Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D

Gene

Napepld

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

An N-acylphosphatidylethanolamine + H2O = an N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate.

Cofactori

Zn2+By similarityNote: Binds 1 or 2 zinc ions per subunit.By similarity

Enzyme regulationi

Activity is stimulated by divalent cations.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi185 – 1851Zinc 1Sequence analysis
Metal bindingi187 – 1871Zinc 1Sequence analysis
Metal bindingi189 – 1891Zinc 2Sequence analysis
Metal bindingi190 – 1901Zinc 2Sequence analysis
Metal bindingi253 – 2531Zinc 1Sequence analysis
Metal bindingi343 – 3431Zinc 2Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.4.54. 3474.

Chemistry

SwissLipidsiSLP:000001130.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (EC:3.1.4.54)
Short name:
N-acyl phosphatidylethanolamine phospholipase D
Short name:
NAPE-PLD
Short name:
NAPE-hydrolyzing phospholipase D
Gene namesi
Name:Napepld
Synonyms:Mbldc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2140885. Napepld.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2163172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase DPRO_0000318160Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BH82.
PaxDbiQ8BH82.
PRIDEiQ8BH82.

PTM databases

iPTMnetiQ8BH82.
PhosphoSiteiQ8BH82.

Expressioni

Tissue specificityi

Widely expressed. Highest expression in brain, kidney and testis (at protein level).1 Publication

Gene expression databases

BgeeiQ8BH82.
CleanExiMM_NAPEPLD.
GenevisibleiQ8BH82. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054458.

Structurei

3D structure databases

ProteinModelPortaliQ8BH82.
SMRiQ8BH82. Positions 57-389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAPE-PLD family.Curated

Phylogenomic databases

eggNOGiKOG3798. Eukaryota.
COG2220. LUCA.
GeneTreeiENSGT00390000017990.
HOGENOMiHOG000267495.
HOVERGENiHBG054649.
InParanoidiQ8BH82.
KOiK13985.
OMAiWGSWSVL.
OrthoDBiEOG7Z95MB.
PhylomeDBiQ8BH82.
TreeFamiTF313520.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR024884. NAPE-PLD.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038896. NAPE-PLD. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BH82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEYEDSQSP APSYQYPKET LRKRQNSVQN SGGSVSSRFS RKSFKLDYRL
60 70 80 90 100
EEDVTKSKKG KDGRFVNPWP TWKNISIPNV LRWLIMEKNH SGVPGSKEEL
110 120 130 140 150
DKELPVLKPY FVSDPEDAGV REAGLRVTWL GHATLMVEMD ELIFLTDPMF
160 170 180 190 200
SSRASPSQYM GPKRFRRPPC TISELPTIDA VLISHNHYDH LDYGSVLALN
210 220 230 240 250
ERFGSELRWF VPLGLLDWMQ KCGCENVIEL DWWEENCVPG HDKVTFVFTP
260 270 280 290 300
SQHWCKRTLL DDNKVLWGSW SVLGPWSRFF FAGDTGYCPA FEEIGKRFGP
310 320 330 340 350
FDLAAIPIGA YEPRWFMKYQ HADPEDAVRI HIDLQTKRSV AIHWGTFALA
360 370 380 390
NEHYLEPPVK LNEALERYGL SCEDFFILKH GESRYLNTDD RAFEET
Length:396
Mass (Da):45,816
Last modified:March 1, 2003 - v1
Checksum:i432E61F81D441E0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB112350 mRNA. Translation: BAD02397.1.
AK049135 mRNA. Translation: BAC33563.1.
AK080888 mRNA. Translation: BAC38064.1.
AK141585 mRNA. Translation: BAE24749.1.
BC062890 mRNA. Translation: AAH62890.1.
CCDSiCCDS19105.1.
RefSeqiNP_848843.1. NM_178728.5.
XP_006535774.1. XM_006535711.2.
XP_006535775.1. XM_006535712.2.
UniGeneiMm.153292.

Genome annotation databases

EnsembliENSMUST00000060899; ENSMUSP00000054458; ENSMUSG00000044968.
ENSMUST00000115217; ENSMUSP00000110872; ENSMUSG00000044968.
GeneIDi242864.
KEGGimmu:242864.
UCSCiuc008wov.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB112350 mRNA. Translation: BAD02397.1.
AK049135 mRNA. Translation: BAC33563.1.
AK080888 mRNA. Translation: BAC38064.1.
AK141585 mRNA. Translation: BAE24749.1.
BC062890 mRNA. Translation: AAH62890.1.
CCDSiCCDS19105.1.
RefSeqiNP_848843.1. NM_178728.5.
XP_006535774.1. XM_006535711.2.
XP_006535775.1. XM_006535712.2.
UniGeneiMm.153292.

3D structure databases

ProteinModelPortaliQ8BH82.
SMRiQ8BH82. Positions 57-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054458.

Chemistry

ChEMBLiCHEMBL2163172.
SwissLipidsiSLP:000001130.

PTM databases

iPTMnetiQ8BH82.
PhosphoSiteiQ8BH82.

Proteomic databases

MaxQBiQ8BH82.
PaxDbiQ8BH82.
PRIDEiQ8BH82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060899; ENSMUSP00000054458; ENSMUSG00000044968.
ENSMUST00000115217; ENSMUSP00000110872; ENSMUSG00000044968.
GeneIDi242864.
KEGGimmu:242864.
UCSCiuc008wov.1. mouse.

Organism-specific databases

CTDi222236.
MGIiMGI:2140885. Napepld.

Phylogenomic databases

eggNOGiKOG3798. Eukaryota.
COG2220. LUCA.
GeneTreeiENSGT00390000017990.
HOGENOMiHOG000267495.
HOVERGENiHBG054649.
InParanoidiQ8BH82.
KOiK13985.
OMAiWGSWSVL.
OrthoDBiEOG7Z95MB.
PhylomeDBiQ8BH82.
TreeFamiTF313520.

Enzyme and pathway databases

BRENDAi3.1.4.54. 3474.

Miscellaneous databases

NextBioi385594.
PROiQ8BH82.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BH82.
CleanExiMM_NAPEPLD.
GenevisibleiQ8BH82. MM.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR024884. NAPE-PLD.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038896. NAPE-PLD. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Adipose tissue and Hippocampus.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiNAPEP_MOUSE
AccessioniPrimary (citable) accession number: Q8BH82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2003
Last modified: January 20, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.