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Identification
HMDB Protein ID HMDBP07303
Secondary Accession Numbers
  • 12925
Name N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
Synonyms
  1. N-acyl phosphatidylethanolamine phospholipase D
  2. NAPE-PLD
  3. NAPE-hydrolyzing phospholipase D
Gene Name NAPEPLD
Protein Type Unknown
Biological Properties
General Function Involved in metal ion binding
Specific Function 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).
Pathways
  • Retrograde endocannabinoid signaling
Reactions
An N-acylphosphatidylethanolamine + Water → an N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate details
GO Classification
Biological Process
phospholipid catabolic process
Cellular Component
membrane
Molecular Function
metal ion binding
NAPE-specific phospholipase D activity
zinc ion binding
Cellular Location
  1. Membrane
Gene Properties
Chromosome Location 7
Locus 7q22.1
SNPs NAPEPLD
Gene Sequence
>1182 bp
ATGGATGAAAATGAAAGCAACCAGTCTCTGATGACAAGCAGCCAATATCCTAAAGAAGCA
GTAAGAAAACGTCAAAATTCAGCACGGAATTCCGGAGCAAGTGATTCTTCTAGGTTTTCT
AGGAAAAGCTTCAAACTGGATTATAGACTAGAAGAAGATGTAACTAAATCCAAGAAAGGA
AAAGATGGGAGATTTGTGAATCCGTGGCCAACATGGAAAAACCCCTCTATTCCAAATGTT
CTCAGATGGCTGATAATGGAGAAAGATCACAGCAGTGTTCCAAGTTCTAAAGAGGAACTA
GACAAAGAACTCCCAGTGCTTAAGCCATATTTTATCACTAACCCTGAAGAAGCTGGAGTG
AGGGAAGCTGGCTTAAGAGTCACATGGCTGGGACATGCCACGGTAATGGTGGAAATGGAT
GAGCTCATATTTCTCACGGATCCCATCTTTAGCTCTCGTGCTTCACCATCGCAGTACATG
GGTCCAAAGCGATTTCGTCGTTCCCCGTGCACAATAAGTGAACTCCCTCCAATAGATGCG
GTCCTTATCAGTCACAACCACTATGACCATCTGGACTACAATTCTGTCATTGCTTTGAAT
GAGCGATTTGGTAATGAGTTGAGATGGTTTGTGCCTTTGGGTCTCCTTGACTGGATGCAA
AAATGTGGCTGTGAGAATGTGATTGAGTTGGACTGGTGGGAGGAGAATTGTGTCCCCGGA
CATGATAAGGTCACTTTTGTCTTTACACCTTCCCAGCACTGGTGTAAAAGGACTCTAATG
GATGACAACAAGGTGCTATGGGGCAGCTGGTCTGTCTTGGGGCCTTGGAATCGATTTTTT
TTCGCAGGAGATACTGGTTATTGCCCTGCTTTTGAAGAGATAGGAAAAAGATTTGGACCT
TTTGACCTTGCAGCTATTCCCATCGGAGCTTATGAACCGAGGTGGTTTATGAAATACCAG
CATGTAGACCCAGAAGAAGCTGTAAGGATTCACACTGATGTCCAAACAAAGAAATCTATG
GCAATTCACTGGGGAACTTTTGCCTTAGCAAATGAGCATTACTTAGAGCCTCCAGTGAAG
CTGAATGAAGCTCTAGAGAGATACGGACTTAACGCTGAAGATTTTTTTGTCTTGAAGCAT
GGAGAATCAAGATACCTAAATAATGATGATGAAAACTTTTAA
Protein Properties
Number of Residues 393
Molecular Weight 45595.15
Theoretical pI 6.059
Pfam Domain Function Not Available
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKG
KDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGV
REAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDA
VLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
HDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGP
FDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVK
LNEALERYGLNAEDFFVLKHGESRYLNNDDENF
GenBank ID Protein 38524476
UniProtKB/Swiss-Prot ID Q6IQ20
UniProtKB/Swiss-Prot Entry Name NAPEP_HUMAN
PDB IDs Not Available
GenBank Gene ID AB112352
GeneCard ID NAPEPLD
GenAtlas ID NAPEPLD
HGNC ID HGNC:21683
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  3. Okamoto Y, Morishita J, Tsuboi K, Tonai T, Ueda N: Molecular characterization of a phospholipase D generating anandamide and its congeners. J Biol Chem. 2004 Feb 13;279(7):5298-305. Epub 2003 Nov 21. [PubMed:14634025 ]
  4. Curtiss NP, Bonifas JM, Lauchle JO, Balkman JD, Kratz CP, Emerling BM, Green ED, Le Beau MM, Shannon KM: Isolation and analysis of candidate myeloid tumor suppressor genes from a commonly deleted segment of 7q22. Genomics. 2005 May;85(5):600-7. [PubMed:15820312 ]
  5. Wang J, Okamoto Y, Morishita J, Tsuboi K, Miyatake A, Ueda N: Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family. J Biol Chem. 2006 May 5;281(18):12325-35. Epub 2006 Mar 9. [PubMed:16527816 ]