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Protein

Lipase 3

Gene

TGL3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Releases specific fatty acids from neutral lipid triacylglycerols (TAG) thereby supplying fatty acids to a general acylation process.2 Publications

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei237 – 2371By similarity

GO - Molecular functioni

  • lysophosphatidylethanolamine acyltransferase activity Source: SGD
  • triglyceride lipase activity Source: SGD

GO - Biological processi

  • cell budding Source: SGD
  • cellular lipid metabolic process Source: SGD
  • triglyceride catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32977-MONOMER.
YEAST:G3O-32977-MONOMER.

Chemistry

SwissLipidsiSLP:000000052.
SLP:000000671.
SLP:000000678.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase 3 (EC:3.1.1.3)
Alternative name(s):
Triacylglycerol lipase 3
Gene namesi
Name:TGL3
Ordered Locus Names:YMR313C
ORF Names:YM9924.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR313C.
SGDiS000004930. TGL3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei200 – 22021HelicalSequence analysisAdd
BLAST
Transmembranei228 – 24821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • lipid particle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 642642Lipase 3PRO_0000203356Add
BLAST

Proteomic databases

MaxQBiP40308.

PTM databases

iPTMnetiP40308.

Interactioni

Protein-protein interaction databases

BioGridi35493. 43 interactions.
DIPiDIP-5641N.
IntActiP40308. 3 interactions.
MINTiMINT-567761.

Structurei

3D structure databases

ProteinModelPortaliP40308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini204 – 379176PatatinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi235 – 2395GXSXG

Sequence similaritiesi

Contains 1 patatin domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000016747.
HOGENOMiHOG000208720.
InParanoidiP40308.
KOiK14675.
OMAiTRCSIEF.
OrthoDBiEOG78SQSV.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
IPR021771. Triacylglycerol_lipase.
[Graphical view]
PfamiPF11815. DUF3336. 1 hit.
PF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.

Sequencei

Sequence statusi: Complete.

P40308-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKETAQEYKV SAVIPTLLKN WILRVVYATL DHIPPFVWEI LHVITDIYFF
60 70 80 90 100
WVQKLINYVR PHSRVIYYNA IKKLDECDTY QMWCQQASVV DEITGANLWR
110 120 130 140 150
RNFFSRRYDF NSVIEQYSIL ENMLREEKYD VVKEKFSTTG PCMLRNFAGI
160 170 180 190 200
GDKKLFTKSL MGTKLLIEQY LTRILEGLDI LNNQTLTPTS FFQRCKLSLG
210 220 230 240 250
TTALILQGGS LFGLFHLGVI RGLLLQDLMP NIISGSSMGA CVASLFGCLS
260 270 280 290 300
NEQLKQLLTD DNLLNIIKND VDLLKSCGYG NLEQHLNLGT LIQNLIHHGY
310 320 330 340 350
SQDVYLFIRF VMKYIVKEKT FEEVYQITGK VFNIVIHPTD KSCPNLLNYV
360 370 380 390 400
TTPNVLIKSA IECSLGSGVI SEDTSLLCKN LENEIEPFLN INKNKQVKFL
410 420 430 440 450
TPENANNPSI TESPYTRLTE LFNVNNFIVS LARPYLAPLV VNDLKHEIKT
460 470 480 490 500
SKYYYYKHYP NMPPINANTV RKTQRSSSQS PIKAGTVEDL EPEPLMSPVP
510 520 530 540 550
PSSAVNDSAE YIIPELGIPQ LNFTEMEPLA FKFKYHLERK LKNIATMEFR
560 570 580 590 600
HRMEVLDNLG LLCSLIKRLI IDEKTPRSAT EIAVVPRMKS LSLTRIIEGQ
610 620 630 640
LNNIPYWIKS GERSTWPALA LIKTRCAVEF KLDDIIRARR SR
Length:642
Mass (Da):73,613
Last modified:October 1, 1996 - v2
Checksum:iA5AE059EF65465D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961A → P in AAA53543 (PubMed:7918444).Curated
Sequence conflicti100 – 1001R → P in AAA53543 (PubMed:7918444).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54141 Genomic DNA. Translation: CAA90831.1.
L34347 Genomic DNA. Translation: AAA53543.1.
BK006946 Genomic DNA. Translation: DAA10214.1.
PIRiS59306.
RefSeqiNP_014044.1. NM_001182824.1.

Genome annotation databases

EnsemblFungiiYMR313C; YMR313C; YMR313C.
GeneIDi855361.
KEGGisce:YMR313C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54141 Genomic DNA. Translation: CAA90831.1.
L34347 Genomic DNA. Translation: AAA53543.1.
BK006946 Genomic DNA. Translation: DAA10214.1.
PIRiS59306.
RefSeqiNP_014044.1. NM_001182824.1.

3D structure databases

ProteinModelPortaliP40308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35493. 43 interactions.
DIPiDIP-5641N.
IntActiP40308. 3 interactions.
MINTiMINT-567761.

Chemistry

SwissLipidsiSLP:000000052.
SLP:000000671.
SLP:000000678.

PTM databases

iPTMnetiP40308.

Proteomic databases

MaxQBiP40308.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR313C; YMR313C; YMR313C.
GeneIDi855361.
KEGGisce:YMR313C.

Organism-specific databases

EuPathDBiFungiDB:YMR313C.
SGDiS000004930. TGL3.

Phylogenomic databases

GeneTreeiENSGT00390000016747.
HOGENOMiHOG000208720.
InParanoidiP40308.
KOiK14675.
OMAiTRCSIEF.
OrthoDBiEOG78SQSV.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32977-MONOMER.
YEAST:G3O-32977-MONOMER.

Miscellaneous databases

PROiP40308.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
IPR021771. Triacylglycerol_lipase.
[Graphical view]
PfamiPF11815. DUF3336. 1 hit.
PF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core."
    Heinemeyer W., Troendle N., Albrecht G., Wolf D.H.
    Biochemistry 33:12229-12237(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-174.
    Strain: ATCC 204508 / S288c.
  4. "Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae."
    Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.
    J. Bacteriol. 181:6441-6448(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae."
    Athenstaedt K., Daum G.
    J. Biol. Chem. 278:23317-23323(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTGL3_YEAST
AccessioniPrimary (citable) accession number: P40308
Secondary accession number(s): D6W0E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3210 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

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 one 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.