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Protein

Monoacylglycerol lipase ABHD6

Gene

Abhd6

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

Functioni

Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol. Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (PubMed:18096503, PubMed:20657592). May also have a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (PubMed:24095738).By similarity3 Publications

Catalytic activityi

Hydrolyzes glycerol monoesters of long-chain fatty acids.2 Publications

Kineticsi

  1. KM=1.9 µM for 13-monoolein1 Publication
  2. KM=0.75 µM for 1-oleoyl lysophosphatidylglycerol (in presence of 5M CHAPS)1 Publication
  1. Vmax=478.6 µmol/h/mg enzyme toward 13-monoolein1 Publication
  2. Vmax=93.2 µmol/h/mg enzyme toward 1-oleoyl lysophosphatidylglycerol1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei148 – 1481Nucleophile1 Publication
Active sitei278 – 2781Charge relay systemBy similarity
Active sitei306 – 3061Charge relay systemBy similarity

GO - Molecular functioni

  • acylglycerol lipase activity Source: UniProtKB
  • phospholipase activity Source: UniProtKB

GO - Biological processi

  • acylglycerol catabolic process Source: UniProtKB
  • long term synaptic depression Source: MGI
  • negative regulation of cell migration Source: MGI
  • phospholipid catabolic process Source: UniProtKB
  • positive regulation of lipid biosynthetic process Source: UniProtKB
  • regulation of endocannabinoid signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

ESTHERimouse-ABHD6. ABHD6-Lip.
MEROPSiS33.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Monoacylglycerol lipase ABHD6Curated (EC:3.1.1.232 Publications)
Alternative name(s):
2-arachidonoylglycerol hydrolase1 Publication
Abhydrolase domain-containing protein 6Imported
Gene namesi
Name:Abhd6Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1913332. Abhd6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88ExtracellularSequence Analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 336307CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: MGI
  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Abhd6 partial knockdown inducing a stronger depletion in liver, kidney and white adipose tissues protects mice against hight-fat diet-induced metabolic disorder and obesity. De novo lipogenesis in liver is reduced and associated with a reduced expression of lipogenic genes. Accumulation of phospholipids and lysophospholipds in the liver is also observed.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481S → A: Loss of the lipid hydrolase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Monoacylglycerol lipase ABHD6PRO_0000281576Add
BLAST

Proteomic databases

MaxQBiQ8R2Y0.
PaxDbiQ8R2Y0.
PRIDEiQ8R2Y0.

PTM databases

PhosphoSiteiQ8R2Y0.

Expressioni

Tissue specificityi

Widely expressed with higher expression in small intestine, liver and brown adipose tissue (PubMed:24095738). In brain, expressed postsynaptically in cortical neurons but not detected in microglia (at protein level) (PubMed:20657592).2 Publications

Inductioni

Up-regulated in small intestine and liver by high-fat diet.1 Publication

Gene expression databases

BgeeiQ8R2Y0.
CleanExiMM_ABHD6.
ExpressionAtlasiQ8R2Y0. baseline and differential.
GenevisibleiQ8R2Y0. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8R2Y0. 1 interaction.
MINTiMINT-4118823.
STRINGi10090.ENSMUSP00000026313.

Structurei

3D structure databases

ProteinModelPortaliQ8R2Y0.
SMRiQ8R2Y0. Positions 43-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00510000047225.
HOGENOMiHOG000008016.
HOVERGENiHBG059524.
InParanoidiQ8R2Y0.
KOiK13700.
OMAiKTANLIL.
OrthoDBiEOG786H3D.
PhylomeDBiQ8R2Y0.
TreeFamiTF331946.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R2Y0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLDVVNMFV IAGGTLAIPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV
60 70 80 90 100
RYAHHEDYQF CYSFRGRPGH KPSILMLHGF SAHKDMWLSV VKFLPKNLHL
110 120 130 140 150
VCVDMPGHEG TTRSSLDDLS IVGQVKRIHQ FVECLKLNKK PFHLIGTSMG
160 170 180 190 200
GHVAGVYAAY YPSDVCSLSL VCPAGLQYST DNPFVQRLKE LEESAAIQKI
210 220 230 240 250
PLIPSTPEEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN SFYRKLFLEI
260 270 280 290 300
VNEKSRYSLH ENMDKIKVPT QIIWGKQDQV LDVSGADILA KSISNSQVEV
310 320 330
LENCGHSVVM ERPRKTAKLI VDFLASVHNT DNKKLN
Length:336
Mass (Da):38,205
Last modified:June 1, 2002 - v1
Checksum:i4C207C66DBE41FE4
GO
Isoform 2 (identifier: Q8R2Y0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Note: No experimental confirmation available.
Show »
Length:289
Mass (Da):32,788
Checksum:i1A55E8CD1C0B71A6
GO

