Reviewed, UniProtKB/Swiss-Prot P06859 (PA21B_TRIFL)

Names and origin

Protein names	Recommended name:     Phospholipase A2 isozyme 1     EC=3.1.1.4 Alternative name(s):     Phospholipase A2 isozyme I     pgPLA 1a/pgPLA 2a     Phosphatidylcholine 2-acylhydrolase
Organism	Trimeresurus flavoviridis (Habu) (Protobothrops flavoviridis)
Taxonomic identifier	88087 [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.
Catalytic activity	Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Homodimer.
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
Coding sequence diversity	Polymorphism
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.6 Ref.7
	Chain	17 – 138	122	Phospholipase A2 isozyme 1		PRO_0000022952
Sites
	Active site	63	1	Ref.8
	Active site	104	1	Ref.8
	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 ↔ 110		By similarity
	Disulfide bond	65 ↔ 138		By similarity
	Disulfide bond	66 ↔ 103		By similarity
	Disulfide bond	73 ↔ 97		By similarity
	Disulfide bond	91 ↔ 101		By similarity
Natural variations
	Natural variant	15	1	D → E
	Natural variant	53	1	K → T in isozyme [Thr37]PLA2.
Experimental info
	Sequence conflict	85 – 88	4	NNGD → QGN AA sequence Ref.6
	Sequence conflict	92	1	E → G AA sequence Ref.6
	Sequence conflict	95 – 97	3	GPC → DPCD AA sequence Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P06859-1 [UniParc]. Last modified August 1, 1991. Version 2. Checksum: FF24B8253FEA1A1A	FASTA	138	15,535
	10 20 30 40 50 60 MRTLWIMAVL LVGVDGGLWQ FENMIIKVVK KSGILSYSAY GCYCGWGGRG KPKDATDRCC 70 80 90 100 110 120 FVHDCCYGKV TGCNPKLGKY TYSWNNGDIV CEGDGPCKEV CECDRAAAIC FRDNLDTYDR 130 NKYWRYPASN CQEDSEPC

References

[1]	"Cloning and sequence analysis of cDNA for Trimeresurus flavoviridis phospholipase A2, and consequent revision of the amino acid sequence." Oda N., Ogawa T., Ohno M., Sasaki H., Sakaki Y., Kihara H. J. Biochem. 108:816-821(1990) [PubMed: 1707052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Unusually high conservation of untranslated sequences in cDNAs for Trimeresurus flavoviridis phospholipase A2 isozymes." Ogawa T., Oda N., Nakashima K., Sasaki H., Hattori M., Sakaki Y., Kihara H., Ohno M. Proc. Natl. Acad. Sci. U.S.A. 89:8557-8561(1992) [PubMed: 1528861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME [THR37]PLA2). Tissue: Venom gland.
[3]	"Accelerated evolution of Trimeresurus flavoviridis venom gland phospholipase A2 isozymes." Nakashima K., Ogawa T., Oda N., Hattori M., Sakaki Y., Kihara H., Ohno M. Proc. Natl. Acad. Sci. U.S.A. 90:5964-5968(1993) [PubMed: 8327468] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[4]	"Polymorphisms of Trimeresurus flavoviridis venom gland phospholipase A2 isozyme genes." Nakashima K., Nobuhisa I., Ogawa T., Hattori M., Sakaki Y., Kihara H., Ohno M. Biosci. Biotechnol. Biochem. 58:1510-1511(1994) [PubMed: 7765285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[5]	"Regional evolution of Trimeresurus flavoviridis venom-gland phospholipase A2 isoenzymes." Chijiwa T., Yamaguchi Y., Ogawa T., Deshimaru M., Nobuhisa I., Nakashima K., Oda-Ueda N., Shimohigashi Y., Fukumaki Y., Hattori S., Ohno M. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Amami-Oshima and Okinawa.
[6]	"Amino acid sequence of Trimeresurus flavoviridis phospholipase A2." Tanaka S., Mohri N., Kihara H., Ohno M. J. Biochem. 99:281-289(1986) [PubMed: 3514593] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-138. Tissue: Venom.
[7]	"Comparison of amino terminal region of three isoenzymes of phospholipases A2 (TFV PL-Ia, TFV PL-Ib, TFV PL-X) from Trimeresurus flavoviridis (habu snake) venom and the complete amino acid sequence of the basic phospholipase, TFV PL-X." Kini R.M., Kawabata S., Iwanaga S. Toxicon 24:1117-1129(1986) [PubMed: 3564060] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-47. Tissue: Venom.
[8]	"Investigation of an active site histidine-aspartate couple in Trimeresurus flavoviridis phospholipase A2." Kohzuma T., Oda N., Kihara H., Ohno M. J. Biochem. 106:1054-1058(1989) [PubMed: 2628422] [Abstract] Cited for: ACTIVE SITES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D10070 mRNA. Translation: BAA00962.1. D10720 mRNA. Translation: BAA01563.1. D10722 Genomic DNA. Translation: BAA01565.1. D10724 Genomic DNA. Translation: BAA01567.1. AB072174 mRNA. Translation: BAB68547.1. AB072175 mRNA. Translation: BAB68548.1.
PIR	A46169. A48188. PSTVIF. B48188.
3D structure databases
HSSP	HSSP built from PDB template 1VAP based on UniProtKB P51972.
SMR	P06859. Positions 18-138.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P06859.
Enzyme and pathway databases
BRENDA	3.1.1.4. 18619.
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.
ProDom	PD000303. PhospholipaseA2. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_TRIFL

Accession

Primary (citable) accession number: P06859
Secondary accession number(s): Q92118

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)