ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9Z280


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PLD1_MOUSE
Primary accession number Q9Z280
Secondary accession number O35911
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Phospholipase D1
Synonyms PLD 1
mPLD1
EC 3.1.4.4
Choline phosphatase 1
Phosphatidylcholine-hydrolyzing phospholipase D1
Gene name
Name: Pld1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
STRAIN=129;
TISSUE=Embryonic brain, and Neonatal brain;
PubMed=9307024 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Cloning and expression analysis of murine phospholipase D1.";
Biochem. J. 326:745-753(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PLD1A).
STRAIN=129;
DOI=10.1016/S0378-1119(98)00465-X; PubMed=9813240 [NCBI, ExPASy, EBI, Israel, Japan]
Redina O.E., Frohman M.A.;
"Genomic analysis of murine phospholipase D1 and comparison to phospholipase D2 reveals an unusual difference in gene size.";
Gene 222:53-60(1998).
[3]
SUBCELLULAR LOCATION.
DOI=10.1016/S0960-9822(97)70090-3; PubMed=9395408 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization.";
Curr. Biol. 7:191-201(1997).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).
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.
  • 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.
  • SUBUNIT: Interacts with PIP5K1A (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side (Potential). Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side (Potential). Late endosome membrane; Lipid-anchor; Cytoplasmic side (Potential).
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NamePLD1A
    Isoform IDQ9Z280-1
    This is the isoform sequence displayed in this entry.
    NamePLD1B
    Isoform IDQ9Z280-2
    Features which should be applied to build the isoform sequence: VSP_005023.
  • TISSUE SPECIFICITY: Expressed in kidney, lung, and at a much lower levels, in brain, liver, heart, testis and spleen.
  • DEVELOPMENTAL STAGE: Expressed most strikingly in selected ventricular cells lining the spinal cord and brain. The level of expression decreases dramatically as the cells differentiate into neurons and migrate to the outer layer of the spinal cord and brain. Expression is observed during development in a restricted region of the nasal neuroepithelium.
  • DISEASE: Defects in Pld1 may result in coa which is associated with coat color dilution and white spotting. It is also associated with platelet-storage pool deficiency characterized by decreased levels in serotonin and dense granules.
  • SIMILARITY: Belongs to the phospholipase D family.
  • SIMILARITY: Contains 1 PH domain.
  • SIMILARITY: Contains 2 PLD phosphodiesterase domains.
  • SIMILARITY: Contains 1 PX (phox homology) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U87868; AAB81245.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083497; AAC84041.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083475; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083476; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083478; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083479; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083480; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083481; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083483; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083484; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083485; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083486; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083488; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083489; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083490; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083492; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083494; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083495; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083496; AAC84041.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T17203; T17203.
T42093; T42093.
UniGene Mm.212039
3D structure databases
ModBase Q9Z280.
PTM databases
PhosphoSite Q9Z280; -.
Organism-specific databases
MGI MGI:109585; Pld1.
Gene expression databases
ArrayExpress Q9Z280; -.
CleanEx MM_PLD1; -.
GermOnline ENSMUSG00000027695; Mus musculus.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000139; Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031902; Cellular component: late endosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0035091; Molecular function: phosphoinositide binding (inferred from electronic annotation from InterPro).
GO:0004630; Molecular function: phospholipase D activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0007154; Biological process: cell communication (inferred from electronic annotation from InterPro).
GO:0050830; Biological process: defense response to Gram-positive bacterium (inferred from mutant phenotype from MGI).
GO:0016042; Biological process: lipid catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001849; PH.
IPR011993; PH_type.
IPR015679; Phospholipase_D.
IPR001736; PLD.
IPR016555; PLipase_D_euk.
IPR001683; PX.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
G3DSA:3.30.1520.10; PX; 1.
PANTHER PTHR18896; Phospholipase_D; 1.
Pfam PF00169; PH; 1.
PF00614; PLDc; 2.
PF00787; PX; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF009376; Phospholipase_D_euk; 1.
SMART SM00233; PH; 1.
SM00155; PLDc; 2.
SM00312; PX; 1.
SMART graphical view of domain structure.
PROSITE PS50003; PH_DOMAIN; 1.
PS50035; PLD; 2.
PS50195; PX; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Z280.
Genome annotation databases
Ensembl ENSMUSG00000027695; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM Q9Z280; -.
HOVERGEN Q9Z280; -.
Other
SOURCE Pld1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cytoplasm; Endoplasmic reticulum; Endosome; Golgi apparatus; Hydrolase; Lipid degradation; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1074  1074     Phospholipase D1. PRO_0000218803
DOMAIN   81    212  132     PX. 
DOMAIN   219    328  110     PH. 
DOMAIN   459    486  28     PLD phosphodiesterase 1. 
DOMAIN   891    918  28     PLD phosphodiesterase 2. 
REGION   463    928  466     Catalytic. 
MOD_RES   538    538        Phosphoserine. 
MOD_RES   629    629        Phosphoserine (By similarity). 
LIPID   240    240        S-palmitoyl cysteine (By similarity). 
LIPID   241    241        S-palmitoyl cysteine (By similarity). 
VAR_SEQ   585    623        SYFSHCRSHQNLIHGLKPHLKLFHPSSESEQGLTRHSTD -> N (in isoform PLD1B). VSP_005023
CONFLICT   71     74        NIQT -> QHPD (in Ref. 1; AAB81245). 
CONFLICT   574    574        A -> V (in Ref. 1; AAB81245). 
CONFLICT   675    675        R -> G (in Ref. 1; AAB81245). 
CONFLICT   781    781        N -> I (in Ref. 1; AAB81245). 
CONFLICT   876    876        C -> V (in Ref. 1; AAB81245). 
CONFLICT   990    990        T -> A (in Ref. 1; AAB81245). 
CONFLICT   1071   1073        EVW -> SLT (in Ref. 1). 
Sequence information
Length: 1074 AA [This is the length of the unprocessed precursor] Molecular weight: 123969 Da [This is the MW of the unprocessed precursor] CRC64: E11260982A217280 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLKSETRVN TSTLQKIAAD MSNLIENLDT RELHFEGEEV EYDASPGDPK AQEGCIPFSS 

        70         80         90        100        110        120 
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTSRVPSI 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 EFRVKVGRKE TETKYGLRID 

       310        320        330        340        350        360 
NLSRTLILKC NSYRHARWWG GAIEEFIRKH GADFLKDHRF GSYAALHENT LAKWYVNAKG 

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

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

       490        500        510        520        530        540 
DLAYGRWDDN EHRLTDVGSV KRVTSGLSLG SLTAASVESM ESLSLKDKHE FHKKEPISKI 

       550        560        570        580        590        600 
VDETDMKLKG IGKSRKFSKF SLYRQLHRHH LHNADSISSI DSTSSYFSHC RSHQNLIHGL 

       610        620        630        640        650        660 
KPHLKLFHPS SESEQGLTRH STDTGSIRSV QTGVGELHGE TRFWHGKDYC NFVFKDWVQL 

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

       730        740        750        760        770        780 
PKSQATAHEL RYQVPGAVPA KVQLLRSAAD WSAGIKHHEE SIHAAYIHVI ENSKHYIYIE 

       790        800        810        820        830        840 
NQFFISCADD KVVFNKVGDR 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 FARDLRLECF 

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

      1030       1040       1050       1060       1070 
NKPILAKEDA LRAEEELRKI RGFLVQFPLY FLSEENLLPS VGTKEAIVPM EVWT 

Q9Z280 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!