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Q8R2Y0

- ABHD6_MOUSE

UniProt

Q8R2Y0 - ABHD6_MOUSE

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Protein
Monoacylglycerol lipase ABHD6
Gene
Abhd6
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Has 2-arachidonoylglycerol hydrolase activity. May be a regulator of endocannabinoid signaling pathways.1 Publication

Catalytic activityi

Hydrolyzes glycerol monoesters of long-chain fatty acids.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei148 – 1481Charge relay system By similarity
Active sitei278 – 2781Charge relay system By similarity
Active sitei306 – 3061Charge relay system By similarity

GO - Molecular functioni

  1. acylglycerol lipase activity Source: MGI

GO - Biological processi

  1. long term synaptic depression Source: MGI
  2. metabolic process Source: GOC
  3. negative regulation of cell migration Source: MGI
  4. regulation of endocannabinoid signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

MEROPSiS33.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Monoacylglycerol lipase ABHD6 (EC:3.1.1.23)
Alternative name(s):
2-arachidonoylglycerol hydrolase
Abhydrolase domain-containing protein 6
Gene namesi
Name:Abhd6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1913332. Abhd6.

Subcellular locationi

Membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Extracellular Reviewed prediction
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini30 – 336307Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: MGI
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Monoacylglycerol lipase ABHD6
PRO_0000281576Add
BLAST

Proteomic databases

MaxQBiQ8R2Y0.
PaxDbiQ8R2Y0.
PRIDEiQ8R2Y0.

PTM databases

PhosphoSiteiQ8R2Y0.

Expressioni

Gene expression databases

ArrayExpressiQ8R2Y0.
BgeeiQ8R2Y0.
CleanExiMM_ABHD6.
GenevestigatoriQ8R2Y0.

Interactioni

Protein-protein interaction databases

IntActiQ8R2Y0. 1 interaction.
MINTiMINT-4118823.

Structurei

3D structure databases

ProteinModelPortaliQ8R2Y0.
SMRiQ8R2Y0. Positions 43-327.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00510000047225.
HOGENOMiHOG000008016.
HOVERGENiHBG059524.
InParanoidiQ8R2Y0.
KOiK13700.
OMAiNSFYRKL.
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]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

MDLDVVNMFV IAGGTLAIPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV    50
RYAHHEDYQF CYSFRGRPGH KPSILMLHGF SAHKDMWLSV VKFLPKNLHL 100
VCVDMPGHEG TTRSSLDDLS IVGQVKRIHQ FVECLKLNKK PFHLIGTSMG 150
GHVAGVYAAY YPSDVCSLSL VCPAGLQYST DNPFVQRLKE LEESAAIQKI 200
PLIPSTPEEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN SFYRKLFLEI 250
VNEKSRYSLH ENMDKIKVPT QIIWGKQDQV LDVSGADILA KSISNSQVEV 300
LENCGHSVVM ERPRKTAKLI VDFLASVHNT DNKKLN 336
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2.
VSP_024012Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851D → G in BAB22430. 1 Publication
Sequence conflicti173 – 1731P → A in BAB22430. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS26808.1. [Q8R2Y0-1 ]
RefSeqi NP_079617.2. NM_025341.3. [Q8R2Y0-1 ]
XP_006518136.1. XM_006518073.1. [Q8R2Y0-1 ]
XP_006518137.1. XM_006518074.1. [Q8R2Y0-1 ]
UniGenei Mm.181473.

3D structure databases

ProteinModelPortali Q8R2Y0.
SMRi Q8R2Y0. Positions 43-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8R2Y0. 1 interaction.
MINTi MINT-4118823.

Chemistry

BindingDBi Q8R2Y0.
ChEMBLi CHEMBL5010.

Protein family/group databases

MEROPSi S33.977.

PTM databases

PhosphoSitei Q8R2Y0.

Proteomic databases

MaxQBi Q8R2Y0.
PaxDbi Q8R2Y0.
PRIDEi Q8R2Y0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026313 ; ENSMUSP00000026313 ; ENSMUSG00000025277 . [Q8R2Y0-1 ]
ENSMUST00000166497 ; ENSMUSP00000129169 ; ENSMUSG00000025277 . [Q8R2Y0-1 ]
GeneIDi 66082.
KEGGi mmu:66082.
UCSCi uc007sen.1. mouse. [Q8R2Y0-1 ]

Organism-specific databases

CTDi 57406.
MGIi MGI:1913332. Abhd6.

Phylogenomic databases

eggNOGi COG0596.
GeneTreei ENSGT00510000047225.
HOGENOMi HOG000008016.
HOVERGENi HBG059524.
InParanoidi Q8R2Y0.
KOi K13700.
OMAi NSFYRKL.
OrthoDBi EOG786H3D.
PhylomeDBi Q8R2Y0.
TreeFami TF331946.

Miscellaneous databases

NextBioi 320572.
PROi Q8R2Y0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8R2Y0.
Bgeei Q8R2Y0.
CleanExi MM_ABHD6.
Genevestigatori Q8R2Y0.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view ]
PRINTSi PR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

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, SUBCELLULAR LOCATION.

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: July 9, 2014
This is version 99 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