 CM-II
Short name=svPLA2
EC=3.1.1.4
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismAspidelaps scutatus (Shield-nose snake)
Taxonomic identifier8607 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Aspidelaps

Protein attributes

Sequence length119 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides By similarity.

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 I 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 – 119119Acidic phospholipase A2 CM-II
PRO_0000161607

Sites

Active site471 By similarity
Active site931 By similarity
Metal binding271Calcium; via carbonyl oxygen
Metal binding291Calcium; via carbonyl oxygen
Metal binding311Calcium; via carbonyl oxygen
Metal binding481Calcium By similarity

Amino acid modifications

Disulfide bond11 ↔ 71 By similarity
Disulfide bond26 ↔ 118 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond43 ↔ 99 By similarity
Disulfide bond50 ↔ 92 By similarity
Disulfide bond60 ↔ 85 By similarity
Disulfide bond78 ↔ 90 By similarity

Sequences

Sequence LengthMass (Da)Tools
P07037 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 149F380DED335991

FASTA11913,388
        10         20         30         40         50         60 
NLYQFKNMIQ CTVPNRSWWH FADYGCFCGY GGSGTPVDEL DRCCQTHDNC YSEAEKLSGC 

        70         80         90        100        110 
KPYIKTYSYD CSQGKLTCSG NDDKCAAFVC NCDRVAAICF AGAPYIDDNY NVDLNERCQ

« Hide

References

[1]"Purification, some properties of two phospholipases A2 (CM-I and CM-II) and the amino-acid sequence of CM-II from Aspidelaps scutatus (shield or shield-nose) venom."
Joubert F.J.
Biol. Chem. Hoppe-Seyler 368:1597-1602(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

Sequence databases

PIRS00227.

3D structure databases

ProteinModelPortalP07037.
SMRP07037. Positions 1-119.
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_ASPSC
AccessionPrimary (citable) accession number: P07037
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 1, 2013
This is version 82 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents