Reviewed, UniProtKB/Swiss-Prot Q41142 (PLDA1_RICCO)

Names and origin

Protein names

Recommended name:
    Phospholipase D alpha 1
      Short name=PLD 1
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 1
    Phosphatidylcholine-hydrolyzing phospholipase D 1

Gene names

Name:

PLD1

Organism

Ricinus communis (Castor bean)

Taxonomic identifier

3988 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Protein attributes

Sequence length	808 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	Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence.
Catalytic activity	A phosphatidylcholine + H2O = choline + a phosphatidate.
Cofactor	Calcium. Calcium requirement for activity depends on pH. Active either under acidic conditions with micromolar levels of calcium (PIP2-dependent) or at neutral pH with millimolar levels of calcium (PIP2-independent).
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Vacuole. Endoplasmic reticulum. Plastid. Cell membrane.
Tissue specificity	Expression is higher in radicle than in endosperm.
Domain	C2 domain is a calcium-binding fold, and the binding promotes the protein association with membranes. A lower affinity toward calcium can be anticipated for PLD alpha due to the absence of two potential calcium ligands.
Miscellaneous	The propeptide appears to play a key role in the proper folding and activation of the enzyme.
Sequence similarities	Belongs to the phospholipase D family. C2-PLD subfamily. Contains 1 C2 domain. Contains 2 PLD phosphodiesterase domains.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cell membrane Cytoplasm Endoplasmic reticulum Membrane Plastid Vacuole
Domain	Repeat
Ligand	Calcium
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylcholine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plastid Inferred from electronic annotation. Source: UniProtKB-SubCell vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase D 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
	Propeptide	1 – 30	30			PRO_0000024653
	Chain	31 – 808	778	Phospholipase D alpha 1		PRO_0000024654
Regions
	Domain	1 – 109	109	C2
	Domain	326 – 364	39	PLD phosphodiesterase 1
	Domain	654 – 681	28	PLD phosphodiesterase 2
Sites
	Active site	331	1	Potential
	Active site	333	1	Potential
	Active site	338	1	Potential
	Active site	659	1	Potential
	Active site	661	1	Potential
	Active site	666	1	Potential
Experimental info
	Sequence conflict	268	1	L → I in AAB37305. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q41142-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: E75F6CFFB9ADF3CB	FASTA	808	91,992
	10 20 30 40 50 60 MAQISLHGTL HVTIYEVDKL HSGGGPHFFR KLVENIEETV GFGKGVSKLY ATIDLEKARV 70 80 90 100 110 120 GRTRILENEQ SNPRWYESFH VYCAHQASNV IFTVKDDNPI GATLIGRAYV PVEELLDGEE 130 140 150 160 170 180 IDRWVEILDE DKNPVHSGSK IHVKLQYFEV TKDRNWGQGI RSSKYPGVPY TYFSQRQGCK 190 200 210 220 230 240 VSLYQDAHIP DKFVPQIPLA GGNYYEPHRC WEDVFDAITN AKHLIYITGW SVYTEISLIR 250 260 270 280 290 300 DSRRPKPGGD ITLGELLKKK ASEGVRVLML VWDDRTSVGL LKKDGLMATH DEETEHFFQN 310 320 330 340 350 360 TDVHCVLCPR NPDDGGSFVQ DLQISTMFTH HQKIVVVDSA MPNGDSQRRR IVSFVGGLDL 370 380 390 400 410 420 CDGRYDSPFH SLFRTLDSAH HDDFHQPNFA GASIEKGGPR EPWHDIHSRL EGPIAWDVLF 430 440 450 460 470 480 NFEQRWRKQG GKDLLIQLRE LEDVIIPPSP VMYPDDFEAW NVQLFRSIDG GAAFGFPETP 490 500 510 520 530 540 EDAPEAGLVS GKDNIIDRSI QDAYIHAIRR AKNFIYIENQ YFLGSSFGWS PDGIKPEDIN 550 560 570 580 590 600 ALHLIPKELS LKILSKIAAG ERFTVYIVVP MWPEGIPESA SVQAILDWQK RTMEMMYKDI 610 620 630 640 650 660 VQALKANGII EDPRNYLTFF CLGNREVKKS GEYEPAEKPE PDTDYIRAQE ARRFMIYVHT 670 680 690 700 710 720 KMMIVDDEYI IIGSANINQR SMDGARDSEI AMGAYQPHHL STRQPARGQI HGFRMSLWYE 730 740 750 760 770 780 HLGMLDESFL NPESEECVRK VNQMAEKYWD LYSSETLEHD LPGHLLRYPI GVASEGDVTE 790 800 LPGTEFFPDT KARVLGAKSD YLPPILTT

References

[1]	"Cloning and expression of phosphatidylcholine-hydrolyzing phospholipase D from Ricinus communis L." Wang X., Xu L., Zheng L. J. Biol. Chem. 269:20312-20317(1994) [PubMed: 8051126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-55. Strain: cv. Hale. Tissue: Endosperm.
[2]	"Structure and analysis of phospholipase D gene from Ricinus communis L." Xu L., Zheng L., Coughlan S.J., Wang X. Plant Mol. Biol. 32:767-771(1996) [PubMed: 8980529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L33686 mRNA. Translation: AAB04095.1. U72693 Genomic DNA. Translation: AAB37305.1.
PIR	T10171.
3D structure databases
SMR	Q41142. Positions 6-146.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.4.4. 816.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR015679. Phospholipase_D. IPR011402. PLD_pln. IPR001736. PLipase_D/transphosphatidylase. [Graphical view]
PANTHER	PTHR18896. Phospholipase_D. 1 hit.
Pfam	PF00168. C2. 1 hit. PF00614. PLDc. 2 hits. [Graphical view]
PIRSF	PIRSF036470. PLD_plant. 1 hit.
SMART	SM00239. C2. 1 hit. SM00155. PLDc. 2 hits. [Graphical view]
PROSITE	PS50004. C2. False negative. PS50035. PLD. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLDA1_RICCO

Accession

Primary (citable) accession number: Q41142
Secondary accession number(s): P93507

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)