Annotations: 5IZ5

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth B]	PF00168	e5iz5B2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: C2 domain (From Topology)	T: C2 domain	F: PF00168	ECOD (1.6)
A [auth B]	PF18695	e5iz5B3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: C2 domain (From Topology)	T: C2 domain	F: PF18695	ECOD (1.6)
A [auth B]	PF01735	e5iz5B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF01735	ECOD (1.6)
B [auth A]	PF00168	e5iz5A2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: C2 domain (From Topology)	T: C2 domain	F: PF00168	ECOD (1.6)
B [auth A]	PF18695	e5iz5A3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: C2 domain (From Topology)	T: C2 domain	F: PF18695	ECOD (1.6)
B [auth A]	PF01735	e5iz5A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF01735	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	PF18695	Cytosolic phospholipases A2 C2-domain (cPLA2_C2)	Cytosolic phospholipases A2 C2-domain	Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. ...	Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. Structural information of full length cPLA2alpha apo form, shows that it is composed of two domains; an N-terminal Ca2 + binding C2 domain and a C-terminal alpha/beta hydrolase core. This entry describes the N-terminal Ca2+ binding C2 domain which is composed of an eight-stranded antiparallel beta-sandwich consisting of two four-stranded beta-sheets. C2 domains are present in many lipid-binding proteins including Copines, CAPRI and Rabphilin-3A all of which are involved in membrane trafficking [1].	Domain
A [auth B], B [auth A]	PF00168	C2 domain (C2)	C2 domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	Cytosolic phospholipase A2 delta	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding calcium-dependent phospholipid binding phospholipid binding lipid binding phospholipase A2 activity calcium-dependent phospholipase A2 activity hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity hydrolase activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding calcium-dependent phospholipid binding phospholipid binding lipid binding phospholipase A2 activity calcium-dependent phospholipase A2 activity hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity hydrolase activity catalytic activity phospholipase activity lipase activity phospholipase A1 activity	fatty acid metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process organic substance metabolic process cellular lipid metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process phosphatidylglycerol metabolic process fatty acid metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process organic substance metabolic process cellular lipid metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process phosphatidylglycerol metabolic process glycerophospholipid metabolic process phospholipid metabolic process organophosphate metabolic process phosphate-containing compound metabolic process glycerolipid metabolic process phosphorus metabolic process phosphatidylglycerol acyl-chain remodeling phosphatidylinositol metabolic process phosphatidylinositol acyl-chain remodeling lipid catabolic process catabolic process phospholipid catabolic process glycerolipid catabolic process organophosphate catabolic process cellular lipid catabolic process cellular catabolic process glycerophospholipid catabolic process organic substance catabolic process	membrane cellular anatomical entity intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
A [auth B], B [auth A]	IPR002642	Lysophospholipase, catalytic domain	Domain
A [auth B], B [auth A]	IPR040723	Cytosolic phospholipases A2, C2-domain	Domain
A [auth B], B [auth A]	IPR041847	Cytosolic phospholipase A2, C2 domain	Domain
A [auth B], B [auth A]	IPR000008	C2 domain	Domain
A [auth B], B [auth A]	IPR035892	C2 domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth B], B [auth A]	Pharos: Q86XP0	psoriasis schizophrenia

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A [auth B], B [auth A]	OPM	Monotopic/peripheral	Alpha/Beta monotopic/peripheral	FabD/lysophospholipase-like	Lysophospholipase catalytic domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.