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Protein

Monoacylglycerol lipase ABHD6

Gene

ABHD6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways. May also have a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity).By similarity1 Publication

Catalytic activityi

Hydrolyzes glycerol monoesters of long-chain fatty acids.1 Publication

Kineticsi

  1. KM=159 µM for 2-arachidonoyglycerol1 Publication

Vmax=45 nmol/min/mg enzyme toward 2-arachidonoyglycerol1 Publication

pH dependencei

Optimum pH is 7.2-9 with 2-arachidonoyglycerol as substrate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei148 – 1481NucleophileBy similarity1 Publication
Active sitei278 – 2781Charge relay systemBy similarity
Active sitei306 – 3061Charge relay systemBy similarity

GO - Molecular functioni

  1. acylglycerol lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. long term synaptic depression Source: Ensembl
  2. negative regulation of cell migration Source: Ensembl
  3. regulation of endocannabinoid signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

MEROPSiS33.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Monoacylglycerol lipase ABHD6Curated (EC:3.1.1.231 Publication)
Alternative name(s):
2-arachidonoylglycerol hydrolaseBy similarity
Abhydrolase domain-containing protein 6Imported
Gene namesi
Name:ABHD6Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:21398. ABHD6.

Subcellular locationi

Membrane By similarity; Single-pass type II membrane protein Sequence Analysis. Mitochondrion By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88ExtracellularSequence Analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 337308CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481S → A: Loss of 2-arachidonoyglycerol hydrolase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134916787.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Monoacylglycerol lipase ABHD6PRO_0000281575Add
BLAST

Proteomic databases

MaxQBiQ9BV23.
PaxDbiQ9BV23.
PRIDEiQ9BV23.

PTM databases

PhosphoSiteiQ9BV23.

Expressioni

Gene expression databases

BgeeiQ9BV23.
CleanExiHS_ABHD6.
ExpressionAtlasiQ9BV23. baseline and differential.
GenevestigatoriQ9BV23.

Organism-specific databases

HPAiHPA017283.

Interactioni

Protein-protein interaction databases

BioGridi121508. 3 interactions.
IntActiQ9BV23. 2 interactions.
STRINGi9606.ENSP00000295962.

Structurei

3D structure databases

ProteinModelPortaliQ9BV23.
SMRiQ9BV23. Positions 69-324.
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.
InParanoidiQ9BV23.
KOiK13700.
OMAiKTANLIL.
OrthoDBiEOG786H3D.
PhylomeDBiQ9BV23.
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.

Sequencei

Sequence statusi: Complete.

Q9BV23-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLDVVNMFV IAGGTLAIPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV
60 70 80 90 100
RYVHHEDYQF CYSFRGRPGH KPSILMLHGF SAHKDMWLSV VKFLPKNLHL
110 120 130 140 150
VCVDMPGHEG TTRSSLDDLS IDGQVKRIHQ FVECLKLNKK PFHLVGTSMG
160 170 180 190 200
GQVAGVYAAY YPSDVSSLCL VCPAGLQYST DNQFVQRLKE LQGSAAVEKI
210 220 230 240 250
PLIPSTPEEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN NFYRKLFLEI
260 270 280 290 300
VSEKSRYSLH QNMDKIKVPT QIIWGKQDQV LDVSGADMLA KSIANCQVEL
310 320 330
LENCGHSVVM ERPRKTAKLI IDFLASVHNT DNNKKLD
Length:337
Mass (Da):38,331
Last modified:June 1, 2001 - v1
Checksum:iD87CEE8316F94910
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111I → T in BAD18771 (PubMed:14702039).Curated
Sequence conflicti135 – 1351L → P in BAD18771 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122983 mRNA. Translation: BAG53832.1.
AK172797 mRNA. Translation: BAD18771.1.
AK313168 mRNA. Translation: BAG35986.1.
AC098479 Genomic DNA. No translation available.
AC137936 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65360.1.
BC001698 mRNA. Translation: AAH01698.1.
CCDSiCCDS2887.1.
RefSeqiNP_065727.4. NM_020676.5.
XP_005265393.1. XM_005265336.2.
UniGeneiHs.476454.

Genome annotation databases

EnsembliENST00000295962; ENSP00000295962; ENSG00000163686.
ENST00000478253; ENSP00000420315; ENSG00000163686.
GeneIDi57406.
KEGGihsa:57406.
UCSCiuc003djs.4. human.

Polymorphism databases

DMDMi74733280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122983 mRNA. Translation: BAG53832.1.
AK172797 mRNA. Translation: BAD18771.1.
AK313168 mRNA. Translation: BAG35986.1.
AC098479 Genomic DNA. No translation available.
AC137936 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65360.1.
BC001698 mRNA. Translation: AAH01698.1.
CCDSiCCDS2887.1.
RefSeqiNP_065727.4. NM_020676.5.
XP_005265393.1. XM_005265336.2.
UniGeneiHs.476454.

3D structure databases

ProteinModelPortaliQ9BV23.
SMRiQ9BV23. Positions 69-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121508. 3 interactions.
IntActiQ9BV23. 2 interactions.
STRINGi9606.ENSP00000295962.

Chemistry

ChEMBLiCHEMBL2189127.

Protein family/group databases

MEROPSiS33.977.

PTM databases

PhosphoSiteiQ9BV23.

Polymorphism databases

DMDMi74733280.

Proteomic databases

MaxQBiQ9BV23.
PaxDbiQ9BV23.
PRIDEiQ9BV23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295962; ENSP00000295962; ENSG00000163686.
ENST00000478253; ENSP00000420315; ENSG00000163686.
GeneIDi57406.
KEGGihsa:57406.
UCSCiuc003djs.4. human.

Organism-specific databases

CTDi57406.
GeneCardsiGC03P058198.
HGNCiHGNC:21398. ABHD6.
HPAiHPA017283.
neXtProtiNX_Q9BV23.
PharmGKBiPA134916787.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00510000047225.
HOGENOMiHOG000008016.
HOVERGENiHBG059524.
InParanoidiQ9BV23.
KOiK13700.
OMAiKTANLIL.
OrthoDBiEOG786H3D.
PhylomeDBiQ9BV23.
TreeFamiTF331946.

Miscellaneous databases

ChiTaRSiABHD6. human.
GenomeRNAii57406.
NextBioi63520.
PROiQ9BV23.

Gene expression databases

BgeeiQ9BV23.
CleanExiHS_ABHD6.
ExpressionAtlasiQ9BV23. baseline and differential.
GenevestigatoriQ9BV23.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum, Hepatoma and Lung.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Skin.
  5. "Biochemical and pharmacological characterization of human alpha/beta-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12)."
    Navia-Paldanius D., Savinainen J.R., Laitinen J.T.
    J. Lipid Res. 53:2413-2424(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-148.

Entry informationi

Entry nameiABHD6_HUMAN
AccessioniPrimary (citable) accession number: Q9BV23
Secondary accession number(s): B2R7Y9, Q6ZMF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  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.