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Protein

Phospholipase D2

Gene

Pld2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have a role in signal-induced cytoskeletal regulation and/or endocytosis.By similarity1 Publication

Catalytic activityi

A phosphatidylcholine + H2O = choline + a phosphatidate.

Enzyme regulationi

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.

GO - Molecular functioni

  • N-acylphosphatidylethanolamine-specific phospholipase D activity Source: UniProtKB-EC
  • phosphatidylinositol binding Source: InterPro
  • phospholipase D activity Source: RGD
  • protein kinase C binding Source: RGD

GO - Biological processi

  • inositol lipid-mediated signaling Source: InterPro
  • neuron projection development Source: RGD
  • phosphatidic acid biosynthetic process Source: InterPro
  • phospholipid catabolic process Source: RGD
  • positive regulation of cell adhesion Source: RGD
  • positive regulation of cell migration Source: RGD
  • positive regulation of mast cell degranulation Source: RGD
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: RGD
  • positive regulation of receptor-mediated endocytosis Source: RGD
  • regulation of phagocytosis Source: InterPro
  • response to hydrogen peroxide Source: RGD
  • response to hypoxia Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.4.4. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase D2 (EC:3.1.4.4)
Short name:
PLD 2
Short name:
rPLD2
Alternative name(s):
Choline phosphatase 2
PLD1C
Phosphatidylcholine-hydrolyzing phospholipase D2
Gene namesi
Name:Pld2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3350. Pld2.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: RGD
  • Golgi apparatus Source: RGD
  • lamellipodium Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • sarcolemma Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933Phospholipase D2PRO_0000218807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated on Tyr-11; most likely by EGFR (By similarity). Phosphorylated by FGR.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP70498.

PTM databases

iPTMnetiP70498.
SwissPalmiP70498.

Expressioni

Tissue specificityi

Expressed in brain, lung, heart, kidney, stomach, small intestine, colon, and testis, and at a much lower levels in thymus, liver and muscle.

Interactioni

Subunit structurei

Interacts with PIP5K1B and EGFR.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Oprm1P335353EBI-6140589,EBI-4392569

GO - Molecular functioni

  • protein kinase C binding Source: RGD

Protein-protein interaction databases

BioGridi247169. 6 interactions.
IntActiP70498. 2 interactions.
MINTiMINT-132445.

Structurei

3D structure databases

ProteinModelPortaliP70498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 195131PXPROSITE-ProRule annotationAdd
BLAST
Domaini203 – 311109PHAdd
BLAST
Domaini437 – 46428PLD phosphodiesterase 1PROSITE-ProRule annotationAdd
BLAST
Domaini751 – 77828PLD phosphodiesterase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni441 – 788348CatalyticAdd
BLAST

