CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003880
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lipoprotein lipase 
Protein Synonyms/Alias
 LPL 
Gene Name
 Lpl 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
40DFSDIESKFALRTPEubiquitination[1]
129PVSAGYTKLVGNDVAubiquitination[1]
265GDVDQLVKCSHERSIubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity). 
Sequence Annotation
 DOMAIN 341 464 PLAT.
 REGION 346 441 Heparin-binding (By similarity).
 ACT_SITE 159 159 Nucleophile (By similarity).
 ACT_SITE 183 183 Charge relay system (By similarity).
 ACT_SITE 268 268 Charge relay system (By similarity).
 MOD_RES 121 121 Nitrated tyrosine (By similarity).
 MOD_RES 191 191 Nitrated tyrosine (By similarity).
 MOD_RES 343 343 Nitrated tyrosine (By similarity).
 CARBOHYD 70 70 N-linked (GlcNAc...) (Potential).
 CARBOHYD 386 386 N-linked (GlcNAc...) (Potential).
 DISULFID 54 67 By similarity.
 DISULFID 243 266 By similarity.
 DISULFID 291 310 By similarity.
 DISULFID 302 305 By similarity.
 DISULFID 445 465 By similarity.  
Keyword
 Cell membrane; Chylomicron; Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor; Heparin-binding; Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Nitration; Reference proteome; Secreted; Signal; VLDL. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 474 AA 
Protein Sequence
MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA EDTCHLIPGL 60
ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLYRAQQH 120
YPVSAGYTKL VGNDVARFIN WMEEEFNYPL DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT 180
GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ 240
PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 300
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTEDGKQHNQ 360
AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMMKLKWI SDSYFSWPDW 420
WSSPSFVIER IRVKAGETQK KVIFCAREKV SHLQKGKDSA VFVKCHDKSL KKSG 474 
Gene Ontology
 GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
 GO:0009986; C:cell surface; IDA:BHF-UCL.
 GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
 GO:0031012; C:extracellular matrix; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
 GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
 GO:0004465; F:lipoprotein lipase activity; IDA:MGI.
 GO:0017129; F:triglyceride binding; IEA:Compara.
 GO:0004806; F:triglyceride lipase activity; IDA:BHF-UCL.
 GO:0010886; P:positive regulation of cholesterol storage; IEA:Compara.
 GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IGI:BHF-UCL.
 GO:0010890; P:positive regulation of sequestering of triglyceride; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0019432; P:triglyceride biosynthetic process; IEA:Compara.
 GO:0019433; P:triglyceride catabolic process; IDA:BHF-UCL.
 GO:0070328; P:triglyceride homeostasis; IEA:Compara. 
Interpro
 IPR000734; Lipase.
 IPR008976; Lipase_LipOase.
 IPR013818; Lipase_N.
 IPR002330; Lipo_Lipase.
 IPR001024; LipOase_LH2.
 IPR016272; Lipoprotein_lipase_LIPH. 
Pfam
 PF00151; Lipase
 PF01477; PLAT 
SMART
 SM00308; LH2 
PROSITE
 PS00120; LIPASE_SER
 PS50095; PLAT 
PRINTS
 PR00822; LIPOLIPASE.
 PR00821; TAGLIPASE.