Reviewed, UniProtKB/Swiss-Prot Q9Z280 (PLD1_MOUSE)

Names and origin

Protein names

Recommended name:
    Phospholipase D1
      Short name=PLD 1
      Short name=mPLD1
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 1
    Phosphatidylcholine-hydrolyzing phospholipase D1

Gene names

Name:

Pld1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1074 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 structure	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 Ref.3.
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.
Involvement in 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.
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
Cellular component	Cytoplasm Endoplasmic reticulum Endosome Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Hydrolase
PTM	Lipoprotein Palmitate Phosphoprotein
Gene Ontology (GO)
Biological process	cell communication Inferred from electronic annotation. Source: InterPro defense response to Gram-positive bacterium Inferred from mutant phenotype. Source: MGI
Cellular component	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 perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phosphoinositide binding Inferred from electronic annotation. Source: InterPro phospholipase D activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform PLD1A (identifier: Q9Z280-1)

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: Q9Z280-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1074	1074	Phospholipase D1		PRO_0000218803
Regions
	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
Amino acid modifications
	Modified residue	538	1	Phosphoserine Ref.4
	Modified residue	629	1	Phosphoserine Ref.5
	Lipidation	240	1	S-palmitoyl cysteine By similarity
	Lipidation	241	1	S-palmitoyl cysteine By similarity
Natural variations
	Alternative sequence	585 – 623	39	SYFSH…RHSTD → N in isoform PLD1B.		VSP_005023
Experimental info
	Sequence conflict	71 – 74	4	NIQT → QHPD in AAB81245. Ref.1
	Sequence conflict	574	1	A → V in AAB81245. Ref.1
	Sequence conflict	675	1	R → G in AAB81245. Ref.1
	Sequence conflict	781	1	N → I in AAB81245. Ref.1
	Sequence conflict	876	1	C → V in AAB81245. Ref.1
	Sequence conflict	990	1	T → A in AAB81245. Ref.1
	Sequence conflict	1071 – 1073	3	EVW → SLT Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform PLD1A [UniParc]. Last modified May 1, 1999. Version 1. Checksum: E11260982A217280	FASTA	1,074	123,969
	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
	Isoform PLD1B. Checksum: 39AFFFE7032D487A	FASTA	1,036	119,588
	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 DSTSNTGSIR SVQTGVGELH 610 620 630 640 650 660 GETRFWHGKD YCNFVFKDWV QLDKPFADFI DRYSTPRMPW HDIGSVVHGK AARDVARHFI 670 680 690 700 710 720 QRWNFTKIMK PKYRSLSYPF LLPKSQATAH ELRYQVPGAV PAKVQLLRSA ADWSAGIKHH 730 740 750 760 770 780 EESIHAAYIH VIENSKHYIY IENQFFISCA DDKVVFNKVG DRIAQRILKA HREGQRYRVY 790 800 810 820 830 840 IVIPLLPGFE GDISTGGGNA LQAIMHFNYR TMCRGESSIL EQLKPELGNK WINYISFCGL 850 860 870 880 890 900 RTHAELEGNL VTELIYVHSK LLIADDNTVI IGSANINDRS MLGKRDSEMA VIVQDTETVP 910 920 930 940 950 960 SVMDGKEYQA GRFARDLRLE CFRLVLGYLS DPSEDLQDPV SDKFFKEIWV STAARNATIY 970 980 990 1000 1010 1020 DKVFRCLPND EVHNLIQLRD FINKPILAKE DALRAEEELR KIRGFLVQFP LYFLSEENLL 1030 PSVGTKEAIV PMEVWT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 9307024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B). Strain: 129. Tissue: Embryonic brain and Neonatal brain.
[2]	"Genomic analysis of murine phospholipase D1 and comparison to phospholipase D2 reveals an unusual difference in gene size." Redina O.E., Frohman M.A. Gene 222:53-60(1998) [PubMed: 9813240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PLD1A). Strain: 129.
[3]	"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: 9395408] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U87868 mRNA. Translation: AAB81245.1. AF083497 , AF083475, AF083476, AF083478, AF083479, AF083480, AF083481, AF083483, AF083484, AF083485, AF083486, AF083488, AF083489, AF083490, AF083492, AF083494, AF083495, AF083496 Genomic DNA. Translation: AAC84041.1.
IPI	IPI00130629. IPI00229888.
PIR	T17203. T42093.
UniGene	Mm.212039
3D structure databases
SMR	Q9Z280. Positions 98-211.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z280.
PTM databases
PhosphoSite	Q9Z280.
Proteomic databases
PRIDE	Q9Z280.
Genome annotation databases
Ensembl	ENSMUST00000067776; ENSMUSP00000066634; ENSMUSG00000027695; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:109585. Pld1.
Phylogenomic databases
eggNOG	roNOG09371.
HOGENOM	HBG590223.
HOVERGEN	Q9Z280.
InParanoid	Q9Z280.
Enzyme and pathway databases
BRENDA	3.1.4.4. 244.
Gene expression databases
ArrayExpress	Q9Z280.
Bgee	Q9Z280.
CleanEx	MM_PLD1.
Genevestigator	Q9Z280.
GermOnline	ENSMUSG00000027695. Mus musculus.
Family and domain databases
InterPro	IPR011993. PH_type. IPR015679. Phospholipase_D. IPR001849. Pleckstrin_homology. IPR001736. PLipase_D/transphosphatidylase. IPR016555. PLipase_D_euk. IPR001683. PX. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:3.30.1520.10. PX. 1 hit.
PANTHER	PTHR18896. Phospholipase_D. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00614. PLDc. 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]
PROSITE	PS50003. PH_DOMAIN. 1 hit. PS50035. PLD. 2 hits. PS50195. PX. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

PLD1_MOUSE

Accession

Primary (citable) accession number: Q9Z280
Secondary accession number(s): O35911

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 1999
Last modified:	February 9, 2010
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)