A0A6M2DRZ6 · A0A6M2DRZ6_9NEOP

Function

Catalytic activity

  • 1,2-di-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+ = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O
    This reaction proceeds in the backward direction.
  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)-octadecenoylglycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-glycerol + H2O = 2-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = 1-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-glycerol + H2O = glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-O-hexadecyl-2-acetyl-sn-glycerol + H2O = 1-O-hexadecyl-sn-glycerol + acetate + H+
    This reaction proceeds in the forward direction.
  • 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = glycerol + (5Z,8Z,11Z,14Z)-eicosatetraenoate + H+
    This reaction proceeds in the forward direction.
  • 2-(9Z-octadecenoyl)-glycerol + H2O = glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • Hydrolyzes glycerol monoesters of long-chain fatty acids.
    EC:3.1.1.23 (UniProtKB | ENZYME | Rhea)
  • a diacylglycerol + H2O = a monoacylglycerol + a fatty acid + H+
    EC:3.1.1.79 (UniProtKB | ENZYME | Rhea)
  • a monoacylglycerol + H2O = glycerol + a fatty acid + H+
    EC:3.1.1.79 (UniProtKB | ENZYME | Rhea)
  • a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
    EC:3.1.1.79 (UniProtKB | ENZYME | Rhea)
  • all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + hexadecanoate + H+
    This reaction proceeds in the forward direction.
  • cholesteryl (9Z-octadecenoate) + H2O = cholesterol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.

Pathway

Glycerolipid metabolism; triacylglycerol degradation.
Lipid metabolism.

GO annotations

AspectTerm
Cellular Componentcaveola
Cellular Componentcytosol
Cellular Componentlipid droplet
Molecular Functiondiacylglycerol lipase activity
Molecular Functionhormone-sensitive lipase activity
Molecular Functionmonoacylglycerol lipase activity
Molecular Functionsterol ester esterase activity
Molecular Functiontriacylglycerol lipase activity
Biological Processcholesterol metabolic process
Biological Processtriglyceride catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hormone-sensitive lipase
  • EC number
  • Alternative names
    • Monoacylglycerol lipase LIPE
    • Retinyl ester hydrolase

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Siphonaptera > Pulicidae > Xenopsyllinae > Xenopsylla

Accessions

  • Primary accession
    A0A6M2DRZ6

Subcellular Location

Cell membrane
Cytoplasm, cytosol
Lipid droplet
Membrane, caveola

Keywords

Interaction

Subunit

Monomer and homodimer. Interacts with CAVIN1 in the adipocyte cytoplasm. Interacts with PLIN5.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain50-353Hormone-sensitive lipase N-terminal
Domain369-528Alpha/beta hydrolase fold-3
Region765-792Disordered
Domain903-964Alpha/beta hydrolase fold-3

Sequence similarities

Belongs to the 'GDXG' lipolytic enzyme family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    994
  • Mass (Da)
    110,040
  • Last updated
    2020-10-07 v1
  • Checksum
    10EA1FE0494A7B72
CQYVLKLIDSHGFKLNIFIWVYKLKLIKMDNASDSKETASHNQNDSDIYMNLSKLCFDNEEFFAKDQSDYGLRLHEAFYGLRCHIDSILPLVTEIRQIAPLYDFDEQTPGNGYRSFVGVVDCCINYSTNLALQICHSRDNLLFRKGHFMKEIEACSHLLASLSTCLSHLKTMSSWCEIGELFPKDDHRPEELFATTSAINQYSFYGRCLGFQYCESMRGILKGLSICMAGFSEAYYNNGNLFSKATSSVFAGGKYVMDPELRARRIVNISQSASVDFCKSFWSLSENEMMHRIPSVMCSHGISVNRVISIPPEKLELPGMQGEGIVEVPIPTSHGGPRPIQVRLISAKRREGMIGEANNECVLPSRGLVIHLHGGGFVAQSSKSHESYLREWAAELGVPIISVDYSLAPEAPFPRACEEVFYAYCWALKNSKLLGTTAERIVLAGDSAGANLHLGLALRCIEMGIQPPSGIFVAYAPVLVSFVPSPARLLCLMDPLLPFGFMMRCLKAYACPSPPNNVNNKVATPLSVPENVNISPTSESMFGALVSESDLAELEARRSGLDNDLDSDSDTITGASLSSIPTNVATYDQNNIESNNYGINVIHGGKDLNKEATDSLHVTIIEPNANNTYGNLSNGVNISQIICTDVIEKSINPTVSSNDNDKVKVNNFKKMCDAGTDPEEVPVISDNYKITEALQGLMQRTKNVKNNVKNFMFNGSISLPPENILDSMPDNVIEPSFTKINSKNDLLANENTSAKDIAEIENHNKISKSESYHSNSSENNKNEVDAKGEEIPSSEANEFVDEFIERYILGIAPEDEPKVKHASTSYDDFSLSDLPHDIAIGIHERITRAARKFLSTVSNTFSSITSSNEIPPVATREDFSVQSNLDALIARSPSDEFIFQVPKNPYLSPYWADDELLRKLPTTRMLTTELDPCLDDCVMFAKKLKKLGNDVGLDVLSGLPHGFLNLSLMSKDAHRGSMLCVRRISDLLDLKHLP

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GIIL01005443
EMBL· GenBank· DDBJ
NOV49169.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

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