Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P70496 (PLD1_RAT)

Last modified January 19, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phospholipase D1
      Short name=PLD 1
      Short name=rPLD1
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 1
    Phosphatidylcholine-hydrolyzing phospholipase D1
Gene names
Name: Pld1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1074 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic By similarity.

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Enzyme regulation

Stimulated by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, activated by the phosphokinase C-alpha, by the ADP-ribosylation factor-1 (ARF-1), and to a lesser extent by GTP-binding proteins: RHO A, RAC-1 and CDC42 By similarity.

Subunit structure

Interacts with PIP5K1A By similarity.

Subcellular location

Cytoplasmperinuclear region By similarity. Endoplasmic reticulum membrane; Lipid-anchor By similarity. Golgi apparatus membrane; Lipid-anchor By similarity. Late endosome membrane; Lipid-anchor By similarity. Note: Membrane-associated.

Post-translational modification

Phosphorylated on serine and threonine residues. Ref.7

It is uncertain whether palmitoylation is on Cys-240 and/or Cys-241. Palmitoylation is required prior to phosphorylation.

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 processLipid degradation
   Cellular componentCytoplasm
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionHydrolase
   PTMLipoprotein
Palmitate
Phosphoprotein
Gene Ontology (GO)
   Biological processcell communication

Inferred from electronic annotation. Source: InterPro

phosphatidic acid biosynthetic process

Inferred from mutant phenotype. Source: MGI

phospholipid catabolic process

Inferred from mutant phenotype. Source: RGD

positive regulation of cell migration

Inferred from mutant phenotype. Source: RGD

response to peptide hormone stimulus

Inferred from mutant phenotype. Source: RGD

   Cellular componentGolgi cisterna

Inferred from direct assay. Source: RGD

anchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

endosome

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium

Inferred from direct assay. Source: RGD

microsome

Inferred from direct assay. Source: RGD

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

vesicle

Inferred from direct assay. Source: RGD

   Molecular functionNAPE-specific phospholipase D activity

Inferred from electronic annotation. Source: EC

phosphoinositide binding

Inferred from electronic annotation. Source: InterPro

phospholipase D activity

Inferred from direct assay. Source: RGD

protein binding

Inferred from direct assay. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform PLD1A (identifier: P70496-1)

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.
Isoform PLD1B (identifier: P70496-2)

The sequence of this isoform differs from the canonical sequence as follows:
     585-623: SYFNHYRSHQNLIHGIKPHLKLFRPSSESEQGLTRHSAD → N
Isoform PLD1C (identifier: P70496-3)

The sequence of this isoform differs from the canonical sequence as follows:
     586-590: YFNHY → ESRLR
     591-1074: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10741074Phospholipase D1
PRO_0000218804

Regions

Domain81 – 212132PX
Domain219 – 328110PH
Domain459 – 48628PLD phosphodiesterase 1
Domain891 – 91828PLD phosphodiesterase 2
Region463 – 928466Catalytic

Amino acid modifications

Modified residue6291Phosphoserine By similarity
Lipidation2401S-palmitoyl cysteine Probable
Lipidation2411S-palmitoyl cysteine Probable

Natural variations

Alternative sequence585 – 62339SYFNH…RHSAD → N in isoform PLD1B.
VSP_005024
Alternative sequence586 – 5905YFNHY → ESRLR in isoform PLD1C.
VSP_005025
Alternative sequence591 – 1074484Missing in isoform PLD1C.
VSP_005026

