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Protein

Hepatic triacylglycerol lipase

Gene

Lipc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei169NucleophileBy similarity1
Active sitei195Charge relay systemPROSITE-ProRule annotation1
Active sitei280Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

  • acylglycerol lipase activity Source: RGD
  • apolipoprotein binding Source: RGD
  • carboxylic ester hydrolase activity Source: RGD
  • chylomicron binding Source: BHF-UCL
  • heparan sulfate proteoglycan binding Source: RGD
  • heparin binding Source: RGD
  • lipid binding Source: RGD
  • low-density lipoprotein particle binding Source: BHF-UCL
  • lysophospholipase activity Source: RGD
  • phosphatidylcholine 1-acylhydrolase activity Source: RGD
  • transferase activity, transferring acyl groups Source: RGD
  • triglyceride lipase activity Source: RGD

GO - Biological processi

  • cellular response to hormone stimulus Source: RGD
  • chylomicron remnant clearance Source: RGD
  • chylomicron remodeling Source: RGD
  • circadian rhythm Source: RGD
  • developmental growth Source: RGD
  • fatty acid metabolic process Source: RGD
  • glycerophospholipid catabolic process Source: RGD
  • heparan sulfate proteoglycan biosynthetic process Source: RGD
  • high-density lipoprotein particle remodeling Source: RGD
  • liver development Source: RGD
  • low-density lipoprotein particle clearance Source: RGD
  • low-density lipoprotein particle remodeling Source: BHF-UCL
  • neutral lipid catabolic process Source: RGD
  • phosphatidic acid metabolic process Source: RGD
  • phosphatidylcholine metabolic process Source: RGD
  • phosphatidylethanolamine metabolic process Source: RGD
  • phosphatidylserine metabolic process Source: RGD
  • protein complex oligomerization Source: RGD
  • regulation of plasma lipoprotein particle levels Source: RGD
  • response to acetate Source: RGD
  • response to amino acid Source: RGD
  • response to calcium ion Source: RGD
  • response to carbohydrate Source: RGD
  • response to copper ion Source: RGD
  • response to drug Source: RGD
  • response to fatty acid Source: RGD
  • response to glucocorticoid Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: RGD
  • response to inorganic substance Source: RGD
  • response to lipid Source: RGD
  • response to magnesium ion Source: RGD
  • response to nutrient levels Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • triglyceride metabolic process Source: RGD
  • very-low-density lipoprotein particle remodeling Source: RGD

Keywordsi

Molecular functionHeparin-binding, Hydrolase
Biological processLipid degradation, Lipid metabolism

Protein family/group databases

ESTHERiratno-1hlip Hepatic_Lipase

Chemistry databases

SwissLipidsiSLP:000000571

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatic triacylglycerol lipase (EC:3.1.1.3)
Short name:
HL
Short name:
Hepatic lipase
Alternative name(s):
Lipase member C
Gene namesi
Name:Lipc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3009 Lipc

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

HDL, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
ChainiPRO_000001777123 – 494Hepatic triacylglycerol lipaseAdd BLAST472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi398N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP07867
PeptideAtlasiP07867
PRIDEiP07867

Interactioni

GO - Molecular functioni

  • apolipoprotein binding Source: RGD
  • heparan sulfate proteoglycan binding Source: RGD

Protein-protein interaction databases

IntActiP07867, 1 interactor
STRINGi10116.ENSRNOP00000047403

Structurei

3D structure databases

ProteinModelPortaliP07867
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini353 – 487PLATPROSITE-ProRule annotationAdd BLAST135

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 194Heparin-bindingSequence analysisAdd BLAST12

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IIHP Eukaryota
ENOG4110MCZ LUCA
HOGENOMiHOG000038553
HOVERGENiHBG002259
InParanoidiP07867
PhylomeDBiP07867

Family and domain databases

CDDicd00707 Pancreat_lipase_like, 1 hit
Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013818 Lipase/vitellogenin
IPR002333 Lipase_hep
IPR016272 Lipase_LIPH
IPR033906 Lipase_N
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
IPR000734 TAG_lipase
PANTHERiPTHR11610 PTHR11610, 1 hit
PTHR11610:SF2 PTHR11610:SF2, 1 hit
PfamiView protein in Pfam
PF00151 Lipase, 1 hit
PF01477 PLAT, 1 hit
PIRSFiPIRSF000865 Lipoprotein_lipase_LIPH, 1 hit
PRINTSiPR00824 HEPLIPASE
PR00821 TAGLIPASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF49723 SSF49723, 1 hit
SSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
PS50095 PLAT, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNHLQISVS LVLCIFIQSS ACGQGVGTEP FGRNLGATEE RKPLQKPEIR
60 70 80 90 100
FLLFKDESDR LGCQLRPQHP ETLQECGFNS SHPLVMIIHG WSVDGLLETW
110 120 130 140 150
IWKIVGALKS RQSQPVNVGL VDWISLAYQH YAIAVRNTRV VGQEVAALLL
160 170 180 190 200
WLEESMKFSR SKVHLIGYSL GAHVSGFAGS SMGGKRKIGR ITGLDPAGPM
210 220 230 240 250
FEGTSPNERL SPDDANFVDA IHTFTREHMG LSVGIKQPIA HYDFYPNGGS
260 270 280 290 300
FQPGCHFLEL YKHIAEHGLN AITQTINCAH ERSVHLFIDS LQHSNLQNTG
310 320 330 340 350
FQCSNMDSFS QGLCLNCKKG RCNSLGYDIR RIGHVKSKTL FLITRAQSPF
360 370 380 390 400
KVYHYQFKIQ FINQMEKPME PTFTMTLLGT KEEIKKIPIT LGEGITSNKT
410 420 430 440 450
YSLLITLNKD IGELIMLKFK WENSAVWANV WNTVQTIMLW DTEPHYAGLI
460 470 480 490
VKTIWVKAGE TQQRMTFCPD NVDDLQLHPT QEKVFVKCDL KSKD
Length:494
Mass (Da):55,623
Last modified:August 1, 1990 - v2
Checksum:i2A9461B1F80845EA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti277N → K in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti302Q → H in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti308S → T in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti335V → A in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti369M → I in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti408N → D in AAA41335 (PubMed:3470738).Curated1
Sequence conflicti451V → L in AAA41335 (PubMed:3470738).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17366 mRNA Translation: CAA35241.1
X17367 Genomic DNA Translation: CAA35242.1
M16235 mRNA Translation: AAA41335.1
PIRiA27442
UniGeneiRn.1195

Genome annotation databases

UCSCiRGD:3009 rat

Similar proteinsi

Entry informationi

Entry nameiLIPC_RAT
AccessioniPrimary (citable) accession number: P07867
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: May 23, 2018
This is version 142 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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