P55939 (PLDA2_BRAOC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phospholipase D alpha 2
Short name=PLD 2
EC=3.1.4.4

Alternative name(s):
Choline phosphatase 2
Phosphatidylcholine-hydrolyzing phospholipase D 2

Gene names

Name:

PLD2

Organism

Brassica oleracea var. capitata (Cabbage)

Taxonomic identifier

3716 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Brassiceae › Brassica

Protein attributes

Sequence length	812 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.
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 C2 due to the absence of two potential calcium ligands.
Miscellaneous	All eight cysteine residues were shown to have free sulfhydryl groups by mass spectrometry. 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	Cytoplasm Membrane
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	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane 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: InterPro 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 – 36	36			PRO_0000024651
	Chain	37 – 812	776	Phospholipase D alpha 2		PRO_0000024652
Regions
	Domain	1 – 111	111	C2
	Domain	328 – 368	41	PLD phosphodiesterase 1
	Domain	658 – 685	28	PLD phosphodiesterase 2
Sites
	Active site	333	1	Potential
	Active site	335	1	Potential
	Active site	340	1	Potential
	Active site	663	1	Potential
	Active site	665	1	Potential
	Active site	670	1	Potential
Experimental info
	Sequence conflict	50	1	Q → E AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P55939 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: F771FC53734E7A2B	FASTA	812	92,062
	10 20 30 40 50 60 MAQHLLHGTL HATIYEVDAL HTGGLRSAGF LGKIISNVEE TIGFGKGETQ LYATIDLQKA 70 80 90 100 110 120 RVGRTRKITD EPKNPKWYES FHIYCAHMAS DIIFTVKDDN PIGATLIGRA YVPVDEVING 130 140 150 160 170 180 EEVEKWVEIL DDDRNPIHGE SKIHVKLQYF AVEADRNWNM GVKSAKFPGV PYTFFSQRQG 190 200 210 220 230 240 CKVSLYQGAH VPDNFVPKIP LAGGKNYEPH RCWEDIFDAI TNAKHLIYIT GWSVYTEITL 250 260 270 280 290 300 VRDSRRPKPG GDMTLGELLK KKATEGVRVL LLVWDDRTSV DVLKKDGLMA THDEDTENYF 310 320 330 340 350 360 NGSEVHCVLC PRNPDDGGSI VQNLQVSAMF THHQKIVVVD SEVPSQGGGS EMRRIMSFVG 370 380 390 400 410 420 GIDLCDGRYD TPFHSLFRTL DTVHHDDFHQ PNFTGASITK GGPREPWQDI HSRLEGPIAW 430 440 450 460 470 480 DVLYNFEQRW SKQGGKDILV KLRELSDIII TPSPVMFQED HDVWNVQLFR SIDGGAAAGF 490 500 510 520 530 540 PDSPEVAAEA GLVSGKDNVI DRSIQDAYIH AIRRAKDFIY IENQYFLGSS FAWAADGITP 550 560 570 580 590 600 EDINALHLIP KELSLKIVDK IEKGEKFRVY VVVPMWPEGI PESASVQAIL DWQRRTLEMM 610 620 630 640 650 660 YKDVTQALRA QGLEEDPRNY LTFFCLGNRE VKKEGEYEPA ERPDPDTDYM RAQEARRFMI 670 680 690 700 710 720 YVHSKMMIVD DEYIIVGSAN INQRSMDGAR DSEIAMGGYQ PHHLSHRQPA RGQVHGFRMS 730 740 750 760 770 780 LWYEHLGMLD ETFLDPSSLE CIEKVNRIAD KYWDFYSSES LEHDLPGHLL RYPISVDNEG 790 800 810 NITELPGFEF FPDSKARILG NKVDYLPPIL TT

References

[1]	"Molecular cloning and functional expression of a phospholipase D from cabbage (Brassica oleracea var. capitata)." Kim D.-U., Roh T.-Y., Lee J., Noh J.-Y., Jang Y.-J., Hoe K.-L., Yoo H.-S., Choi M.-U. Biochim. Biophys. Acta 1437:409-414(1999) [PubMed: 10101274] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification of two isoenzymes of phospholipase D from cabbage (Brassica oleracea var. capitata)." Pannenberg I., Mansfeld J., Ulbrich-Hofmann R. Plant Gene Register PGR98-188 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Improved purification and biochemical characterization of phospholipase D from cabbage." Abousalham A., Riviere M., Teissere M., Verger R. Biochim. Biophys. Acta 1158:1-7(1993) [PubMed: 8353126] [Abstract] Cited for: PROTEIN SEQUENCE OF 37-68. Tissue: Leaf.
[4]	"Investigation of sulfhydryl groups in cabbage phospholipase D by combination of derivatization methods and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry." Hwang I.S., Park S.J., Roh T.-Y., Choi M.-U., Kim H.J. Rapid Commun. Mass Spectrom. 15:110-115(2001) [PubMed: 11180538] [Abstract] Cited for: CHARACTERIZATION OF SULFHYDRYL GROUPS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U85482 mRNA. Translation: AAC79125.1. AF090444 mRNA. Translation: AAC78486.1. AF113919 Genomic DNA. Translation: AAD17209.1.
3D structure databases
ProteinModelPortal	P55939.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.1.4.4. 947.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR015679. PLipase_D. IPR001736. PLipase_D/transphosphatidylase. IPR024632. PLipase_D_C. IPR011402. PLipase_D_pln. [Graphical view]
PANTHER	PTHR18896. Phospholipase_D. 1 hit.
Pfam	PF00168. C2. 1 hit. PF12357. PLD_C. 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]
SUPFAM	SSF49562. C2_CaLB. 1 hit.
PROSITE	PS50004. C2. False negative. PS50035. PLD. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLDA2_BRAOC

Accession

Primary (citable) accession number: P55939
Secondary accession number(s): O49981, O82548

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 21, 2001
Last modified:	October 19, 2011
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program