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PLD1 (human)

Overview PLD1 a phosphatidylcholine-hydrolyzing phospholipase. Activated by ADP-ribosylated Rho and protein kinase C. Implicated as a critical step in numerous cellular pathways including membrane trafficking and the regulation polymorphonuclear leukocyte degranulation and oxidant production. May be involved in the regulation of perinuclear intravesicular membrane traffic. Four splice-variant isoforms have been described. Note: This description may include information from UniProtKB. Protein type: Lipid Metabolism - glycerophospholipid; EC 3.1.4.4; Phospholipase; Lipid Metabolism - ether lipid; Motility/polarity/chemotaxis Cellular Component: Golgi membrane; Golgi apparatus; Golgi cisterna; endoplasmic reticulum membrane; membrane; late endosome membrane; perinuclear region of cytoplasm; lamellipodium; endosome; vesicle Molecular Function: phospholipase D activity; phosphoinositide binding Biological Process: response to peptide hormone stimulus; defense response to Gram-positive bacterium; phosphatidylglycerol biosynthetic process; phospholipid catabolic process; phospholipid metabolic process; small GTPase mediated signal transduction; Ras protein signal transduction; glycerophospholipid biosynthetic process; phosphatidic acid biosynthetic process; chemotaxis; positive regulation of cell migration Reference #:  Q13393 (UniProtKB) Alt. Names/Synonyms: Choline phosphatase 1; hPLD1; Phosphatidylcholine-hydrolyzing phospholipase D1; Phospholipase D1; phospholipase D1, phophatidylcholine-specific; phospholipase D1, phosphatidylcholine-specific; PLD 1; PLD1 Gene Symbols: PLD1 Molecular weight: 124,184 Da Basal Isoelectric point: 8.91  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PLD1

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	Sites Implicated In
enzymatic activity, induced: S505‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human ► Hide Isoforms
4	0		S2	______MSLKNEPRV
0	5		Y42-p	FEGEEVDyDVsPSDP
0	1		S45-p	EEVDyDVsPSDPKIQ
5	0		T147	PIPTRRHTFRRQNVR
0	2		K189-u	QLEDYLTkILKMPMY
1	0		C240	HRIPGLNCCGQGRAC
1	0		C241	RIPGLNCCGQGRACY
0	1		S431-p	ELALGINsEyTKRTL
0	1		Y433-p	ALGINsEyTKRTLMR
0	1		T495-p	DDNEHRLtDVGSVKR
1	1		S505-p	GSVKRVTsGPsLGSL
0	1		S508-p	KRVTsGPsLGSLPPA
0	1		Q538	PVQNLPIQKSIDDVD
3	0		S561	PRKFSKFSLYKQLHR
0	1		S579	HDADSISSIDSTSSy
0	1		S582	DSISSIDSTSSyFNH
0	1		Y586-p	SIDSTSSyFNHyRSH
0	2		Y590-p	TSSyFNHyRSHHNLI
1	0		S610-p	HFKLFHPssESEQGL
1	0		S611-p	FKLFHPssESEQGLT
0	1		S629-p	ADTGSIRsLQTGVGE
0	1		Y711-p	TKIMKSKyRSLSYPF
0	1		K796	DDKVVFNKIGDAIAQ
0	1		K807-a	AIAQRILkAHRENQK
0	1		K807	AIAQRILKAHRENQK
0	1		K1000-u	RNATIYDkVFRCLPN

	PLD1 iso2
S2-p	______MsLKNEPRV
Y42	FEGEEVDYDVSPSDP
S45	EEVDYDVSPSDPKIQ
T147-p	PIPTRRHtFRRQNVR
K189	QLEDYLTKILKMPMY
C240	HRIPGLNCCGQGRAC
C241	RIPGLNCCGQGRACY
S431	ELALGINSEYTKRTL
Y433	ALGINSEYTKRTLMR
T495	DDNEHRLTDVGSVKR
S505	GSVKRVTSGPSLGSL
S508	KRVTSGPSLGSLPPA
Q538	PVQNLPIQKSIDDVD
S561	PRKFSKFSLYKQLHR
S579	HDADSISSIDSTSNT
S582	DSISSIDSTSNTGSI
-	gap
-	gap
-	gap
-	gap
S591	SNTGSIRSLQTGVGE
Y673	TKIMKSKYRSLSYPF
K758	DDKVVFNKIGDAIAQ
K769-a	AIAQRILkAHRENQK
K769	AIAQRILKAHRENQK
K962	RNATIYDKVFRCLPN

