Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00437
Entry Name
UniProt Accession
Theoretical PI
8.91
Molecular Weight
124184.13
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phospholipase D1
Protein Synonyms/Alias
PLD 1; hPLD1; 3.1.4.4; Choline phosphatase 1; Phosphatidylcholine-hydrolyzing phospholipase D1;
Gene Name
PLD1
Gene Synonyms/Alias
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
240
Canonical
HRIPGLNCCGQGRAC
[1][2]
S-Palmitoylation
241
Canonical
RIPGLNCCGQGRACY
[1][2]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Sugars JM, Cellek S, Manifava M, Coadwell J, Ktistakis NT. Hierarchy ofmembrane-targeting signals of phospholipase D1 involving lipid modification of a pleckstrin homology domain. J Biol Chem. 2002 Aug 9;277(32):29152-61. Epub 2002May 20.[PMID:12021265]
[2] Han JM, Kim Y, Lee JS, Lee CS, Lee BD, Ohba M, Kuroki T, Suh PG, Ryu SH.Localization of phospholipase D1 to caveolin-enriched membrane viapalmitoylation: implications for epidermal growth factor signaling. Mol BiolCell. 2002 Nov;13(11):3976-88.[PMID:12429840]
Functional Description
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).
Sequence Annotation
Domain: 81 212 PX.
Domain: 219 328 PH.
Domain: 459 486 PLD phosphodiesterase 1.
Domain: 891 918 PLD phosphodiesterase 2.
Region: 463 928 Catalytic.
Modified residue: 629 629 Phosphoserine.
Protein Length
1074 AA.
Protein Sequence
(Canonical)
MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK IQEVYIPFSA  60
IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI NLYTIELTHG EFKWQVKRKF  120
KHFQEFHREL LKYKAFIRIP IPTRRHTFRR QNVREEPREM PSLPRSSENM IREEQFLGRR  180
KQLEDYLTKI LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC  240
CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID  300
NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA LAKWYVNAKG  360
YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY  420
KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSTVYL WAHHEKLVII DQSVAFVGGI  480
DLAYGRWDDN EHRLTDVGSV KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PVQNLPIQKS  540
IDDVDSKLKG IGKPRKFSKF SLYKQLHRHH LHDADSISSI DSTSSYFNHY RSHHNLIHGL  600
KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC NFVFKDWVQL  660
DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR WNFTKIMKSK YRSLSYPFLL  720
PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE  780
NQFFISCADD KVVFNKIGDA IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ  840
AIMHFNYRTM CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL  900
IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FARGLRLQCF  960
RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI  1020
NKPVLAKEDP IRAEEELKKI RGFLVQFPFY FLSEESLLPS VGTKEAIVPM EVWT        1074
FASTA
(Canonical)
>LipidDB-9606-00437|Q13393
MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSA
IYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKF
KHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRR
KQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRID
NLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKG
YFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLY
KEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKS
IDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGL
KPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQL
DKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIE
NQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQ
AIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLL
IADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFI
NKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Gene Ontology
GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome
GO:0005768; C:endosome; IDA:MGI
GO:0005794; C:Golgi apparatus; IDA:MGI
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC
GO:0035091; F:phosphatidylinositol binding; IEA:InterPro
GO:0004630; F:phospholipase D activity; TAS:ProtInc
GO:0006935; P:chemotaxis; TAS:ProtInc
GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl
GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome
GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW
GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome
GO:0006655; P:phosphatidylglycerol biosynthetic process; TAS:Reactome
GO:0006644; P:phospholipid metabolic process; TAS:Reactome
GO:0007265; P:Ras protein signal transduction; TAS:ProtInc
GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc
GO:0044281; P:small molecule metabolic process; TAS:Reactome
Interpro
InterPro; IPR001849; PH_domain
InterPro; IPR011993; PH_like_dom
InterPro; IPR001683; Phox
InterPro; IPR025202; PLD-like_dom
InterPro; IPR001736; PLipase_D/transphosphatidylase
InterPro; IPR016555; PLipase_D_euk
InterPro; IPR015679; PLipase_D_fam
Pfam
Pfam; PF00169; PH;
Pfam; PF00614; PLDc;
Pfam; PF13091; PLDc_2;
Pfam; PF00787; PX;
SMART
SMART; SM00233; PH;
SMART; SM00155; PLDc;
SMART; SM00312; PX;
PROSITE
PROSITE; PS50035; PLD;
PROSITE; PS50195; PX;
PRINTS