P16354 (PA23_HELSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phospholipase A2 isozymes PA3A/PA3B/PA5 Short name=PLA2 EC=3.1.1.4 Alternative name(s): Phosphatidylcholine 2-acylhydrolase
Organism	Heloderma suspectum (Gila monster)
Taxonomic identifier	8554 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Anguimorpha › Helodermatidae › Heloderma

Protein attributes

Sequence length	143 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PLA2 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.
Tissue specificity	Expressed by the venom gland.
Miscellaneous	The sequence of isozyme pa3b is shown.
Sequence similarities	Belongs to the phospholipase A2 family. Group III subfamily.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
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
	Chain	1 – 143	143	Phospholipase A2 isozymes PA3A/PA3B/PA5		PRO_0000161648
Sites
	Active site	36	1	By similarity
	Metal binding	10	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	12	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	14	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	37	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	11 ↔ 33		By similarity
	Disulfide bond	32 ↔ 72		By similarity
	Disulfide bond	39 ↔ 65		By similarity
Natural variations
	Natural variant	142 – 143	2	Missing in isozyme PA3A.
	Natural variant	143	1	Missing in isozyme PA5.

Sequences

	Sequence		Length	Mass (Da)
	P16354 [UniParc]. Last modified November 1, 1995. Version 3. Checksum: 75A3FFA0FA1CC9A7	FASTA	143	16,048
	10 20 30 40 50 60 GAFIMPGTLW CGAGNAASDY SQLGTEKDTD MCCRDHDHCE NWISALEYKH GMRNYYPSTI 70 80 90 100 110 120 SHCDCDNQFR SCLMKLKDGT ADYVGQTYFN VLKIPCFELE EGEGCVDWNF WLECTESKIM 130 140 PVAKLVSAAP YQAQAETQSG EGR

References

[1]

"Differences in primary structure among five phospholipases A2 from Heloderma suspectum." Vandermeers A., Vandermeers-Piret M.-C., Vigneron L., Rathe J., Stievenart M., Christophe J. Eur. J. Biochem. 196:537-544(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

[2]

"Purification and characterization of five variants of phospholipase A2 and complete primary structure of the main phospholipase A2 variant in Heloderma suspectum (Gila monster) venom." Gomez F., Vandermeers A., Vandermeers-Piret M.-C., Herzog R., Rathe J., Stievenart M., Winand J., Christophe J. Eur. J. Biochem. 186:23-33(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

Sequence databases
PIR	PSGHA5. S14764.
3D structure databases
ProteinModelPortal	P16354.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG008138.
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	PTHR12253. PTHR12253. 1 hit.
Pfam	PF05826. Phospholip_A2_2. 1 hit. [Graphical view]
SMART	SM00085. PA2c. 1 hit. [Graphical view]
SUPFAM	SSF48619. PhospholipaseA2. 1 hit.
PROSITE	PS00119. PA2_ASP. False negative. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA23_HELSU

Accession

Primary (citable) accession number: P16354
Secondary accession number(s): P80004, P80005

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program