Sequence cautioni

The sequence BAE40616.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE40616.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851D → G in BAB22430 (PubMed:16141072).Curated
Sequence conflicti173 – 1731P → A in BAB22430 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2. 1 PublicationVSP_024012Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002883 mRNA. Translation: BAB22430.1.
AK076105 mRNA. Translation: BAC36186.1.
AK090076 mRNA. Translation: BAC41081.1.
AK168782 mRNA. Translation: BAE40616.1. Different initiation.
BC027011 mRNA. Translation: AAH27011.1.
CCDSiCCDS26808.1. [Q8R2Y0-1]
RefSeqiNP_079617.2. NM_025341.3. [Q8R2Y0-1]
XP_006518136.1. XM_006518073.1. [Q8R2Y0-1]
XP_006518137.1. XM_006518074.1. [Q8R2Y0-1]
UniGeneiMm.181473.

Genome annotation databases

EnsembliENSMUST00000026313; ENSMUSP00000026313; ENSMUSG00000025277. [Q8R2Y0-1]
ENSMUST00000166497; ENSMUSP00000129169; ENSMUSG00000025277. [Q8R2Y0-1]
GeneIDi66082.
KEGGimmu:66082.
UCSCiuc007sen.1. mouse. [Q8R2Y0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002883 mRNA. Translation: BAB22430.1.
AK076105 mRNA. Translation: BAC36186.1.
AK090076 mRNA. Translation: BAC41081.1.
AK168782 mRNA. Translation: BAE40616.1. Different initiation.
BC027011 mRNA. Translation: AAH27011.1.
CCDSiCCDS26808.1. [Q8R2Y0-1]
RefSeqiNP_079617.2. NM_025341.3. [Q8R2Y0-1]
XP_006518136.1. XM_006518073.1. [Q8R2Y0-1]
XP_006518137.1. XM_006518074.1. [Q8R2Y0-1]
UniGeneiMm.181473.

3D structure databases

ProteinModelPortaliQ8R2Y0.
SMRiQ8R2Y0. Positions 43-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R2Y0. 1 interaction.
MINTiMINT-4118823.
STRINGi10090.ENSMUSP00000026313.

Chemistry

BindingDBiQ8R2Y0.
ChEMBLiCHEMBL5010.

Protein family/group databases

ESTHERimouse-ABHD6. ABHD6-Lip.
MEROPSiS33.977.

PTM databases

PhosphoSiteiQ8R2Y0.

Proteomic databases

MaxQBiQ8R2Y0.
PaxDbiQ8R2Y0.
PRIDEiQ8R2Y0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026313; ENSMUSP00000026313; ENSMUSG00000025277. [Q8R2Y0-1]
ENSMUST00000166497; ENSMUSP00000129169; ENSMUSG00000025277. [Q8R2Y0-1]
GeneIDi66082.
KEGGimmu:66082.
UCSCiuc007sen.1. mouse. [Q8R2Y0-1]

Organism-specific databases

CTDi57406.
MGIiMGI:1913332. Abhd6.

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00510000047225.
HOGENOMiHOG000008016.
HOVERGENiHBG059524.
InParanoidiQ8R2Y0.
KOiK13700.
OMAiKTANLIL.
OrthoDBiEOG786H3D.
PhylomeDBiQ8R2Y0.
TreeFamiTF331946.

Miscellaneous databases

NextBioi320572.
PROiQ8R2Y0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R2Y0.
CleanExiMM_ABHD6.
ExpressionAtlasiQ8R2Y0. baseline and differential.
GenevisibleiQ8R2Y0. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Amnion, Embryo and Kidney.
  2. "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] (ISOFORM 1).
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  3. "A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol."
    Blankman J.L., Simon G.M., Cravatt B.F.
    Chem. Biol. 14:1347-1356(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  4. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-148, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiABHD6_MOUSE
AccessioniPrimary (citable) accession number: Q8R2Y0
Secondary accession number(s): Q3TGD2, Q9DCD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 1, 2002
Last modified: June 24, 2015
This is version 107 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

External Data

Dasty 3

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 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.