Sequence similaritiesi

Belongs to the phospholipase D family.Curated
Contains 1 PH domain.Curated
Contains 2 PLD phosphodiesterase domains.PROSITE-ProRule annotation
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000246972.
HOVERGENiHBG006650.
InParanoidiP70498.
KOiK01115.
PhylomeDBiP70498.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001683. Phox.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D1/D2.
IPR015679. PLipase_D_fam.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 2 hits.
PfamiPF00614. PLDc. 1 hit.
PF13091. PLDc_2. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
PIRSFiPIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTiSM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70498-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVTQTDLFP YGDYLNSSQL HMEPDVVDTL KEGEDPADRM HPFLAIYDLQ
60 70 80 90 100
PLRAHPLVFA PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT
110 120 130 140 150
KKKFRHFQEL HRDLQRHKVL MSLLNLARFA AAHSPAREAA NENIPSLPRG
160 170 180 190 200
GSEGSARHTA SKQKYLENYL NRLLTMSFYR NYHAMTEFLE VSQLSFIPDL
210 220 230 240 250
GSKGLEGVIR KRSGGHRVPG FTCCGRDQVC YRWSKRWLVV KDSFLLYMRP
260 270 280 290 300
ETGAISFVQL FDPGFEVQVG KRSTEARYGV RIDTSHRSLI LKCSSYRQAR
310 320 330 340 350
WWGQEITELA QGPGRDFLQL HQHDSYAPPR PGTLARWFVN GAGYFAAVAD
360 370 380 390 400
AILRAREEIF ITDWWLSPEI YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL
410 420 430 440 450
LFKEVELALG INSGYSKRTL MLLHPNIKVM RHPDLVTLWA HHEKLLVVDQ
460 470 480 490 500
AVAFLGGLDL AYGRWDDVQY RLTDLGDPSE SADSQTPTPG SDPAATPDLS
510 520 530 540 550
HNHFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW RDVGVVVHGV
560 570 580 590 600
AARDLARHFI QRWNFTKTIK ARYKIPQYPY LLPKSASTAN HLPFIIPGGQ
610 620 630 640 650
CATVQVLRSV DRWSAGTLES SILNAYLHTI RESQHFLYIE NQFFISCSDG
660 670 680 690 700
RTVLNKVGDE IVDRILKAHE QGQCFRVYVL LPLLPGFEGD ISTGGGNSIQ
710 720 730 740 750
AILHFTYRTL CRGEYSILHR LKAAMGTAWR DYMSICGLRT HGELGGHPIS
760 770 780 790 800
ELIYIHSKLL IADDRTVIIG SANINDRSLL GKRDSELAIL IKDTEMEPSL
810 820 830 840 850
MDGVEYQAGR FALSLRGRCF SVILGANTWP DLDLRDPVCD DFFQLWQETA
860 870 880 890 900
ENNATIYEQI FRCLPSNATR SLRALREYVA VESLATVSPS LAQSELAHIR
910 920 930
GHLVHFPLKF LEDESLLPHW GAKRGMIPLE VWT
Length:933
Mass (Da):106,037
Last modified:May 30, 2000 - v2
Checksum:iD430843B4D541EEA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261V → E in BAA19882 (PubMed:9111050).Curated
Sequence conflicti125 – 1251N → P in BAA19882 (PubMed:9111050).Curated
Sequence conflicti599 – 5991G → A in BAA19882 (PubMed:9111050).Curated
Sequence conflicti792 – 7921K → E in BAA19882 (PubMed:9111050).Curated
Sequence conflicti817 – 8182GR → KH in BAA19882 (PubMed:9111050).Curated
Sequence conflicti919 – 9246HWGAKR → PLGSKE in BAA19882 (PubMed:9111050).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003172 mRNA. Translation: BAA24078.1.
D88672 mRNA. Translation: BAA19882.1.
PIRiPC4194.
RefSeqiNP_150641.2. NM_033299.2.
UniGeneiRn.9798.

Genome annotation databases

GeneIDi25097.
KEGGirno:25097.
UCSCiRGD:3350. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003172 mRNA. Translation: BAA24078.1.
D88672 mRNA. Translation: BAA19882.1.
PIRiPC4194.
RefSeqiNP_150641.2. NM_033299.2.
UniGeneiRn.9798.

3D structure databases

ProteinModelPortaliP70498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247169. 6 interactions.
IntActiP70498. 2 interactions.
MINTiMINT-132445.

PTM databases

iPTMnetiP70498.
SwissPalmiP70498.

Proteomic databases

PRIDEiP70498.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25097.
KEGGirno:25097.
UCSCiRGD:3350. rat.

Organism-specific databases

CTDi5338.
RGDi3350. Pld2.

Phylogenomic databases

HOGENOMiHOG000246972.
HOVERGENiHBG006650.
InParanoidiP70498.
KOiK01115.
PhylomeDBiP70498.

Enzyme and pathway databases

BRENDAi3.1.4.4. 5301.

Miscellaneous databases

PROiP70498.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001683. Phox.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D1/D2.
IPR015679. PLipase_D_fam.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 2 hits.
PfamiPF00614. PLDc. 1 hit.
PF13091. PLDc_2. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
PIRSFiPIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTiSM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 445-535.
    Tissue: Glial cell.
  4. "Activation of RBL-2H3 mast cells is dependent on tyrosine phosphorylation of phospholipase D2 by Fyn and Fgr."
    Choi W.S., Hiragun T., Lee J.H., Kim Y.M., Kim H.P., Chahdi A., Her E., Han J.W., Beaven M.A.
    Mol. Cell. Biol. 24:6980-6992(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAST CELL ACTIVATION, PHOSPHORYLATION BY FGR.

Entry informationi

Entry nameiPLD2_RAT
AccessioniPrimary (citable) accession number: P70498
Secondary accession number(s): O08768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: June 8, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.