CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006623
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lipase 4 
Protein Synonyms/Alias
 Triacylglycerol lipase 4 
Gene Name
 TGL4 
Gene Synonyms/Alias
 STC1; YKR089C; YKR409 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
174RLDDLTGKTEWKQKLubiquitination[1]
664EQTSDESKNPENSTLubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Releases specific fatty acids from neutral lipid triacylglycerols (TAG) thereby supplying fatty acids to a general acylation process. May have a specific role in sporulation. 
Sequence Annotation
 DOMAIN 282 483 Patatin.
 MOTIF 313 317 GXSXG.
 ACT_SITE 315 315 By similarity.
 MOD_RES 55 55 Phosphoserine.
 MOD_RES 737 737 Phosphoserine.
 MOD_RES 749 749 Phosphoserine.
 MOD_RES 751 751 Phosphoserine.
 MOD_RES 836 836 Phosphoserine.  
Keyword
 Complete proteome; Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Sporulation; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 910 AA 
Protein Sequence
MSSKISDLTS TQNKPLLVTQ QLIEKYYEQI LGTSQNIIPI LNPKNKFIRP SKDNSDVERV 60
EEDAGKRLQT GKNKTTNKVN FNLDTGNEDK LDDDQETVTE NENNDIEMVE TDEGEDERQG 120
SSLASKCKSF LYNVFVGNYE RDILIDKVCS QKQHAMSFEE WCSAGARLDD LTGKTEWKQK 180
LESPLYDYKL IKDLTSRMRE ERLNRNYAQL LYIIRTNWVR NLGNMGNVNL YRHSHVGTKY 240
LIDEYMMESR LALESLMESD LDDSYLLGIL QQTRRNIGRT ALVLSGGGTF GLFHIGVLGT 300
LFELDLLPRV ISGSSAGAIV ASILSVHHKE EIPVLLNHIL DKEFNIFKDD KQKSESENLL 360
IKISRFFKNG TWFDNKHLVN TMIEFLGDLT FREAYNRTGK ILNITVSPAS LFEQPRLLNN 420
LTAPNVLIWS AVCASCSLPG IFPSSPLYEK DPKTGERKPW TGSSSVKFVD GSVDNDLPIS 480
RLSEMFNVDH IIACQVNIHV FPFLKLSLSC VGGEIEDEFS ARLKQNLSSI YNFMANEAIH 540
ILEIGSEMGI AKNALTKLRS VLSQQYSGDI TILPDMCMLF RIKELLSNPT KEFLLREITN 600
GAKATWPKVS IIQNHCGQEF ALDKAISYIK GRMIVTSSLK TPFQFADSVI GLIKAPEQTS 660
DESKNPENST LLTRTPTKGD NHISNVLDDN LLESESTNSL LLLRENASTY GRSPSGFRPR 720
YSITSASLNP RHQRRKSDTI STSRRPAKSF SFSVASPTSR MLRQSSKING HPPPILQKKT 780
SMGRLMFPMD AKTYDPESHE LIPHSASIET PAMVDKKLHF GRKSRYLRHM NKKWVSSSNI 840
LYTDSDKEDH PTLRLISNFD SDAMIHSDLA GNFRRHSIDG RPPSQATKSS PFRSRPSSST 900
QHKSTTSFTQ 910 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005811; C:lipid particle; IDA:SGD.
 GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:SGD.
 GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:SGD.
 GO:0050253; F:retinyl-palmitate esterase activity; IEA:EC.
 GO:0004771; F:sterol esterase activity; IDA:SGD.
 GO:0004806; F:triglyceride lipase activity; IDA:SGD.
 GO:0007114; P:cell budding; IMP:SGD.
 GO:0006644; P:phospholipid metabolic process; IMP:SGD.
 GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
 GO:0019433; P:triglyceride catabolic process; IMP:SGD.
 GO:0006642; P:triglyceride mobilization; IDA:SGD. 
Interpro
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR002641; Patatin/PLipase_A2-rel.
 IPR021771; Triacylglycerol_lipase. 
Pfam
 PF11815; DUF3336
 PF01734; Patatin 
SMART
  
PROSITE
  
PRINTS