A0A3Q2XVL8 · A0A3Q2XVL8_HIPCM

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.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site428

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

Gene names

    • Name
      LIPE

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Syngnathiaria > Syngnathiformes > Syngnathoidei > Syngnathidae > Hippocampus

Accessions

  • Primary accession
    A0A3Q2XVL8

Proteomes

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

Type
IDPosition(s)Description
Domain7-317Hormone-sensitive lipase N-terminal
Domain350-499Alpha/beta hydrolase fold-3
Compositional bias533-562Polar residues
Region533-577Disordered
Domain667-732Alpha/beta hydrolase fold-3
Region759-778Disordered
Compositional bias762-777Basic and acidic residues

Sequence similarities

Belongs to the 'GDXG' lipolytic enzyme family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    817
  • Mass (Da)
    89,354
  • Last updated
    2019-04-10 v1
  • MD5 Checksum
    8A2760D55DB1C9C9B5EC29650E5C4C6B
MDTKAVFVALYNVCEENAAYFSGRAKGPQNDTARRLVDTMKLIQEHARSLEPVISGFAAVYHHFDFDPHIPANGYRSLVKVVRCCLLHIIHKGRYITANRRSIFFRMAHNAGEMEAYCNALCQLRALLYLAQRMLHDNGHGNLFFHDESGLSESFVREYSSMHKGCFYGRCLGFQFCPGIRPSLQTIAIGLVAFGENYRPHQSGIGVAASSFFTSGKYAIDPELRGAEFERITQNLDVHFWKTFWNVTETEVLSSLASMTSVPVKVNRTLSVPPVPFDLPLAANHQASVTIPPPSAHIGTAPVQMRLISYDLREGQDSETLLSLTRSDVGAKSLSLGLKTKRLPSSPCLLIHFHGGGFVAQTSKSHEPYLKSWSQDLGVPILSVDYSLAPEAPFPRALEECFYAYCWALRNHHLLGWTGEKVCLAGDSAGGNLCVTTSMRAAAYGVRMPDGLLATYPATLLTAYASPSRLLTLIDPMLPLSVLSRCLSAYAGSEPQTDKQVEKVSTLGMVRKDTALLLRDFRQGASNWIHSLLDSNRADNPPSTQPEDTDAVRTSVSEASISSPHVDPPRPSEPTEFLAGKLPVKSQTCQDLGADNSTSHCAPLVSERAPEEVHFSFSISTDTPSEWHCDLSLLAIPPPGGEEGSEFPQGFEPLRSEQLSEMKLHSSPVVKDPFCSPLLAPDSMLKALPPVHIVACALDPMLDDSVMFAKRLRAVGKPVTLCIVDDLPHGFLSLSQLSRETREAANVCAERIRAVFTQEETPPPEPRKHRKLERTDRGSATAALLVRGELDAGLGTKMAEADGFVTITQNGVEGVGA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias533-562Polar residues
Compositional bias762-777Basic and acidic residues

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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