Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00211
Entry Name
UniProt Accession
Theoretical PI
7.44
Molecular Weight
106037.12
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Phospholipase D2
Protein Synonyms/Alias
PLD 2; rPLD2; 3.1.4.4; Choline phosphatase 2; PLD1C; Phosphatidylcholine-hydrolyzing phospholipase D2;
Gene Name
Pld2
Gene Synonyms/Alias
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
223
Canonical
HRVPGFTCCGRDQVC
[1]
S-Palmitoylation
224
Canonical
RVPGFTCCGRDQVCY
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Xie Z, Ho WT, Exton JH. Functional implications of post-translationalmodifications of phospholipases D1 and D2. Biochim Biophys Acta. 2002 Jan30;1580(1):9-21.[PMID:11923096]
Functional Description
May have a role in signal-induced cytoskeletal regulation and/or endocytosis.
Sequence Annotation
Domain: 65 195 PX.
Domain: 203 311 PH.
Domain: 437 464 PLD phosphodiesterase 1.
Domain: 751 778 PLD phosphodiesterase 2.
Region: 441 788 Catalytic.
Modified residue: 11 11 Phosphotyrosine.
Protein Length
933 AA.
Protein Sequence
(Canonical)
MTVTQTDLFP YGDYLNSSQL HMEPDVVDTL KEGEDPADRM HPFLAIYDLQ PLRAHPLVFA  60
PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT KKKFRHFQEL HRDLQRHKVL  120
MSLLNLARFA AAHSPAREAA NENIPSLPRG GSEGSARHTA SKQKYLENYL NRLLTMSFYR  180
NYHAMTEFLE VSQLSFIPDL GSKGLEGVIR KRSGGHRVPG FTCCGRDQVC YRWSKRWLVV  240
KDSFLLYMRP ETGAISFVQL FDPGFEVQVG KRSTEARYGV RIDTSHRSLI LKCSSYRQAR  300
WWGQEITELA QGPGRDFLQL HQHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAREEIF  360
ITDWWLSPEI YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL LFKEVELALG INSGYSKRTL  420
MLLHPNIKVM RHPDLVTLWA HHEKLLVVDQ AVAFLGGLDL AYGRWDDVQY RLTDLGDPSE  480
SADSQTPTPG SDPAATPDLS HNHFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW  540
RDVGVVVHGV AARDLARHFI QRWNFTKTIK ARYKIPQYPY LLPKSASTAN HLPFIIPGGQ  600
CATVQVLRSV DRWSAGTLES SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE  660
IVDRILKAHE QGQCFRVYVL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEYSILHR  720
LKAAMGTAWR DYMSICGLRT HGELGGHPIS ELIYIHSKLL IADDRTVIIG SANINDRSLL  780
GKRDSELAIL IKDTEMEPSL MDGVEYQAGR FALSLRGRCF SVILGANTWP DLDLRDPVCD  840
DFFQLWQETA ENNATIYEQI FRCLPSNATR SLRALREYVA VESLATVSPS LAQSELAHIR  900
GHLVHFPLKF LEDESLLPHW GAKRGMIPLE VWT                               933
FASTA
(Canonical)
>LipidDB-10116-00211|P70498
MTVTQTDLFPYGDYLNSSQLHMEPDVVDTLKEGEDPADRMHPFLAIYDLQPLRAHPLVFA
PGVPVIAQVVGTERYTSGSKVGTCTLYSVRLTHGDFTWTTKKKFRHFQELHRDLQRHKVL
MSLLNLARFAAAHSPAREAANENIPSLPRGGSEGSARHTASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGSKGLEGVIRKRSGGHRVPGFTCCGRDQVCYRWSKRWLVV
KDSFLLYMRPETGAISFVQLFDPGFEVQVGKRSTEARYGVRIDTSHRSLILKCSSYRQAR
WWGQEITELAQGPGRDFLQLHQHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAREEIF
ITDWWLSPEIYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRTL
MLLHPNIKVMRHPDLVTLWAHHEKLLVVDQAVAFLGGLDLAYGRWDDVQYRLTDLGDPSE
SADSQTPTPGSDPAATPDLSHNHFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGVAARDLARHFIQRWNFTKTIKARYKIPQYPYLLPKSASTANHLPFIIPGGQ
CATVQVLRSVDRWSAGTLESSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHEQGQCFRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYMSICGLRTHGELGGHPISELIYIHSKLLIADDRTVIIGSANINDRSLL
GKRDSELAILIKDTEMEPSLMDGVEYQAGRFALSLRGRCFSVILGANTWPDLDLRDPVCD
DFFQLWQETAENNATIYEQIFRCLPSNATRSLRALREYVAVESLATVSPSLAQSELAHIR
GHLVHFPLKFLEDESLLPHWGAKRGMIPLEVWT
Gene Ontology
GO:0005901; C:caveola; IDA:RGD
GO:0005794; C:Golgi apparatus; IDA:RGD
GO:0030027; C:lamellipodium; IDA:RGD
GO:0005634; C:nucleus; IDA:RGD
GO:0005886; C:plasma membrane; IDA:RGD
GO:0042383; C:sarcolemma; IDA:RGD
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; IDA:RGD
GO:0005080; F:protein kinase C binding; IPI:RGD
GO:0031175; P:neuron projection development; IMP:RGD
GO:0009395; P:phospholipid catabolic process; IMP:RGD
GO:0045785; P:positive regulation of cell adhesion; IMP:RGD
GO:0030335; P:positive regulation of cell migration; IMP:RGD
GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD
GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:RGD
GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:RGD
GO:0042542; P:response to hydrogen peroxide; IMP:RGD
GO:0001666; P:response to hypoxia; IDA:RGD
GO:0014070; P:response to organic cyclic compound; IDA:RGD
GO:0043434; P:response to peptide hormone; IMP:RGD
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; 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