CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014964
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D 
Protein Synonyms/Alias
 N-acyl phosphatidylethanolamine phospholipase D; NAPE-PLD; NAPE-hydrolyzing phospholipase D 
Gene Name
 NAPEPLD 
Gene Synonyms/Alias
 C7orf18 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73VNPWPTWKNPSIPNVubiquitination[1, 2]
97HSSVPSSKEELDKELubiquitination[2]
102SSKEELDKELPVLKPubiquitination[1]
296PAFEEIGKRFGPFDLubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of anandamide (N- arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors (By similarity). 
Sequence Annotation
 METAL 185 185 Zinc 1 (Potential).
 METAL 187 187 Zinc 1 (Potential).
 METAL 189 189 Zinc 2 (Potential).
 METAL 190 190 Zinc 2 (Potential).
 METAL 253 253 Zinc 1 (Potential).
 METAL 343 343 Zinc 2 (Potential).  
Keyword
 Complete proteome; Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Metal-binding; Phospholipid degradation; Phospholipid metabolism; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 393 AA 
Protein Sequence
MDENESNQSL MTSSQYPKEA VRKRQNSARN SGASDSSRFS RKSFKLDYRL EEDVTKSKKG 60
KDGRFVNPWP TWKNPSIPNV LRWLIMEKDH SSVPSSKEEL DKELPVLKPY FITNPEEAGV 120
REAGLRVTWL GHATVMVEMD ELIFLTDPIF SSRASPSQYM GPKRFRRSPC TISELPPIDA 180
VLISHNHYDH LDYNSVIALN ERFGNELRWF VPLGLLDWMQ KCGCENVIEL DWWEENCVPG 240
HDKVTFVFTP SQHWCKRTLM DDNKVLWGSW SVLGPWNRFF FAGDTGYCPA FEEIGKRFGP 300
FDLAAIPIGA YEPRWFMKYQ HVDPEEAVRI HTDVQTKKSM AIHWGTFALA NEHYLEPPVK 360
LNEALERYGL NAEDFFVLKH GESRYLNNDD ENF 393 
Gene Ontology
 GO:0042622; C:photoreceptor outer segment membrane; TAS:Reactome.
 GO:0070290; F:NAPE-specific phospholipase D activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR024884; NAPE-PLD. 
Pfam
  
SMART
  
PROSITE
  
PRINTS