	mouse ► Hide Isoforms
S2	______MSLKSETRV
Y42	FEGEEVEYDASPGDP
S45	EEVEYDASPGDPKAQ
T147	PIPTKRHTFRRQNVK
K189-u	QLEDYLTkILKMPMY
C240	HRIPGVNCCGHGRAC
C241	RIPGVNCCGHGRACY
S431	ELALGINSEYSKRTL
Y433	ALGINSEYSKRTLMR
T495	DDNEHRLTDVGSVKR
S505	GSVKRVTSGLSLGSL
S508	KRVTSGLSLGSLTAA
S538-p	FHKKEPIsKIVDETD
S561	SRKFSKFSLYRQLHR
S579	HNADSISSIDSTSSY
S582	DSISSIDSTSSYFSH
Y586	SIDSTSSYFSHCRSH
C590	TSSYFSHCRSHQNLI
S610	HLKLFHPSSESEQGL
S611	LKLFHPSSESEQGLT
S629-p	TDTGSIRsVQTGVGE
Y711	TKIMKPKYRSLSYPF
K796-u	DDKVVFNkVGDRIAQ
K807	RIAQRILKAHREGQR
K807-u	RIAQRILkAHREGQR
K1000	RNATIYDKVFRCLPN

	PLD1 iso2
S2	______MSLKSETRV
Y42	FEGEEVEYDASPGDP
S45	EEVEYDASPGDPKAQ
T147	PIPTKRHTFRRQNVK
K189	QLEDYLTKILKMPMY
C240	HRIPGVNCCGHGRAC
C241	RIPGVNCCGHGRACY
S431	ELALGINSEYSKRTL
Y433	ALGINSEYSKRTLMR
T495	DDNEHRLTDVGSVKR
S505	GSVKRVTSGLSLGSL
S508	KRVTSGLSLGSLTAA
S538	FHKKEPISKIVDETD
S561	SRKFSKFSLYRQLHR
S579-p	HNADSISsIDsTSNT
S582-p	DSISsIDsTSNTGSI
-	gap
-	gap
-	gap
-	gap
S591	SNTGSIRSVQTGVGE
Y673	TKIMKPKYRSLSYPF
K758	DDKVVFNKVGDRIAQ
K769	RIAQRILKAHREGQR
K769	RIAQRILKAHREGQR
K962	RNATIYDKVFRCLPN

	rat ► Hide Isoforms
S2-p	______MsLRSEARV
Y42	FEGEEVEYDASPGDP
S45	EEVEYDASPGDPTAQ
T147-p	PIPTKRHtFRRQNVK
K189	QLEDYLTKILKMPMY
C240-h	HRIPGVNccGHGRAC
C241-h	RIPGVNccGHGRACY
S431	ELALGINSEYTKRTL
Y433	ALGINSEYTKRTLMR
T495	DDNEHRLTDVGSVKR
S505	GSVKRVTSGQSLGSL
S508	KRVTSGQSLGSLTAA
L538	SHKNEPVLKSVNDTD
S561-p	SRKFSKFsLYRQLHR
S579	HNSDSISSVDSASSY
S582	DSISSVDSASSYFNH
Y586	SVDSASSYFNHYRSH
Y590	ASSYFNHYRSHQNLI
S610	HLKLFRPSSESEQGL
S611	LKLFRPSSESEQGLT
S629	ADTGSIRSVQTGVGE
Y711	TKIMKPKYRSLSYPF
K796	DDKVVFNKVGNAIAQ
K807	AIAQRILKAHREGQR
K807	AIAQRILKAHREGQR
K1000	RNATIYDKVFRCLPN

	PLD1 iso2
S2-p	______MsLRSEARV
Y42	FEGEEVEYDASPGDP
S45	EEVEYDASPGDPTAQ
T147-p	PIPTKRHtFRRQNVK
K189	QLEDYLTKILKMPMY
C240	HRIPGVNCCGHGRAC
C241	RIPGVNCCGHGRACY
S431	ELALGINSEYTKRTL
Y433	ALGINSEYTKRTLMR
T495	DDNEHRLTDVGSVKR
S505	GSVKRVTSGQSLGSL
S508	KRVTSGQSLGSLTAA
L538	SHKNEPVLKSVNDTD
S561-p	SRKFSKFsLYRQLHR
S579	HNSDSISSVDSASNT
S582	DSISSVDSASNTGSI
-	gap
-	gap
-	gap
-	gap
S591	SNTGSIRSVQTGVGE
Y673	TKIMKPKYRSLSYPF
K758	DDKVVFNKVGNAIAQ
K769	AIAQRILKAHREGQR
K769	AIAQRILKAHREGQR
K962	RNATIYDKVFRCLPN

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