Reviewed, UniProtKB/Swiss-Prot P70498 (PLD2_RAT)

Names and origin

Protein names

Recommended name:
    Phospholipase D2
      Short name=PLD 2
      Short name=rPLD2
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 2
    Phosphatidylcholine-hydrolyzing phospholipase D2
    PLD1C

Gene names

Name:

Pld2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	933 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May have a role in signal-induced cytoskeletal regulation and/or endocytosis By similarity.
Catalytic activity	A phosphatidylcholine + H2O = choline + a phosphatidate.
Enzyme regulation	Stimulated by phosphatidylinositol 4,5-bisphosphate and phosphatidylethanolamine. Inhibited by phosphatidylserine and by oleate. Is not responsive to ADP-ribosylation factor 1 (ARF1), nor to GTP-binding protein RhoA.
Subunit structure	Interacts with PIP5K1A and EGFR By similarity.
Subcellular location	Membrane; Peripheral membrane protein By similarity.
Tissue specificity	Expressed in brain, lung, heart, kidney, stomach, small intestine, colon, and testis, and at a much lower levels in thymus, liver and muscle.
Post-translational modification	Phosphorylated on Tyr-11; most likely by EGFR By similarity.
Sequence similarities	Belongs to the phospholipase D family. Contains 1 PH domain. Contains 2 PLD phosphodiesterase domains. Contains 1 PX (phox homology) domain.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Membrane
Domain	Repeat
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell communication Inferred from electronic annotation. Source: InterPro neuron projection development Inferred from mutant phenotype. Source: RGD phospholipid catabolic process Inferred from mutant phenotype. Source: RGD positive regulation of cell adhesion Inferred from mutant phenotype. Source: RGD positive regulation of cell migration Inferred from mutant phenotype. Source: RGD positive regulation of mast cell degranulation Inferred from mutant phenotype. Source: RGD positive regulation of phosphoinositide 3-kinase cascade Inferred from mutant phenotype. Source: RGD positive regulation of receptor-mediated endocytosis Inferred from mutant phenotype. Source: RGD response to hydrogen peroxide Inferred from mutant phenotype. Source: RGD response to hypoxia Inferred from direct assay. Source: RGD response to organic cyclic substance Inferred from direct assay. Source: RGD response to peptide hormone stimulus Inferred from mutant phenotype. Source: RGD
Cellular component	Golgi apparatus Inferred from direct assay. Source: RGD caveola Inferred from direct assay. Source: RGD extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from direct assay. Source: RGD nucleus Inferred from direct assay. Source: RGD sarcolemma Inferred from direct assay. Source: RGD
Molecular function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phosphoinositide binding Inferred from electronic annotation. Source: InterPro phospholipase D activity Ref.2 Inferred from direct assay. Source: RGD protein kinase C binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 933	933	Phospholipase D2		PRO_0000218807
Regions
	Domain	65 – 195	131	PX
	Domain	203 – 311	109	PH
	Domain	437 – 464	28	PLD phosphodiesterase 1
	Domain	751 – 778	28	PLD phosphodiesterase 2
	Region	441 – 788	348	Catalytic
Amino acid modifications
	Modified residue	11	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	26	1	V → E in BAA19882. Ref.2
	Sequence conflict	125	1	N → P in BAA19882. Ref.2
	Sequence conflict	599	1	G → A in BAA19882. Ref.2
	Sequence conflict	792	1	K → E in BAA19882. Ref.2
	Sequence conflict	817 – 818	2	GR → KH in BAA19882. Ref.2
	Sequence conflict	919 – 924	6	HWGAKR → PLGSKE in BAA19882. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P70498-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: D430843B4D541EEA	FASTA	933	106,037
	10 20 30 40 50 60 MTVTQTDLFP YGDYLNSSQL HMEPDVVDTL KEGEDPADRM HPFLAIYDLQ PLRAHPLVFA 70 80 90 100 110 120 PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT KKKFRHFQEL HRDLQRHKVL 130 140 150 160 170 180 MSLLNLARFA AAHSPAREAA NENIPSLPRG GSEGSARHTA SKQKYLENYL NRLLTMSFYR 190 200 210 220 230 240 NYHAMTEFLE VSQLSFIPDL GSKGLEGVIR KRSGGHRVPG FTCCGRDQVC YRWSKRWLVV 250 260 270 280 290 300 KDSFLLYMRP ETGAISFVQL FDPGFEVQVG KRSTEARYGV RIDTSHRSLI LKCSSYRQAR 310 320 330 340 350 360 WWGQEITELA QGPGRDFLQL HQHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAREEIF 370 380 390 400 410 420 ITDWWLSPEI YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL LFKEVELALG INSGYSKRTL 430 440 450 460 470 480 MLLHPNIKVM RHPDLVTLWA HHEKLLVVDQ AVAFLGGLDL AYGRWDDVQY RLTDLGDPSE 490 500 510 520 530 540 SADSQTPTPG SDPAATPDLS HNHFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW 550 560 570 580 590 600 RDVGVVVHGV AARDLARHFI QRWNFTKTIK ARYKIPQYPY LLPKSASTAN HLPFIIPGGQ 610 620 630 640 650 660 CATVQVLRSV DRWSAGTLES SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE 670 680 690 700 710 720 IVDRILKAHE QGQCFRVYVL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEYSILHR 730 740 750 760 770 780 LKAAMGTAWR DYMSICGLRT HGELGGHPIS ELIYIHSKLL IADDRTVIIG SANINDRSLL 790 800 810 820 830 840 GKRDSELAIL IKDTEMEPSL MDGVEYQAGR FALSLRGRCF SVILGANTWP DLDLRDPVCD 850 860 870 880 890 900 DFFQLWQETA ENNATIYEQI FRCLPSNATR SLRALREYVA VESLATVSPS LAQSELAHIR 910 920 930 GHLVHFPLKF LEDESLLPHW GAKRGMIPLE VWT

