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Q13393 (PLD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase D1

Short name=PLD 1
Short name=hPLD1
EC=3.1.4.4
Alternative name(s):
Choline phosphatase 1
Phosphatidylcholine-hydrolyzing phospholipase D1
Gene names
Name:PLD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Inhibited by oleate.

Subunit structure

Interacts with PIP5K1B. Ref.7

Subcellular location

Cytoplasmperinuclear region By similarity. Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side By similarity. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side By similarity. Late endosome membrane; Lipid-anchor; Cytoplasmic side By similarity.

Tissue specificity

Expressed abundantly in the pancreas and heart and at high levels in brain, placenta, spleen, uterus and small intestine. Ref.6

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
Lipid metabolism
   Cellular componentCytoplasm
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionHydrolase
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Traceable author statement PubMed 10848592. Source: ProtInc

chemotaxis

Traceable author statement PubMed 10848592. Source: ProtInc

defense response to Gram-positive bacterium

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylglycerol biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 14718562. Source: MGI

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

endosome

Inferred from direct assay PubMed 14718562. Source: MGI

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

membrane

Traceable author statement Ref.1. Source: ProtInc

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNAPE-specific phospholipase D activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphatidylinositol binding

Inferred from electronic annotation. Source: InterPro

phospholipase D activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 17853892. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CFL1P235284EBI-2827556,EBI-352733

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform PLD1A (identifier: Q13393-1)

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: Q13393-2)

The sequence of this isoform differs from the canonical sequence as follows:
     585-623: SYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHAD → N
Isoform PLD1C (identifier: Q13393-3)

The sequence of this isoform differs from the canonical sequence as follows:
     514-597: PAAMESMESL...NHYRSHHNLI → IPGPSVVYRQ...SSSAGTSQKL
     598-1074: Missing.
Isoform PLD1D (identifier: Q13393-4)

The sequence of this isoform differs from the canonical sequence as follows:
     962-971: VVLGYLDDPS → SKMTPGVEDP
     972-1074: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10741074Phospholipase D1
PRO_0000218802

Regions

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

Amino acid modifications

Modified residue6291Phosphoserine Ref.8
Lipidation2401S-palmitoyl cysteine By similarity
Lipidation2411S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence514 – 59784PAAME…HHNLI → IPGPSVVYRQVWESCMGKPD SGMERTTAISSSKTGFNLIN LLLISLTGTPRPGCPGMTLP LQSTGRRLVMWHVTSSSAGT SQKL in isoform PLD1C.
VSP_005018
Alternative sequence585 – 62339SYFNH…RPHAD → N in isoform PLD1B.
VSP_005020
Alternative sequence598 – 1074477Missing in isoform PLD1C.
VSP_005019
Alternative sequence962 – 97110VVLGYLDDPS → SKMTPGVEDP in isoform PLD1D.
VSP_005021
Alternative sequence972 – 1074103Missing in isoform PLD1D.
VSP_005022
Natural variant491P → A.
Corresponds to variant rs9819927 [ dbSNP | Ensembl ].
VAR_034387
Natural variant6221A → S.
Corresponds to variant rs2290480 [ dbSNP | Ensembl ].
VAR_022056
Natural variant8201V → M.
Corresponds to variant rs2287579 [ dbSNP | Ensembl ].
VAR_022057
Natural variant10241V → I.
Corresponds to variant rs9827333 [ dbSNP | Ensembl ].
VAR_051703

Experimental info

Sequence conflict8321S → P in CAB76564. Ref.3

Sequences

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

Last modified November 1, 1997. Version 1.
Checksum: 734F285790A0BF7A

FASTA1,074124,184
        10         20         30         40         50         60 
MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK IQEVYIPFSA 

        70         80         90        100        110        120 
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI NLYTIELTHG EFKWQVKRKF 

       130        140        150        160        170        180 
KHFQEFHREL LKYKAFIRIP IPTRRHTFRR QNVREEPREM PSLPRSSENM IREEQFLGRR 

       190        200        210        220        230        240 
KQLEDYLTKI LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC 

       250        260        270        280        290        300 
CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID 

       310        320        330        340        350        360 
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA LAKWYVNAKG 

       370        380        390        400        410        420 
YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY 

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

       490        500        510        520        530        540 
DLAYGRWDDN EHRLTDVGSV KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PVQNLPIQKS 

       550        560        570        580        590        600 
IDDVDSKLKG IGKPRKFSKF SLYKQLHRHH LHDADSISSI DSTSSYFNHY RSHHNLIHGL 

       610        620        630        640        650        660 
KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC NFVFKDWVQL 

       670        680        690        700        710        720 
DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR WNFTKIMKSK YRSLSYPFLL 

       730        740        750        760        770        780 
PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE 

       790        800        810        820        830        840 
NQFFISCADD KVVFNKIGDA IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ 

       850        860        870        880        890        900 
AIMHFNYRTM CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL 

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

       970        980        990       1000       1010       1020 
RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI 

      1030       1040       1050       1060       1070 
NKPVLAKEDP IRAEEELKKI RGFLVQFPFY FLSEESLLPS VGTKEAIVPM EVWT 

« Hide

Isoform PLD1B [UniParc].

