Phospholipase A2-beta precursor - Arabidopsis thaliana (Mouse-ear cress)

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Q8GZB4 (PLA2B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phospholipase A2-beta
EC=3.1.1.4

Alternative name(s):
Secretory phospholipase A2-beta
Short name=AtsPLA2-beta

Gene names

Name:	PLA2-BETA
Ordered Locus Names:	At2g19690
ORF Names:	F6F22.28

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	147 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. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli. Regulates the process of cell elongation and plays important roles in shoot gravitropism by mediating auxin-induced cell elongation. Involved in stomatal opening in response to light. Plays a role in pollen development and germination and tube growth. Ref.1 Ref.7 Ref.9
Catalytic activity	Phosphatidylcholine + H₂O = 1-acylglycerophosphocholine + a carboxylate. Ref.1
Cofactor	Binds 1 calcium ion per subunit.
Enzyme regulation	Inhibited by aristolochic acid. Ref.7
Subcellular location	Secreted. Endoplasmic reticulum Ref.1 Ref.8.
Tissue specificity	Ubiquitous but expressed at a low level. Detected in vascular tissues and in the guard cells. Predominantly detected in pollen. Ref.1 Ref.6 Ref.7 Ref.9
Developmental stage	Expressed in the actively growing young stages of Arabidopsis seedlings. When plants grew, however, expression was evident only in cotyledons, primary leaves, and hypocotyls. The activity decreased in the secondary leaves, being detectable only in vascular tissues. In the roots as well, expression was localized mostly in vascular tissues. Expression becomes highly active when floral shoots bolted, especially in the young or actively growing tissues of inflorescence stems. Continuously expressed during pollen development. Ref.1 Ref.9
Induction	By auxin. By light. Ref.1 Ref.7
Disruption phenotype	RNAi mutant exhibits delayed light-induced stomatal opening. Ref.7
Miscellaneous	The enzyme has a preference towards palmitoyl acyl chain over linoleoyl acyl chain. It also has a slight preference for phosphatidylethanolamine over phosphatidylcholine.
Sequence similarities	Belongs to the phospholipase A2 family.
Sequence caution	The sequence AAC62146.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Endoplasmic reticulum Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gravitropism Inferred from mutant phenotype Ref.1. Source: UniProtKB lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from electronic annotation. Source: InterPro pollen germination Inferred from direct assay Ref.9. Source: UniProtKB pollen tube growth Inferred from direct assay Ref.9. Source: UniProtKB positive regulation of cell growth Inferred from mutant phenotype Ref.1. Source: UniProtKB response to auxin stimulus Inferred from expression pattern Ref.1. Source: UniProtKB
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.8. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phospholipase A2 activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select] Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8GZB4-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

Potential

Chain

29 – 147

119

Phospholipase A2-beta

PRO_0000417562

Regions

Motif

144 – 147

Prevents secretion from ER Potential

Sites

Active site

By similarity

Metal binding

Calcium; via carbonyl oxygen By similarity

Metal binding

Calcium; via carbonyl oxygen By similarity

Metal binding

Calcium; via carbonyl oxygen By similarity

Metal binding

Calcium By similarity

Amino acid modifications

Disulfide bond

31 ↔ 58

By similarity

Disulfide bond

35 ↔ 64

By similarity

Disulfide bond

40 ↔ 117

By similarity

Disulfide bond

51 ↔ 71

By similarity

Disulfide bond

70 ↔ 95

By similarity

Disulfide bond

77 ↔ 88

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C60D376FE4AB63D4
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FASTA

147

16,286

        10         20         30         40         50         60 
MMFRTSLMRF AAAFFAIVFV VLVGVARSEE CTRTCIAQNC DTLSIRYGKY CGIGHSGCPG 

        70         80         90        100        110        120 
EEPCDDLDAC CKIHDHCVEL NGMTNISCHK KFQRCVNRLS KAIKQSKNKK VGFSTKCPYS 

       130        140 
VVIPTVNQGM DIGILFSQLG NDMKTEL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Secretory low molecular weight phospholipase A2 plays important roles in cell elongation and shoot gravitropism in Arabidopsis." Lee H.Y., Bahn S.C., Kang Y.M., Lee K.H., Kim H.J., Noh E.K., Palta J.P., Shin J.S., Ryu S.B. Plant Cell 15:1990-2002(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY AUXIN, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation." Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M. Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Phospholipid-derived signaling mediated by phospholipase A in plants." Ryu S.B. Trends Plant Sci. 9:229-235(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[6]	"Multiple forms of secretory phospholipase A2 in plants." Lee H.Y., Bahn S.C., Shin J.S., Hwang I., Back K., Doelling J.H., Ryu S.B. Prog. Lipid Res. 44:52-67(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"Phospholipase A2beta mediates light-induced stomatal opening in Arabidopsis." Seo J., Lee H.Y., Choi H., Choi Y., Lee Y., Kim Y.W., Ryu S.B., Lee Y. J. Exp. Bot. 59:3587-3594(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY LIGHT, ENZYME REGULATION, TISSUE SPECIFICITY.
[8]	"Phospholipase A(2) is required for PIN-FORMED protein trafficking to the plasma membrane in the Arabidopsis root." Lee O.R., Kim S.J., Kim H.J., Hong J.K., Ryu S.B., Lee S.H., Ganguly A., Cho H.T. Plant Cell 22:1812-1825(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Endoplasmic reticulum- and Golgi-localized phospholipase A2 plays critical roles in Arabidopsis pollen development and germination." Kim H.J., Ok S.H., Bahn S.C., Jang J., Oh S.A., Park S.K., Twell D., Ryu S.B., Shin J.S. Plant Cell 23:94-110(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF541915 mRNA. Translation: AAN77229.1. AC005169 Genomic DNA. Translation: AAC62146.1. Sequence problems. CP002685 Genomic DNA. Translation: AEC06913.1. BX821623 mRNA. No translation available.
IPI	IPI00517903.
PIR	H84579.
RefSeq	NP_179559.2. NM_127527.3.
UniGene	At.39803.
3D structure databases
HSSP	HSSP built from PDB template 1O3W based on UniProtKB P00593.
ProteinModelPortal	Q8GZB4.
SMR	Q8GZB4. Positions 31-112.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G19690.1-P.
Proteomic databases
PRIDE	Q8GZB4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G19690.1; AT2G19690.1; AT2G19690.
GeneID	816488.
KEGG	ath:AT2G19690.
Organism-specific databases
TAIR	At2g19690.
Phylogenomic databases
eggNOG	NOG269950.
HOGENOM	HOG000239638.
InParanoid	Q8GZB4.
PhylomeDB	Q8GZB4.
ProtClustDB	CLSN2685359.
Gene expression databases
Genevestigator	Q8GZB4.
Family and domain databases
Gene3D	1.20.90.10. 1 hit.
InterPro	IPR001211. PLipase_A2. IPR013090. PLipase_A2_AS. IPR016090. PLipase_A2_dom. [Graphical view]
PANTHER	PTHR11716. PTHR11716. 1 hit.
Pfam	PF00068. Phospholip_A2_1. 1 hit. [Graphical view]
SMART	SM00085. PA2c. 1 hit. [Graphical view]
SUPFAM	SSF48619. PhospholipaseA2. 1 hit.
PROSITE	PS00119. PA2_ASP. False negative. PS00118. PA2_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLA2B_ARATH

Accession

Primary (citable) accession number: Q8GZB4
Secondary accession number(s): O82208

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2012
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents