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P00594 (PA21B_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. 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:
Phospholipase A2

EC=3.1.1.4
Alternative name(s):
Group IB phospholipase A2
Phosphatidylcholine 2-acylhydrolase 1B

Cleaved into the following chain:

  1. Phospholipase A2 isoform 2
Gene names
Name:PLA2G1B
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

Protein attributes

Sequence length132 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer or homodimer. The inactive pro-form is a homotrimer By similarity.

Subcellular location

Secreted. Note: secreted from pancreatic acinar cells in its inactive form By similarity.

Post-translational modification

Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically By similarity.

Sequence similarities

Belongs to the phospholipase A2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 77Removed by trypsin Ref.1
PRO_0000022737
Chain8 – 132125Phospholipase A2 Ref.2 Ref.3
PRO_0000022738
Chain10 – 132123Phospholipase A2 isoform 2
PRO_0000045893

Sites

Active site551 By similarity
Active site1061 By similarity
Metal binding351Calcium; via carbonyl oxygen By similarity
Metal binding371Calcium; via carbonyl oxygen By similarity
Metal binding391Calcium; via carbonyl oxygen By similarity
Metal binding561Calcium By similarity

Amino acid modifications

Disulfide bond18 ↔ 84 By similarity
Disulfide bond34 ↔ 131 By similarity
Disulfide bond36 ↔ 52 By similarity
Disulfide bond51 ↔ 112 By similarity
Disulfide bond58 ↔ 105 By similarity
Disulfide bond68 ↔ 98 By similarity
Disulfide bond91 ↔ 103 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P00594 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: BC6B809A244052EA

FASTA13214,694
        10         20         30         40         50         60 
ENGISPRAVW QFRSMIQCTI PNSKPYLEFN DYGCYCGLGG SGTPVDELDA CCQVHDNCYT 

        70         80         90        100        110        120 
QAKELSSCRF LVDNPYTESY KFSCSGTEVT CSDKNNACEA FICNCDRNAA ICFSKAPYNP 

       130 
ENKNLDSKRK CA 

« Hide

References

[1]"Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice."
Evenberg A., Meyer H., Verheij H.M., de Haas G.H.
Biochim. Biophys. Acta 491:265-274(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-7.
Tissue: Pancreas.
[2]"Amino acid sequence of phospholipase A2 from horse pancreas."
Evenberg A., Meyer H., Gaastra W., Verheij H.M., de Haas G.H.
J. Biol. Chem. 252:1189-1196(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-132, ACTIVE SITE.
Tissue: Pancreas.
[3]"The complete primary structure of phospholipase A2 from human pancreas."
Verheij H.M., Westerman J., Sternby B., de Haas G.H.
Biochim. Biophys. Acta 747:93-99(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 131-132.

Cross-references

Sequence databases

PIRPSHOA. A90615.

3D structure databases

ProteinModelPortalP00594.
SMRP00594. Positions 3-131.
ModBaseSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000007194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG290764.
HOGENOMHOG000231749.
HOVERGENHBG008137.
InParanoidP00594.
OrthoDBEOG4GHZQJ.

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 namePA21B_HORSE
AccessionPrimary (citable) accession number: P00594
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 1, 2013
This is version 92 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