Experimental info

Mutagenesis2401C → A: Abolishes palmitoylation and weakens membrane association; when associated with A-241. Ref.7
Mutagenesis2411C → A: Abolishes palmitoylation and weakens membrane association; when associated with A-240. Ref.7
Sequence conflict41R → K in BAA24576. Ref.4
Sequence conflict221S → R Ref.3
Sequence conflict221S → R Ref.6
Sequence conflict2831R → K in BAA24076. Ref.1
Sequence conflict2831R → K in BAA24077. Ref.1
Sequence conflict5421N → D Ref.1
Sequence conflict5421N → D Ref.2
Sequence conflict5421N → D Ref.4
Sequence conflict6001I → L in BAA24576. Ref.4
Sequence conflict7091P → A in BAA24076. Ref.1
Sequence conflict7091P → A in BAA24077. Ref.1
Sequence conflict735 – 7362PG → EV in BAA24076. Ref.1
Sequence conflict735 – 7362PG → EV in BAA24077. Ref.1
Sequence conflict739 – 7402HA → QP in BAA24076. Ref.1
Sequence conflict739 – 7402HA → QP in BAA24077. Ref.1
Sequence conflict7731S → T Ref.1
Sequence conflict7751H → R Ref.1
Sequence conflict7861S → T in BAA24076. Ref.1
Sequence conflict7861S → T in BAA24077. Ref.1
Sequence conflict8001A → C in BAA24076. Ref.1
Sequence conflict8001A → C in BAA24077. Ref.1
Sequence conflict8091H → T in BAA24076. Ref.1
Sequence conflict8091H → T in BAA24077. Ref.1
Sequence conflict8301D → N in BAA24076. Ref.1
Sequence conflict8301D → N in BAA24077. Ref.1
Sequence conflict934 – 9352TE → RQ in AAB86910. Ref.3
Sequence conflict951 – 9544FAQG → SLSTV Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform PLD1A [UniParc].

Last modified October 18, 2001. Version 3.
Checksum: 286943A447A881DB

FASTA1,074123,814
        10         20         30         40         50         60 
MSLRSEARVN TSTLQKIAAD MSNLIENLDT RELHFEGEEV EYDASPGDPT AQEACIPFSS 

        70         80         90        100        110        120 
IYNTQGFKEP NIQIYLSGCP VKAQVLEVER FTSTSRMPSV NLYTIELTHG EFTWQVKRKF 

       130        140        150        160        170        180 
KHFQEFHREL LKYKAFIRIP IPTKRHTFRR QNVKEEPREM PSLPRSSENA IQEEQFFGRR 

       190        200        210        220        230        240 
KQLEDYLTKI LKMPMYRNYH ATTEFLDVSQ LSFIHDLGPK GLEGMIMKRS GGHRIPGVNC 

       250        260        270        280        290        300 
CGHGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFRIKVGKKE TETKYGLRID 

       310        320        330        340        350        360 
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTDFLKDHRF GSYAAVHENI LAKWYVNAKG 

       370        380        390        400        410        420 
YFEDIANAME GATEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY 

       430        440        450        460        470        480 
KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSSVYL WAHHEKLVII DQSVAFVGGI 

       490        500        510        520        530        540 
DLAYGRWDDN EHRLTDVGSV KRVTSGQSLG SLTAASVESM ESLSLKDKHQ SHKNEPVLKS 

       550        560        570        580        590        600 
VNDTDMKLKG IGKSRKFSKF SLYRQLHRRN LHNSDSISSV DSASSYFNHY RSHQNLIHGI 

       610        620        630        640        650        660 
KPHLKLFRPS SESEQGLTRH SADTGSIRSV QTGVGELHGE TRFWHGKDYC NFVFKDWVQL 

       670        680        690        700        710        720 
DKPFADFIDR YSTPRMPWHD IGSVVHGKAA RDVARHFIQR WNFTKIMKPK YRSLSYPFLL 

       730        740        750        760        770        780 
PKSQATAHEL RYQVPGAVHA KAQLLRSAAD WSAGIKHHEE SIHAAYTHVI ENSKHYIYIE 

       790        800        810        820        830        840 
NQFFISCADD KVVFNKVGNA IAQRILKAHR EGQRYRVYIV IPLLPGFEGD ISTGGGNALQ 

       850        860        870        880        890        900 
AIMHFNYRTM CRGESSILEQ LKPELGNKWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL 

       910        920        930        940        950        960 
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FAQGLRLECF 

       970        980        990       1000       1010       1020 
RLVLGYLSDP SEDIQDPVSD KFFKEIWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI 

      1030       1040       1050       1060       1070 
NKPILAKEDR LRAEEELRKI RGFLVQFPFY FLSEENLLPS VGTKEAIVPM EVWT 

« Hide

Isoform PLD1B.

