P00594 (PA21B_HORSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Equus caballus (Horse) [Reference proteome]

Taxonomic identifier

9796 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › Equus

Protein attributes

Sequence length	132 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Autocatalytic cleavage Disulfide bond Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phospholipase A2 activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 7	7	Removed by trypsin Ref.1		PRO_0000022737
	Chain	8 – 132	125	Phospholipase A2 Ref.2 Ref.3		PRO_0000022738
	Chain	10 – 132	123	Phospholipase A2 isoform 2		PRO_0000045893
Sites
	Active site	55	1	By similarity
	Active site	106	1	By similarity
	Metal binding	35	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	37	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	39	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	56	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	18 ↔ 84		By similarity
	Disulfide bond	34 ↔ 131		By similarity
	Disulfide bond	36 ↔ 52		By similarity
	Disulfide bond	51 ↔ 112		By similarity
	Disulfide bond	58 ↔ 105		By similarity
	Disulfide bond	68 ↔ 98		By similarity
	Disulfide bond	91 ↔ 103		By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P00594 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: BC6B809A244052EA	FASTA	132	14,694
	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

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
PIR	PSHOA. A90615.
3D structure databases
ProteinModelPortal	P00594.
SMR	P00594. Positions 3-131.
ModBase	Search...
Protein-protein interaction databases
STRING	9796.ENSECAP00000007194.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG290764.
HOGENOM	HOG000231749.
HOVERGEN	HBG008137.
InParanoid	P00594.
OrthoDB	EOG4GHZQJ.
Family and domain databases
Gene3D	1.20.90.10. 1 hit.
InterPro	IPR001211. PLipase_A2. IPR013090. PLipase_A2_AS. IPR016090. PLipase_A2_dom. [Graphical view]
PANTHER	PTHR11716. PTHR11716. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PRINTS	PR00389. PHPHLIPASEA2.
SMART	SM00085. PA2c. 1 hit. [Graphical view]
SUPFAM	SSF48619. PhospholipaseA2. 1 hit.
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21B_HORSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program