Q12043 · TGL5_YEAST

Function

function

Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways (PubMed:16135509).
Also catalyzes the acylation of lysophosphatidic acid (LPA) (PubMed:20016004).

Miscellaneous

Present with 358 molecules/cell in log phase SD medium.

Catalytic activity

Activity regulation

Loses its lipolytic activity in cells lacking nonpolar lipids, but retains its side activity as lysophospholipid acyltransferase.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
18.7 μM1-(9Z-octadecenoyl)-sn-glycero-3-phosphate
29.3 μM(9Z)-octadecenoyl-CoA
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
28.8 nmol/min/mgtowards 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate
38.1 nmol/min/mgtowards (9Z)-octadecenoyl-CoA

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site216Nucleophile
Active site375Proton acceptor

GO annotations

AspectTerm
Cellular Componentlipid droplet
Molecular Functionlysophosphatidic acid acyltransferase activity
Molecular Functiontriglyceride lipase activity
Biological Processlipid catabolic process
Biological Processsporulation resulting in formation of a cellular spore
Biological Processtriglyceride mobilization

Keywords

Enzyme and pathway databases

Chemistry

Names & Taxonomy

Protein names

  • Recommended name
    Triacylglycerol lipase 5
  • EC number
  • Short names
    TAG lipase 5; TG lipase 5
  • Alternative names
    • Lipase 5

Gene names

    • Name
      TGL5
    • Synonyms
      STC2
    • ORF names
      YOR29-32, YOR2964C
    • Ordered locus names
      YOR081C

Organism names

Accessions

  • Primary accession
    Q12043
  • Secondary accessions
    • D6W2E4
    • Q7LH13

Proteomes

Organism-specific databases

Subcellular Location

Lipid droplet
Note: Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols.

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002709181-749Triacylglycerol lipase 5
Glycosylation270N-linked (GlcNAc...) asparagine
Glycosylation289N-linked (GlcNAc...) asparagine
Glycosylation297N-linked (GlcNAc...) asparagine
Glycosylation304N-linked (GlcNAc...) asparagine
Glycosylation321N-linked (GlcNAc...) asparagine
Glycosylation474N-linked (GlcNAc...) asparagine
Glycosylation589N-linked (GlcNAc...) asparagine
Modified residue645Phosphoserine
Glycosylation680N-linked (GlcNAc...) asparagine
Glycosylation714N-linked (GlcNAc...) asparagine
Glycosylation742N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for motif, domain, region, compositional bias.

TypeIDPosition(s)Description
Motif54-59HXXXXD acyltransferase motif
Domain183-388PNPLA
Motif214-218GXSXG
Region585-643Disordered
Compositional bias602-643Polar residues

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    749
  • Mass (Da)
    84,716
  • Last updated
    1996-11-01 v1
  • Checksum
    F3C5DBA97B6BA58B
MSNTLPVTEFLLSKYYELSNTPATDSSSLFKWLYHKTLSRKQLLISDLSSQKKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRRNIGRTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNSKSPNENLLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEKDPHTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITARFRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMVGQFHEVLKNPSQLFLLHQTTLGARATWPKISMIQNNCGQEFALDKAITFLKEKIIISSSIKNPLQFYQPRFSEQIKSLSIMDADLPGVDLEESSSNSLSIIKSPNKTAAPGRFPLQPLPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKANSLSFAIGASSLRLKKSPLKVPSRPQFKKRSSYYNQNMSAEMRKNRKKSGTISSYDVQTNSEDFPIPAIENGSFDNTLFNPSRFPMDAMSAATNDNFMNNSDIFQN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias602-643Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X94335
EMBL· GenBank· DDBJ
CAA64004.1
EMBL· GenBank· DDBJ
Genomic DNA
Z74989
EMBL· GenBank· DDBJ
CAA99274.1
EMBL· GenBank· DDBJ
Genomic DNA
Z70678
EMBL· GenBank· DDBJ
CAA94566.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006948
EMBL· GenBank· DDBJ
DAA10860.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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