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Reviewed, UniProtKB/Swiss-Prot P19000 (PA21B_LATLA)

Last modified June 16, 2009. Version 63. 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

Names and origin

Protein namesRecommended name:
    Phospholipase A2 P'513
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
OrganismLaticauda laticaudata (Blue-ringed sea krait)
Taxonomic identifier8630 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaElapidaeLaticaudinaeLaticauda

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

PA2 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 per subunit By similarity.

Subunit structure

In contrast to the pancreatic enzymes, the molecules of venom phospholipases A2 are dimers of identical chains; the monomers appear to be inactive.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the phospholipase A2 family. Group I subfamily.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 276
PRO_0000022886
Chain28 – 145118Phospholipase A2 P'513
PRO_0000022887

Sites

Active site751 By similarity
Active site1191 By similarity
Metal binding551Calcium; via carbonyl oxygen By similarity
Metal binding571Calcium; via carbonyl oxygen By similarity
Metal binding591Calcium; via carbonyl oxygen By similarity
Metal binding761Calcium By similarity

Amino acid modifications

Disulfide bond38 ↔ 98 By similarity
Disulfide bond54 ↔ 144 By similarity
Disulfide bond56 ↔ 72 By similarity
Disulfide bond71 ↔ 125 By similarity
Disulfide bond78 ↔ 118 By similarity
Disulfide bond87 ↔ 111 By similarity
Disulfide bond105 ↔ 116 By similarity

Sequences

Sequence LengthMass (Da)Tools
P19000-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: C6C2A9B4EE653630

FASTA14516,242
        10         20         30         40         50         60 
MYPAHLLLLL AVCVSLLGAS AIPPLPLNLA QFALVIKCAD KGKRPRWHYM DYGCYCGPGG 

        70         80         90        100        110        120 
SGTPVDELDR CCKTHDQCYA QAEKKGCYPK LTMYSYYCGG DGPYCNSKTE CQRFVCDCDV 

       130        140 
RAADCFARYP YNNKNYNINT SKRCK 

« Hide

References

[1]"Sequence of a cDNA encoding a snake venom phospholipase A2."
Guignery Frelat G., Ducancel F., Menez A., Boulain J.-C.
Nucleic Acids Res. 15:5892-5892(1987) [PubMed: 3615209] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.

Cross-references

Sequence databases

Y00377 mRNA. Translation: CAA68449.1.
PIRA27099.

3D structure databases

HSSPHSSP built from PDB template 1AE7 based on UniProtKB P00608.
SMRP19000. Positions 28-145.
ModBaseSearch...

Phylogenomic databases

HOVERGENP19000.

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.
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...

Entry information

Entry namePA21B_LATLA
AccessionPrimary (citable) accession number: P19000
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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