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Reviewed, UniProtKB/Swiss-Prot P00594 (PA21B_HORSE)

Last modified June 16, 2009. Version 68. 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
    EC=3.1.1.4
Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    Group IB phospholipase A2
Cleaved into the following chain:
    1- Recommended name:
            Phospholipase A2 isoform 2
Gene names
Name: PLA2G1B
OrganismEquus caballus (Horse)
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.

Catalytic activity

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the phospholipase A2 family.

Ontologies

Keywords
   Biological processLipid degradation
   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: 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

Propeptide1 – 77Removed by trypsin Ref.2
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
P00594-1 [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: 849461] [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: 838712] [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: 6349696] [Abstract]
Cited for: SEQUENCE REVISION TO 131-132.

Cross-references

Sequence databases

PIRPSHOA. A90615.

3D structure databases

HSSPHSSP built from PDB template 1HN4 based on UniProtKB P00592.
SMRP00594. Positions 1-126.
ModBaseSearch...

Genome annotation databases

EnsemblENSECAG00000009152. Equus caballus. [Contig view]

Phylogenomic databases

HOVERGENP00594.

Enzyme and pathway databases

BRENDA3.1.1.4. 1464.

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.
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_HORSE
AccessionPrimary (citable) accession number: P00594
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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