Checksum: 350956C43A38E506
Show »

FASTA1,036119,357
Isoform PLD1C.

Checksum: FBD1FD4D7FAF9D18
Show »

FASTA59068,318

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] (ISOFORMS PLD1A AND PLD1B).
[2]"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 467-673 (ISOFORMS PLD1A AND PLD1B).
Tissue: Glial cell.
[3]"Cloning and characterization of phospholipase D from rat brain."
Park S.K., Provost J.J., Bae C.D., Ho W.T., Exton J.H.
J. Biol. Chem. 272:29263-29271(1997) [PubMed: 9361006] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1B).
[4]"Cloning, differential regulation and tissue distribution of alternatively spliced isoforms of ADP-ribosylation-factor-dependent phospholipase D from rat liver."
Katayama K., Kodaki T., Nagamachi Y., Yamashita S.
Biochem. J. 329:647-652(1998) [PubMed: 9445394] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
[5]"Molecular cloning of a cDNA homologous to a phospholipase D1 segment."
Lassegue B., Alexander R.W., Griendling K.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-511.
[6]"Phospholipase D not having transphosphatidylation reaction."
Park S.K., Exton J.H.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1C).
Tissue: Lung.
[7]"Requirements and effects of palmitoylation of rat PLD1."
Xie Z., Ho W.T., Exton J.H.
J. Biol. Chem. 276:9383-9391(2001) [PubMed: 11121416] [Abstract]
Cited for: PALMITOYLATION AT CYS-240 AND CYS-241, MUTAGENESIS OF CYS-240 AND CYS-241, PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB003170 mRNA. Translation: BAA24076.1.
AB003171 mRNA. Translation: BAA24077.1.
U69550 mRNA. Translation: AAB86910.1.
AB000778 mRNA. Translation: BAA24576.1.
AB000779 mRNA. Translation: BAA24577.1.
U88986 mRNA. Translation: AAB91329.1.
AF017251 mRNA. Translation: AAD01609.1.
IPIIPI00188898.
IPI00231169.
IPI00231170.
PIRT13725.
T13732.
T13943.
T46635.
RefSeqNP_112254.1.
UniGeneRn.11130

3D structure databases

SMRP70496. Positions 97-211, 759-940.
ModBaseSearch...

Protein-protein interaction databases

STRINGP70496.

PTM databases

PhosphoSiteP70496.

Genome annotation databases

EnsemblENSRNOT00000039296; ENSRNOP00000034466; ENSRNOG00000028156; Rattus norvegicus. [Genome view]
GeneID25096.
KEGGrno:25096.
UCSCNM_030992. rat.

Organism-specific databases

CTD25096.
RGD3349. Pld1.

Phylogenomic databases

eggNOGroNOG09371.
HOVERGENP70496.
InParanoidP70496.

Enzyme and pathway databases

BRENDA3.1.4.4. 248.

Gene expression databases

ArrayExpressP70496.
GenevestigatorP70496.
GermOnlineENSRNOG00000028156. Rattus norvegicus.

Family and domain databases

InterProIPR011993. PH_type.
IPR015679. Phospholipase_D.
IPR001849. Pleckstrin_homology.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
IPR001683. PX.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.30.1520.10. PX. 1 hit.
PANTHERPTHR18896. Phospholipase_D. 1 hit.
PfamPF00169. PH. 1 hit.
PF00614. PLDc. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
PIRSFPIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTSM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio605397.

Entry information

Entry namePLD1_RAT
AccessionPrimary (citable) accession number: P70496
Secondary accession number(s): O08959 expand/collapse secondary AC list , O35856, O54765, P70497, Q9QWJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 18, 2001
Last modified: January 19, 2010
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents