Q6IQ20 (NAPEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
Short name=N-acyl phosphatidylethanolamine phospholipase D
Short name=NAPE-PLD
Short name=NAPE-hydrolyzing phospholipase D
EC=3.1.4.54

Gene names

Name:	NAPEPLD
Synonyms:	C7orf18

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Catalytic activity	An N-acylphosphatidylethanolamine + H2O = an N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate.
Cofactor	Binds 1 or 2 zinc ions per subunit By similarity.
Enzyme regulation	Activity is stimulated by divalent cations By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Membrane By similarity.
Sequence similarities	Belongs to the NAPE-PLD family.

Ontologies

Keywords
Biological process	Lipid metabolism Phospholipid degradation
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phospholipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D		PRO_0000318159
Sites
	Metal binding	185	1	Zinc 1 Potential
	Metal binding	187	1	Zinc 1 Potential
	Metal binding	189	1	Zinc 2 Potential
	Metal binding	190	1	Zinc 2 Potential
	Metal binding	253	1	Zinc 1 Potential
	Metal binding	343	1	Zinc 2 Potential
Natural variations
	Natural variant	152	1	S → A. Corresponds to variant rs12540583 [ dbSNP | Ensembl ].		VAR_038695
	Natural variant	389	1	D → N. Ref.3 Ref.4 Ref.5 Corresponds to variant rs3181009 [ dbSNP | Ensembl ].		VAR_038694
Experimental info
	Mutagenesis	152	1	S → A: Almost no change in activity. Ref.6
	Mutagenesis	207	1	L → F: Loss of activity. Ref.6
	Mutagenesis	380	1	H → R: Loss of activity. Ref.6
	Mutagenesis	389	1	D → N: Almost no change in activity. Ref.6
	Sequence conflict	281	1	Missing in CAI56779. Ref.3
	Sequence conflict	371	1	N → Y in CAI56779. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q6IQ20 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 5CE3114CC557B698	FASTA	393	45,596
	10 20 30 40 50 60 MDENESNQSL MTSSQYPKEA VRKRQNSARN SGASDSSRFS RKSFKLDYRL EEDVTKSKKG 70 80 90 100 110 120 KDGRFVNPWP TWKNPSIPNV LRWLIMEKDH SSVPSSKEEL DKELPVLKPY FITNPEEAGV 130 140 150 160 170 180 REAGLRVTWL GHATVMVEMD ELIFLTDPIF SSRASPSQYM GPKRFRRSPC TISELPPIDA 190 200 210 220 230 240 VLISHNHYDH LDYNSVIALN ERFGNELRWF VPLGLLDWMQ KCGCENVIEL DWWEENCVPG 250 260 270 280 290 300 HDKVTFVFTP SQHWCKRTLM DDNKVLWGSW SVLGPWNRFF FAGDTGYCPA FEEIGKRFGP 310 320 330 340 350 360 FDLAAIPIGA YEPRWFMKYQ HVDPEEAVRI HTDVQTKKSM AIHWGTFALA NEHYLEPPVK 370 380 390 LNEALERYGL NAEDFFVLKH GESRYLNNDD ENF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of a phospholipase D generating anandamide and its congeners." Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N. J. Biol. Chem. 279:5298-5305(2004) [PubMed: 14634025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
[2]	"Isolation and analysis of candidate myeloid tumor suppressor genes from a commonly deleted segment of 7q22." Curtiss N.P., Bonifas J.M., Lauchle J.O., Balkman J.D., Kratz C.P., Emerling B.M., Green E.D., Le Beau M.M., Shannon K.M. Genomics 85:600-607(2005) [PubMed: 15820312] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-389. Tissue: Colon carcinoma.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-389.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-389. Tissue: Brain.
[6]	"Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family." Wang J., Okamoto Y., Morishita J., Tsuboi K., Miyatake A., Ueda N. J. Biol. Chem. 281:12325-12335(2006) [PubMed: 16527816] [Abstract] Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF SER-152; LEU-207; HIS-380 AND ASP-389.
+	Additional computationally mapped references.

Web resources

Wikipedia

N-acyl phosphatidylethanolamine-specific phospholipase D entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY357337 mRNA. Translation: AAR13673.1. AB112352 mRNA. Translation: BAD02399.1. CR936639 mRNA. Translation: CAI56779.1. CH471070 Genomic DNA. Translation: EAW83314.1. BC071604 mRNA. Translation: AAH71604.1.
IPI	IPI00939660.
RefSeq	NP_001116310.1. NM_001122838.1. NP_945341.3. NM_198990.4.
UniGene	Hs.324271.
3D structure databases
ProteinModelPortal	Q6IQ20.
SMR	Q6IQ20. Positions 319-389.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6IQ20.
Polymorphism databases
DMDM	167016292.
Proteomic databases
PeptideAtlas	Q6IQ20.
PRIDE	Q6IQ20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341533; ENSP00000340093; ENSG00000161048. ENST00000417955; ENSP00000407112; ENSG00000161048. ENST00000422589; ENSP00000412376; ENSG00000161048. ENST00000427257; ENSP00000392775; ENSG00000161048. ENST00000455523; ENSP00000414364; ENSG00000161048. ENST00000465647; ENSP00000419188; ENSG00000161048.
GeneID	222236.
KEGG	hsa:222236.
UCSC	uc003vbc.2. human.
Organism-specific databases
CTD	222236.
GeneCards	GC07M102742.
H-InvDB	HIX0019491.
HGNC	HGNC:21683. NAPEPLD.
HPA	HPA019832.
MIM	612334. gene.
neXtProt	NX_Q6IQ20.
PharmGKB	PA162396960.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000017990.
HOVERGEN	HBG054649.
InParanoid	Q6IQ20.
OrthoDB	EOG41ZFB5.
PhylomeDB	Q6IQ20.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000161048-MONOMER.
Gene expression databases
ArrayExpress	Q6IQ20.
Bgee	Q6IQ20.
CleanEx	HS_NAPEPLD.
Genevestigator	Q6IQ20.
Family and domain databases
InterPro	IPR024884. NAPE-PLD. [Graphical view]
KO	K13985.
PANTHER	PTHR15032:SF3. PTHR15032:SF3. 1 hit.
PIRSF	PIRSF038896. NAPE-PLD. 1 hit.
ProtoNet	Search...
Other
NextBio	91585.
SOURCE	Search...

Entry information

Entry name

NAPEP_HUMAN

Accession

Primary (citable) accession number: Q6IQ20
Secondary accession number(s): Q5CZ87, Q769K1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.