NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 37-65; 165-183; 247-263 AND 273-294.
TISSUE=Venom, and Venom gland;
DOI=10.1016/S0091-6749(96)70093-3; PubMed=8828537 [NCBI, ExPASy, EBI, Israel, Japan]
King T.P., Lu G., Gonzalez M., Qian N., Soldatova L.;
"Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy.";
J. Allergy Clin. Immunol. 98:588-600(1996).

Comments

FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities (By similarity).
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 2-acylglycerophosphocholine + a carboxylate.
CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Contains six disulfide bonds (By similarity).
ALLERGEN: Causes an allergic reaction in human.
SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L43561; AAB48072.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P16233; 1LPB. [HSSP ENTRY / PDB]

ModBase

P49369.

Ontologies

GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR002334; Dol/Ves_allerg.
IPR000734; Lipase.
IPR008262; Lipase_AS.
IPR013818; Lipase_N.
Graphical view of domain structure.

PANTHER

PTHR11610; Lipase; 1.

Pfam

PF00151; Lipase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00825; DOLALLERGEN.

PROSITE

PS00120; LIPASE_SER; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allergen; Direct protein sequencing; Hydrolase; Lipid degradation; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 36`	`36`
`CHAIN`	`37 336`	`300`	`Phospholipase A1.`	`PRO_0000017813`
`ACT_SITE`	`173 173`		`Charge relay system (By similarity).`
`ACT_SITE`	`201 201`		`Charge relay system (By similarity).`
`ACT_SITE`	`265 265`		`Charge relay system (By similarity).`
`CONFLICT`	`37 37`		`G -> F (in Ref. 1; AA sequence).`

Sequence information

Length: 336 AA [This is the length of the unprocessed precursor]

Molecular weight: 37676 Da [This is the MW of the unprocessed precursor]

CRC64: 65548B7F5BE56456 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEENMNLKYL LLFVYFVQVL NCCYGHGDPL SYELDRGPKC PFNSDTVSII IETRENRNRD 

        70         80         90        100        110        120 
LYTLQTLQNH PEFKKKTITR PVVFITHGFT SSASETNFIN LAKALVDKDN YMVISIDWQT 

       130        140        150        160        170        180 
AACTNEAAGL KYLYYPTAAR NTRLVGQYIA TITQKLVKHY KISMANIRLI GHSLGAHASG 

       190        200        210        220        230        240 
FAGKKVQELK LGKYSEIIGL DPARPSFDSN HCSERLCETD AEYVQIIHTS NYLGTEKTLG 

       250        260        270        280        290        300 
TVDFYMNNGK NQPGCGRFFS EVCSHSRAVI YMAECIKHEC CLIGIPKSKS SQPISSCTKQ 

       310        320        330 
ECVCVGLNAK KYPSRGSFYV PVESTAPFCN NKGKII

P49369 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools