Reviewed, UniProtKB/Swiss-Prot P00611 (PA21B_LATSE)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme 1     EC=3.1.1.4 Alternative name(s):     Phospholipase A2 isozyme I     Phosphatidylcholine 2-acylhydrolase     GL5-1
Organism	Laticauda semifasciata (Broad-banded blue sea snake) (Erabu sea snake)
Taxonomic identifier	8631 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Laticaudinae › Laticauda

Protein attributes

Sequence length	145 AA.
Sequence status	Complete.
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.
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.
Sequence similarities	Belongs to the phospholipase A2 family.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
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: UniProtKB-KW 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
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 27	6			PRO_0000022896
	Chain	28 – 145	118	Phospholipase A2 isozyme 1		PRO_0000022897
Sites
	Active site	75	1	By similarity
	Active site	119	1	By similarity
	Metal binding	55	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	57	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	59	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	76	1	Calcium By similarity
	Site	91	1	Specific activity reduced 20-fold by modification
Amino acid modifications
	Disulfide bond	38 ↔ 98		By similarity
	Disulfide bond	54 ↔ 144		By similarity
	Disulfide bond	56 ↔ 72		By similarity
	Disulfide bond	71 ↔ 125		By similarity
	Disulfide bond	78 ↔ 118		By similarity
	Disulfide bond	87 ↔ 111		By similarity
	Disulfide bond	105 ↔ 116		By similarity
Experimental info
	Sequence conflict	39 – 40	2	VN → NV AA sequence Ref.2
	Sequence conflict	77	1	D → N AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P00611-1 [UniParc]. Last modified November 1, 2002. Version 3. Checksum: 1F84DF6F7BC5348F	FASTA	145	15,900
	10 20 30 40 50 60 MYPAHLLVLL AVCVSLLGAT AIPPLPLNLV QFSNLIQCVN KGSRASYHYA DYGCYCGAGG 70 80 90 100 110 120 SGTPVDELDR CCKIHDDCYG EAEKMGCYPK WTLYTYDCST EEPNCSTKTG CQGFVCACDL 130 140 EAAKCFARSP YNNKNYNIDT SKRCK

References

[1]	"A comparative analysis of invaded sequences from group IA phospholipase A(2) genes provides evidence about the divergence period of genes groups and snake families." Fujimi T.J., Tsuchiya T., Tamiya T. Toxicon 40:873-884(2002) [PubMed: 12076640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[2]	"Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata." Nishida S., Kim H.S., Tamiya N. Biochem. J. 207:589-594(1982) [PubMed: 7165712] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-145. Tissue: Venom.
[3]	"Correction of amino acid sequence of phospholipase A2 I from the venom of Laticauda semifasciata (Erabu sea snake)." Takasaki C., Kuramochi H., Shimazu T., Tamiya N. Toxicon 26:747-749(1988) [PubMed: 3188064] [Abstract] Cited for: SEQUENCE REVISION TO 97-107.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB062440 Genomic DNA. Translation: BAB72247.1.
PIR	PSLT1E. A94325.
3D structure databases
SMR	P00611. Positions 28-145.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00611.
Enzyme and pathway databases
BRENDA	3.1.1.4. 96002.
Family and domain databases
InterPro	IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. IPR001211. Phospholipase_A2_euk. [Graphical view]
Gene3D	G3DSA:1.20.90.10. Phospholipase_A2. 1 hit.
PANTHER	PTHR11716. Phospholipase_A2. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
PRINTS	PR00389. PHPHLIPASEA2.
SMART	SM00085. PA2c. 1 hit. [Graphical view]
PROSITE	PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PA21B_LATSE

Accession

Primary (citable) accession number: P00611
Secondary accession number(s): Q9I848

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 2002
Last modified:	January 19, 2010
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)