Reviewed, UniProtKB/Swiss-Prot P20476 (PA21B_TRIGA)

Names and origin

Protein names

Recommended name:
    Phospholipase A2 isozyme 1
    EC=3.1.1.4
Alternative name(s):
    Phospholipase A2 isozyme I
      Short name=PLA2-I
    Phosphatidylcholine 2-acylhydrolase

Gene names

Name:

PLA1

Organism

Trimeresurus gramineus (Indian green tree viper) (Green habu snake)

Taxonomic identifier

8767 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Trimeresurus

Protein attributes

Sequence length	138 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. Has high lipolytic activity.
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. Group II subfamily.

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 – 16	16	Ref.2 Ref.3
	Chain	17 – 138	122	Phospholipase A2 isozyme 1		PRO_0000022959
Sites
	Active site	63	1	By similarity
	Active site	105	1	By similarity
	Metal binding	43	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	45	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	47	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	64	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	42 ↔ 131		By similarity
	Disulfide bond	44 ↔ 60		By similarity
	Disulfide bond	59 ↔ 111		By similarity
	Disulfide bond	65 ↔ 138		By similarity
	Disulfide bond	66 ↔ 104		By similarity
	Disulfide bond	73 ↔ 97		By similarity
	Disulfide bond	91 ↔ 102		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20476-1 [UniParc]. Last modified December 15, 1998. Version 3. Checksum: 1D1EF551CCB155ED	FASTA	138	15,519
	10 20 30 40 50 60 MRTLWIMAVL LVGVEGHLMQ FETLIMKVAG RSGVWYYGSY GCFCGAGGQG RPQDASDRCC 70 80 90 100 110 120 FVHDCCYGKV NGCDPKKDFY TYSEENGAIV CGGDDPCKKE ICECDKDAAI CFRDNKDTYD 130 NKYWFFPAKN CQEESEPC

References

[1]	"Accelerated evolution in the protein-coding regions is universal in crotalinae snake venom gland phospholipase A2 isozyme genes." Nakashima K., Nobuhisa I., Deshimaru M., Nakai M., Ogawa T., Shimohigashi Y., Fukumaki Y., Hattori M., Sakaki Y., Hattori S., Ohno M. Proc. Natl. Acad. Sci. U.S.A. 92:5605-5609(1995) [PubMed: 7777556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Venom gland.
[2]	"Amino acid sequence of a phospholipase A2 from the venom of Trimeresurus gramineus (green habu snake)." Oda N., Nakamura H., Sakamoto S., Liu S.-Y., Kihara H., Chang C.-C., Ohno M. Toxicon 29:157-166(1991) [PubMed: 2048135] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-138. Tissue: Venom.
[3]	"Purification and characterization of phospholipase A2 from Trimeresurus gramineus venom." Oda N., Sakai H., Shieh T.C., Nakamura H., Sakamoto S., Kihara H., Chang C.-C., Ohno M. J. Biochem. 102:1441-1449(1987) [PubMed: 3448089] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-54. Tissue: Venom.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D31774 mRNA. Translation: BAA06552.1. Different initiation. D31780 Genomic DNA. Translation: BAA06558.1.
PIR	A39557.
3D structure databases
SMR	P20476. Positions 18-138.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P20476.
Enzyme and pathway databases
BRENDA	3.1.1.4. 96085.
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_TRIGA

Accession

Primary (citable) accession number: P20476
Secondary accession number(s): P87480, P87481

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	December 15, 1998
Last modified:	November 24, 2009
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)