Phospholipase D2 - Mus musculus (Mouse)

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P97813 (PLD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. 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 D2
Short name=PLD 2
Short name=mPLD2
EC=3.1.4.4

Alternative name(s):
Choline phosphatase 2
PLD1C
Phosphatidylcholine-hydrolyzing phospholipase D2

Gene names

Name:

Pld2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	933 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May have a role in signal-induced cytoskeletal regulation and/or endocytosis.
Catalytic activity	A phosphatidylcholine + H₂O = choline + a phosphatidate.
Enzyme regulation	Stimulated by phosphatidylinositol 4,5-bisphosphate. Is not responsive to either ADP-ribosylation factor-1 (ARF-1) or GTP-binding proteins such as RHOA.
Subunit structure	Interacts with PIP5K1B By similarity. Interacts with EGFR.
Subcellular location	Membrane; Peripheral membrane protein.
Tissue specificity	Ubiquitous. Highest levels in brain and lung. Ref.3
Developmental stage	Expressed at high levels in the hippocampus at the earliest time at which it is defined as a structure and also in ventricular neural cells as well as differentiating neurons outside of the ventricular region. Expressed during development in lower levels in mesenchymal cells derived from the neural crest that are destined to form bones of the skull.
Post-translational modification	Phosphorylated by FGR By similarity. Phosphorylated on Tyr-11; most likely by EGFR. Ref.4
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 Lipid metabolism
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor internalization Inferred from direct assay PubMed 14718562. Source: MGI cell communication Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	brush border membrane Inferred from direct assay PubMed 15598876. Source: MGI endoplasmic reticulum membrane Traceable author statement. Source: Reactome
Molecular_function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro phospholipase D activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select] Note: At least 3 isoforms are produced.

Isoform 1 (identifier: P97813-1) 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

Chain

1 – 933

933

Phospholipase D2

PRO_0000218806

Regions

Domain

65 – 195

131

Domain

203 – 311

109

Domain

437 – 464

PLD phosphodiesterase 1

Domain

751 – 778

PLD phosphodiesterase 2

Region

441 – 788

348

Catalytic

Amino acid modifications

Modified residue

Phosphotyrosine Ref.4

Experimental info

Mutagenesis

Y → F: 2-fold increase in basal phospholipase activity. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified July 1, 1997. Version 2.
Checksum: BADE1E0DF2EAC9ED
Show »

FASTA

933

106,168

        10         20         30         40         50         60 
MTVTQKNLFP YGDYLNSSQL HMEPDEVDTL REGEDPADRM HPYLAIYDLQ PLKAHPLVFA 

        70         80         90        100        110        120 
PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT KKKFRHFQEL HRDLQRHKVL 

       130        140        150        160        170        180 
MSLLPLARFA VTHSPAREAA AEDIPSLPRG GSEGSARHTA SKQKYLENYL NRLLTMSFYR 

       190        200        210        220        230        240 
NYHAMTEFLE VSQLSFIPDL GSKGLEGVIR KRSGGHRVPG FTFCGRDQVC YRWSKRWLVV 

       250        260        270        280        290        300 
KDSFLLYMRP ETGAISFVQL FDPGFEVQVG KRSTETRYGV RIDTSHRSLI LKCSSYRQAR 

       310        320        330        340        350        360 
WWGQEITELA QGSGRDFLQL HQHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAQEEIF 

       370        380        390        400        410        420 
ITDWWLSPEI YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL LFKEVELALG INSGYSKRTL 

       430        440        450        460        470        480 
MLLHPNIKVM RHPDLVTLWA HHEKLLVVDQ VVAFLGGLDL AFGRWDDVQY RLTDLGDPSE 

       490        500        510        520        530        540 
PVHLQTPTLG SDPAATPDLS HNQFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW 

       550        560        570        580        590        600 
RDVGVVVHGV AARDLARHFI QRWNFTKTTK ARYKTPLYPY LLPKSTSTAN NLPFMIPGGQ 

       610        620        630        640        650        660 
CATVQVLRSV DRWSAGTLEN SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE 

