[1]	PROTEIN SEQUENCE. TISSUE=Venom; PubMed=8199462 [NCBI, ExPASy, EBI, Israel, Japan] Hoffman D.R.; "Allergens in hymenoptera venom. XXVI: the complete amino acid sequences of two vespid venom phospholipases."; Int. Arch. Allergy Immunol. 104:184-190(1994).

Comments

FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
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

PIR

A44563; A44563.

3D structure databases

HSSP

P54318; 1BU8. [HSSP ENTRY / PDB]

ModBase

P53357.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0008970;	Molecular function: phospholipase A1 activity (inferred from electronic annotation from InterPro).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from EC).
GO:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from UniProtKB-KW).
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.
PR00821; TAGLIPASE.

PROSITE

PS00120; LIPASE_SER; 1.

Other

ProtoNet

P53357.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 303`	`303`	`Phospholipase A1 2.`	`PRO_0000090375`
`ACT_SITE`	`140 140`		`Charge relay system (By similarity).`
`ACT_SITE`	`168 168`		`Charge relay system (By similarity).`
`ACT_SITE`	`232 232`		`Charge relay system (By similarity).`
`VARIANT`	`55 55`	`1`	`G -> E.`
`VARIANT`	`295 295`	`1`	`F -> Y.`

Sequence information

Length: 303 AA [This is the length of the unprocessed precursor]

Molecular weight: 33782 Da [This is the MW of the unprocessed precursor]

CRC64: 85816A837C0F3AF8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
GILPECKLVP EEISFVLSTR ENRDGVYLTL QKLKNGKMFK NSDLSSKKVP FLIHGFISSA 

        70         80         90        100        110        120 
TNKNYADMTR ALLDKDDIMV ISIDWRDGAC SNEFALLKFI GYPKAVENTR AVGKYIADFS 

       130        140        150        160        170        180 
KILIQKYKVL LENIRLIGHS LGAQIAGFAG KEFQRFKLGK YPEIIGLDPA GPSFKKKDCP 

       190        200        210        220        230        240 
ERICETDAHY VQILHTSSNL GTERTLGTVD FYINDGSNQP GCTYIIGETC SHTRAVKYLT 

       250        260        270        280        290        300 
ECIRRECCLI GVPQSKNPQP VSKCTRNECV CVGLNAKEYP KKGSFYVPVE AKAPFCNNNG 


KII

P53357 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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