[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Kordis D., Gubensek F.; "Evolutionary relationships of Viperidae phospholipase A2 genes inferred from intron sequences."; Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate.
COFACTOR: Binds 1 calcium ion (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.

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

AF253050; AAK49823.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P04084; 1VPI. [HSSP ENTRY / PDB]

ModBase

Q90ZZ9.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004623;	Molecular function: phospholipase A2 activity (inferred from electronic annotation from InterPro).
GO:0016042;	Biological process: lipid catabolic process (inferred from electronic annotation from InterPro).
GO:0006644;	Biological process: phospholipid metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016090; Phospholipase_A2.
IPR013090; Phospholipase_A2_AS.
IPR001211; Phospholipase_A2_euk.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.90.10; Phospholipase_A2; 1.

PANTHER

PTHR11716; Phospholipase_A2; 1.

Pfam

PF00068; Phospholip_A2_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00389; PHPHLIPASEA2.

ProDom

PD000303; PhospholipaseA2; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00085; PA2c; 1.
SMART graphical view of domain structure.

PROSITE

PS00119; PA2_ASP; 1.
PS00118; PA2_HIS; 1.

ProtoNet

Q90ZZ9.

Phylogenomic databases

HOVERGEN

Q90ZZ9; -.

Other

UniRef

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

Keywords

Calcium; Hydrolase; Lipid degradation; Metal-binding; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`By similarity.`
`CHAIN`	`17 138`	`122`	`Phospholipase A2 EC1.`	`PRO_0000022868`
`ACT_SITE`	`63 63`		`By similarity.`
`ACT_SITE`	`105 105`		`By similarity.`
`METAL`	`43 43`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`45 45`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`47 47`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`64 64`		`Calcium (By similarity).`
`DISULFID`	`42 131`		`By similarity.`
`DISULFID`	`44 60`		`By similarity.`
`DISULFID`	`59 111`		`By similarity.`
`DISULFID`	`65 138`		`By similarity.`
`DISULFID`	`66 104`		`By similarity.`
`DISULFID`	`73 97`		`By similarity.`
`DISULFID`	`91 102`		`By similarity.`

Sequence information

Length: 138 AA [This is the length of the unprocessed precursor]

Molecular weight: 15770 Da [This is the MW of the unprocessed precursor]

CRC64: 1A5D9F17FDAA9D56 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRTLWIVAVW LMSVEGNLYQ FGKMIKNKTG KPAMFSYSAY GCYCGWGGQG KPQDASDRCC 

        70         80         90        100        110        120 
FVHDCCYTRV NDCSPKMTSY SYSFENRDII CGDDDSCRKA VCECDREAAI CLGENVNTYD 

       130 
EKYRFYSSSH CVEETEQC

Q90ZZ9 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