       670        680        690        700        710        720 
IVDRILKAHE QGQCFRVYLL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEHSILHR 

       730        740        750        760        770        780 
LKAAMGTAWR DYMSICGLRT HGELGGHPIS ELIYIHSKML IADDRTVIIG SANINDRSLL 

       790        800        810        820        830        840 
GKRDSELAIL IKDTEMEPSL MDGVEYQAGR FALSLRKHCF SVILGANTWP DLDLRDPVCD 

       850        860        870        880        890        900 
DFFQLWQETA ENNATIYEQI FRCLPSNATR SLRALREYVA VESLATVSPS LAQSELAHIQ 

       910        920        930 
GHLVHFPLKF LEDESLLPPL GSKEGMIPLE VWT

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References

[1]	"Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization." Colley W.C., Sung T.-C., Roll R., Jenco J.M., Hammond S.M., Altshuller Y.M., Bar-Sagi D., Morris A.J., Frohman M.A. Curr. Biol. 7:191-201(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Embryo and Neonatal brain.
[2]	"Organization and alternative splicing of the murine phospholipase D2 gene." Redina O.E., Frohman M.A. Biochem. J. 331:845-851(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129.
[3]	"Cloning and expression analysis of murine phospholipase D1." Colley W.C., Altshuller Y.M., Sue-Ling C.K., Copeland N.G., Gilbert D.J., Jenkins N.A., Branch K.D., Tsirka S.E., Bollag R.J., Bollag W.B., Frohman M.A. Biochem. J. 326:745-753(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation." Slaaby R., Jensen T., Hansen H.S., Frohman M.A., Seedorf K. J. Biol. Chem. 273:33722-33727(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-11, MUTAGENESIS OF TYR-11.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U87557 mRNA. Translation: AAC53173.1. AF052294 , AF052291, AF052293, AF052292 Genomic DNA. Translation: AAC24519.1.
IPI	IPI00469217.
RefSeq	NP_032902.1. NM_008876.2.
UniGene	Mm.260177.
3D structure databases
ProteinModelPortal	P97813.
SMR	P97813. Positions 341-402, 755-794.
ModBase	Search...
PTM databases
PhosphoSite	P97813.
Proteomic databases
PaxDb	P97813.
PRIDE	P97813.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000018429; ENSMUSP00000018429; ENSMUSG00000020828.
GeneID	18806.
KEGG	mmu:18806.
Organism-specific databases
CTD	5338.
MGI	MGI:892877. Pld2.
Phylogenomic databases
eggNOG	COG1502.
HOGENOM	HOG000246972.
HOVERGEN	HBG006650.
KO	K01115.
OrthoDB	EOG49ZXNK.
Enzyme and pathway databases
BRENDA	3.1.4.4. 3474.
Reactome	REACT_112621. Metabolism.
Gene expression databases
ArrayExpress	P97813.
Bgee	P97813.
CleanEx	MM_PLD2.
Genevestigator	P97813.
GermOnline	ENSMUSG00000020828. Mus musculus.
Family and domain databases
Gene3D	2.30.29.30. 1 hit. 3.30.1520.10. 1 hit.
InterPro	IPR011993. PH_like_dom. IPR001683. Phox. IPR025202. PLD-like_dom. IPR001849. Pleckstrin_homology. IPR001736. PLipase_D/transphosphatidylase. IPR016555. PLipase_D_euk. IPR015679. PLipase_D_fam. [Graphical view]
PANTHER	PTHR18896. PTHR18896. 1 hit.
Pfam	PF00614. PLDc. 1 hit. PF13091. PLDc_2. 1 hit. 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]
SUPFAM	SSF64268. PX. 1 hit.
PROSITE	PS50003. PH_DOMAIN. False negative. PS50035. PLD. 2 hits. PS50195. PX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PLD2. mouse.
NextBio	295114.
SOURCE	Search...

Entry information

Entry name

PLD2_MOUSE

Accession

Primary (citable) accession number: P97813

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents