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Q13393

- PLD1_HUMAN

UniProt

Q13393 - PLD1_HUMAN

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Protein

Phospholipase D1

Gene
PLD1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

A phosphatidylcholine + H2O = choline + a phosphatidate.

Enzyme regulationi

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.

GO - Molecular functioni

  1. N-acylphosphatidylethanolamine-specific phospholipase D activity Source: UniProtKB-EC
  2. phosphatidylinositol binding Source: InterPro
  3. phospholipase D activity Source: ProtInc
  4. protein binding Source: IntAct

GO - Biological processi

  1. chemotaxis Source: ProtInc
  2. defense response to Gram-positive bacterium Source: Ensembl
  3. glycerophospholipid biosynthetic process Source: Reactome
  4. lipid catabolic process Source: UniProtKB-KW
  5. phosphatidic acid biosynthetic process Source: Reactome
  6. phosphatidylglycerol biosynthetic process Source: Reactome
  7. phospholipid metabolic process Source: Reactome
  8. Ras protein signal transduction Source: ProtInc
  9. small GTPase mediated signal transduction Source: ProtInc
  10. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.4.4. 2681.
ReactomeiREACT_120906. Synthesis of PA.
REACT_121280. Synthesis of PG.
REACT_160158. Role of phospholipids in phagocytosis.
SignaLinkiQ13393.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase D1 (EC:3.1.4.4)
Short name:
PLD 1
Short name:
hPLD1
Alternative name(s):
Choline phosphatase 1
Phosphatidylcholine-hydrolyzing phospholipase D1
Gene namesi
Name:PLD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9067. PLD1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. endosome Source: MGI
  3. Golgi apparatus Source: MGI
  4. Golgi membrane Source: UniProtKB-SubCell
  5. late endosome membrane Source: UniProtKB-SubCell
  6. lysosomal membrane Source: UniProtKB
  7. membrane Source: ProtInc
  8. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164742228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10741074Phospholipase D1PRO_0000218802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi240 – 2401S-palmitoyl cysteine By similarity
Lipidationi241 – 2411S-palmitoyl cysteine By similarity
Modified residuei629 – 6291Phosphoserine1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ13393.
PaxDbiQ13393.
PRIDEiQ13393.

PTM databases

PhosphoSiteiQ13393.

Expressioni

Tissue specificityi

Expressed abundantly in the pancreas and heart and at high levels in brain, placenta, spleen, uterus and small intestine.1 Publication

Gene expression databases

ArrayExpressiQ13393.
BgeeiQ13393.
CleanExiHS_PLD1.
GenevestigatoriQ13393.

Organism-specific databases

HPAiCAB004527.
HPA042396.

Interactioni

Subunit structurei

Interacts with PIP5K1B.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CFL1P235284EBI-2827556,EBI-352733

Protein-protein interaction databases

BioGridi111353. 17 interactions.
DIPiDIP-40821N.
IntActiQ13393. 4 interactions.
MINTiMINT-141519.
STRINGi9606.ENSP00000342793.

Structurei

3D structure databases

ProteinModelPortaliQ13393.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 212132PXAdd
BLAST
Domaini219 – 328110PHAdd
BLAST
Domaini459 – 48628PLD phosphodiesterase 1Add
BLAST
Domaini891 – 91828PLD phosphodiesterase 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni463 – 928466CatalyticAdd
BLAST

Sequence similaritiesi

Belongs to the phospholipase D family.
Contains 1 PH domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1502.
HOGENOMiHOG000246972.
HOVERGENiHBG006650.
InParanoidiQ13393.
KOiK01115.
OMAiEYSIISQ.
OrthoDBiEOG7N63KT.
PhylomeDBiQ13393.
TreeFamiTF300589.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.1520.10. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001683. Phox.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
IPR015679. PLipase_D_fam.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00614. 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]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform PLD1A (identifier: Q13393-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK     50
IQEVYIPFSA IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI 100
NLYTIELTHG EFKWQVKRKF KHFQEFHREL LKYKAFIRIP IPTRRHTFRR 150
QNVREEPREM PSLPRSSENM IREEQFLGRR KQLEDYLTKI LKMPMYRNYH 200
ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC CGQGRACYRW 250
SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID 300
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA 350
LAKWYVNAKG YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR 400
LDCILKRKAQ QGVRIFIMLY KEVELALGIN SEYTKRTLMR LHPNIKVMRH 450
PDHVSSTVYL WAHHEKLVII DQSVAFVGGI DLAYGRWDDN EHRLTDVGSV 500
KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PVQNLPIQKS IDDVDSKLKG 550
IGKPRKFSKF SLYKQLHRHH LHDADSISSI DSTSSYFNHY RSHHNLIHGL 600
KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC 650
NFVFKDWVQL DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR 700
WNFTKIMKSK YRSLSYPFLL PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD 750
WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE NQFFISCADD KVVFNKIGDA 800
IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ AIMHFNYRTM 850
CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL 900
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR 950
FARGLRLQCF RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK 1000
VFRCLPNDEV HNLIQLRDFI NKPVLAKEDP IRAEEELKKI RGFLVQFPFY 1050
FLSEESLLPS VGTKEAIVPM EVWT 1074
Length:1,074
Mass (Da):124,184
Last modified:November 1, 1997 - v1
Checksum:i734F285790A0BF7A
GO
Isoform PLD1B (identifier: Q13393-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     585-623: SYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHAD → N

Show »
Length:1,036
Mass (Da):119,693
Checksum:i7AFA088570479777
GO
Isoform PLD1C (identifier: Q13393-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     514-597: PAAMESMESL...NHYRSHHNLI → IPGPSVVYRQ...SSSAGTSQKL
     598-1074: Missing.

Show »
Length:597
Mass (Da):68,898
Checksum:iBA03FFD5DD72AED7
GO
Isoform PLD1D (identifier: Q13393-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:971
Mass (Da):112,184
Checksum:i0B7F963953A48ECC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491P → A.
Corresponds to variant rs9819927 [ dbSNP | Ensembl ].
VAR_034387
Natural varianti622 – 6221A → S.
Corresponds to variant rs2290480 [ dbSNP | Ensembl ].
VAR_022056
Natural varianti820 – 8201V → M.
Corresponds to variant rs2287579 [ dbSNP | Ensembl ].
VAR_022057
Natural varianti1024 – 10241V → I.
Corresponds to variant rs9827333 [ dbSNP | Ensembl ].
VAR_051703

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei514 – 59784PAAME…HHNLI → IPGPSVVYRQVWESCMGKPD SGMERTTAISSSKTGFNLIN LLLISLTGTPRPGCPGMTLP LQSTGRRLVMWHVTSSSAGT SQKL in isoform PLD1C. VSP_005018Add
BLAST
Alternative sequencei585 – 62339SYFNH…RPHAD → N in isoform PLD1B. VSP_005020Add
BLAST
Alternative sequencei598 – 1074477Missing in isoform PLD1C. VSP_005019Add
BLAST
Alternative sequencei962 – 97110VVLGYLDDPS → SKMTPGVEDP in isoform PLD1D. VSP_005021
Alternative sequencei972 – 1074103Missing in isoform PLD1D. VSP_005022Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti832 – 8321S → P in CAB76564. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38545 mRNA. Translation: AAB49031.1.
BC068976 mRNA. Translation: AAH68976.1.
AJ276230 mRNA. Translation: CAB76564.1.
CCDSiCCDS3216.1. [Q13393-1]
CCDS46957.1. [Q13393-2]
RefSeqiNP_002653.1. NM_002662.4. [Q13393-1]
XP_005247590.1. XM_005247533.1. [Q13393-1]
XP_005247591.1. XM_005247534.1. [Q13393-2]
UniGeneiHs.382865.

Genome annotation databases

EnsembliENST00000340989; ENSP00000340326; ENSG00000075651. [Q13393-4]
ENST00000342215; ENSP00000339936; ENSG00000075651. [Q13393-3]
ENST00000351298; ENSP00000342793; ENSG00000075651. [Q13393-1]
ENST00000356327; ENSP00000348681; ENSG00000075651. [Q13393-2]
GeneIDi5337.
KEGGihsa:5337.
UCSCiuc003fhs.3. human. [Q13393-1]
uc003fht.3. human. [Q13393-2]

Polymorphism databases

DMDMi2499703.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Phospholipase D entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38545 mRNA. Translation: AAB49031.1 .
BC068976 mRNA. Translation: AAH68976.1 .
AJ276230 mRNA. Translation: CAB76564.1 .
CCDSi CCDS3216.1. [Q13393-1 ]
CCDS46957.1. [Q13393-2 ]
RefSeqi NP_002653.1. NM_002662.4. [Q13393-1 ]
XP_005247590.1. XM_005247533.1. [Q13393-1 ]
XP_005247591.1. XM_005247534.1. [Q13393-2 ]
UniGenei Hs.382865.

3D structure databases

ProteinModelPortali Q13393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111353. 17 interactions.
DIPi DIP-40821N.
IntActi Q13393. 4 interactions.
MINTi MINT-141519.
STRINGi 9606.ENSP00000342793.

Chemistry

BindingDBi Q13393.
ChEMBLi CHEMBL2536.
DrugBanki DB00122. Choline.

PTM databases

PhosphoSitei Q13393.

Polymorphism databases

DMDMi 2499703.

Proteomic databases

MaxQBi Q13393.
PaxDbi Q13393.
PRIDEi Q13393.

Protocols and materials databases

DNASUi 5337.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340989 ; ENSP00000340326 ; ENSG00000075651 . [Q13393-4 ]
ENST00000342215 ; ENSP00000339936 ; ENSG00000075651 . [Q13393-3 ]
ENST00000351298 ; ENSP00000342793 ; ENSG00000075651 . [Q13393-1 ]
ENST00000356327 ; ENSP00000348681 ; ENSG00000075651 . [Q13393-2 ]
GeneIDi 5337.
KEGGi hsa:5337.
UCSCi uc003fhs.3. human. [Q13393-1 ]
uc003fht.3. human. [Q13393-2 ]

Organism-specific databases

CTDi 5337.
GeneCardsi GC03M171318.
HGNCi HGNC:9067. PLD1.
HPAi CAB004527.
HPA042396.
MIMi 602382. gene.
neXtProti NX_Q13393.
PharmGKBi PA164742228.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1502.
HOGENOMi HOG000246972.
HOVERGENi HBG006650.
InParanoidi Q13393.
KOi K01115.
OMAi EYSIISQ.
OrthoDBi EOG7N63KT.
PhylomeDBi Q13393.
TreeFami TF300589.

Enzyme and pathway databases

BRENDAi 3.1.4.4. 2681.
Reactomei REACT_120906. Synthesis of PA.
REACT_121280. Synthesis of PG.
REACT_160158. Role of phospholipids in phagocytosis.
SignaLinki Q13393.

Miscellaneous databases

ChiTaRSi PLD1. human.
GeneWikii Phospholipase_D1.
GenomeRNAii 5337.
NextBioi 20672.
PROi Q13393.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13393.
Bgeei Q13393.
CleanExi HS_PLD1.
Genevestigatori Q13393.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.1520.10. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001683. Phox.
IPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
IPR015679. PLipase_D_fam.
[Graphical view ]
PANTHERi PTHR18896. PTHR18896. 1 hit.
Pfami PF00169. PH. 1 hit.
PF00614. PLDc. 1 hit.
PF13091. PLDc_2. 1 hit.
PF00787. PX. 1 hit.
[Graphical view ]
PIRSFi PIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTi SM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF64268. SSF64268. 1 hit.
PROSITEi PS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiPLD1_HUMAN
AccessioniPrimary (citable) accession number: Q13393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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