References

[1]	"Molecular cloning and chromosome mapping of rat phospholipase D genes, Pld1a, Pld1b and Pld2." Nakashima S., Matsuda Y., Akao Y., Yoshimura S., Sakai H., Hayakawa K., Andoh M., Nozawa Y. Cytogenet. Cell Genet. 79:109-113(1997) [PubMed: 9533024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning, expression, and characterization of a novel phospholipase D complementary DNA from rat brain." Kodaki T., Yamashita S. J. Biol. Chem. 272:11408-11413(1997) [PubMed: 9111050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Brain.
[3]	"Differential mRNA expression of phospholipase D (PLD) isozymes during cAMP-induced differentiation in C6 glioma cells." Yoshimura S., Nakashima S., Ohguchi K., Sakai H., Shinoda J., Sakai N., Nozawa Y. Biochem. Biophys. Res. Commun. 225:494-499(1996) [PubMed: 8753790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 445-535. Tissue: Glial cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB003172 mRNA. Translation: BAA24078.1. D88672 mRNA. Translation: BAA19882.1.
IPI	IPI00188899.
PIR	PC4194.
RefSeq	NP_150641.2.
UniGene	Rn.9798
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P70498.
Genome annotation databases
GeneID	25097.
KEGG	rno:25097.
Organism-specific databases
CTD	25097.
RGD	3350. Pld2.
Phylogenomic databases
HOVERGEN	P70498.
Enzyme and pathway databases
BRENDA	3.1.4.4. 248.
Gene expression databases
Genevestigator	P70498.
Family and domain databases
InterPro	IPR011993. PH_type. IPR015679. Phospholipase_D. IPR001849. Pleckstrin_homology. IPR001736. PLipase_D/transphosphatidylase. IPR016555. PLipase_D_euk. IPR001683. PX. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:3.30.1520.10. PX. 1 hit.
PANTHER	PTHR18896. Phospholipase_D. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00614. PLDc. 2 hits. PF00787. PX. 1 hit. [Graphical view]
PIRSF	PIRSF009376. Phospholipase_D_euk. 1 hit.
SMART	SM00233. PH. 1 hit. SM00155. PLDc. 2 hits. SM00312. PX. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. False negative. PS50035. PLD. 2 hits. PS50195. PX. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	605401.

Entry information

Entry name

PLD2_RAT

Accession

Primary (citable) accession number: P70498
Secondary accession number(s): O08768

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 30, 2000
Last modified:	October 13, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)