Checksum: 7AFA088570479777
Show »

FASTA1,036119,693
Isoform PLD1C [UniParc].

Checksum: BA03FFD5DD72AED7
Show »

FASTA59768,898
Isoform PLD1D [UniParc].

Checksum: 0B7F963953A48ECC
Show »

FASTA971112,184

References

« Hide 'large scale' references
[1]"Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family."
Hammond S.M., Altshuller Y.M., Sung T.-C., Rudge S.A., Rose K., Engebrecht J., Morris A.J., Frohman M.A.
J. Biol. Chem. 270:29640-29643(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1A).
[2]"Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha."
Hammond S.M., Jenco J.M., Nakashima S., Cadwallader K., Gu Q.-M., Cook S., Nozawa Y., Prestwich G.D., Frohman M.A., Morris A.J.
J. Biol. Chem. 272:3860-3868(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
[3]"Characterization of human PLD2 and the analysis of PLD isoform splice variants."
Steed P.M., Clark K.L., Boyar W.C., Lasala D.J.
FASEB J. 12:1309-1317(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A; PLD1B AND PLD1C).
Tissue: Brain, Cervix carcinoma, Chondrocyte and Skeletal muscle.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLD1A).
Tissue: Testis.
[5]"A novel human phospholipase D1 splice variant displays conserved regulation in vitro but altered localisation in vivo."
Hughes W.E., Parker P.J.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 739-1074 (ISOFORM PLD1D).
[6]"Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2."
Lopez I., Arnold R.S., Lambeth J.D.
J. Biol. Chem. 273:12846-12852(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity."
Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M., Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.
EMBO J. 19:5440-5449(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIP5K1B.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38545 mRNA. Translation: AAB49031.1.
BC068976 mRNA. Translation: AAH68976.1.
AJ276230 mRNA. Translation: CAB76564.1.
CCDSCCDS3216.1. [Q13393-1]
CCDS46957.1. [Q13393-2]
RefSeqNP_002653.1. NM_002662.4. [Q13393-1]
XP_005247590.1. XM_005247533.1. [Q13393-1]
XP_005247591.1. XM_005247534.1. [Q13393-2]
UniGeneHs.382865.

3D structure databases

ProteinModelPortalQ13393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111353. 18 interactions.
DIPDIP-40821N.
IntActQ13393. 4 interactions.
MINTMINT-141519.
STRING9606.ENSP00000342793.

Chemistry

BindingDBQ13393.
ChEMBLCHEMBL2536.
DrugBankDB00122. Choline.

PTM databases

PhosphoSiteQ13393.

Polymorphism databases

DMDM2499703.

Proteomic databases

MaxQBQ13393.
PaxDbQ13393.
PRIDEQ13393.

Protocols and materials databases

DNASU5337.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340989; ENSP00000340326; ENSG00000075651. [Q13393-4]
ENST00000342215; ENSP00000339936; ENSG00000075651. [Q13393-3]
ENST00000351298; ENSP00000342793; ENSG00000075651. [Q13393-1]
ENST00000356327; ENSP00000348681; ENSG00000075651. [Q13393-2]
GeneID5337.
KEGGhsa:5337.
UCSCuc003fhs.3. human. [Q13393-1]
uc003fht.3. human. [Q13393-2]

Organism-specific databases

CTD5337.
GeneCardsGC03M171318.
HGNCHGNC:9067. PLD1.
HPACAB004527.
HPA042396.
MIM602382. gene.
neXtProtNX_Q13393.
PharmGKBPA164742228.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1502.
HOGENOMHOG000246972.
HOVERGENHBG006650.
InParanoidQ13393.
KOK01115.
OMAEYSIISQ.
OrthoDBEOG7N63KT.
PhylomeDBQ13393.
TreeFamTF300589.

Enzyme and pathway databases

BRENDA3.1.4.4. 2681.
ReactomeREACT_111217. Metabolism.
REACT_6900. Immune System.
SignaLinkQ13393.

Gene expression databases

ArrayExpressQ13393.
BgeeQ13393.
CleanExHS_PLD1.
GenevestigatorQ13393.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.1520.10. 1 hit.
InterProIPR011993. 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]
PANTHERPTHR18896. PTHR18896. 1 hit.
PfamPF00169. PH. 1 hit.
PF00614. PLDc. 1 hit.
PF13091. PLDc_2. 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]
SUPFAMSSF64268. SSF64268. 1 hit.
PROSITEPS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLD1. human.
GeneWikiPhospholipase_D1.
GenomeRNAi5337.
NextBio20672.
PROQ13393.
SOURCESearch...

Entry information

Entry namePLD1_HUMAN
AccessionPrimary (citable) accession number: Q13393
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM