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Protein

Hepatic triacylglycerol lipase

Gene

Lipc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691NucleophileBy similarity
Active sitei195 – 1951Charge relay systemPROSITE-ProRule annotation
Active sitei280 – 2801Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  • acylglycerol lipase activity Source: RGD
  • apolipoprotein binding Source: BHF-UCL
  • 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 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Protein family/group databases

ESTHERiratno-1hlip. Hepatic_Lipase.

Chemistry

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3009. Lipc.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: RGD
  • early endosome Source: RGD
  • extracellular space Source: RGD
  • high-density lipoprotein particle Source: UniProtKB-KW
  • late endosome Source: RGD
  • microvillus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

HDL, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 494472Hepatic triacylglycerol lipasePRO_0000017771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP07867.
PeptideAtlasiP07867.
PRIDEiP07867.

Interactioni

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • heparan sulfate proteoglycan binding Source: RGD

Protein-protein interaction databases

IntActiP07867. 1 interaction.
STRINGi10116.ENSRNOP00000047403.

Structurei

3D structure databases

ProteinModelPortaliP07867.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini353 – 487135PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 19412Heparin-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IIHP. Eukaryota.
ENOG4110MCZ. LUCA.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP07867.
PhylomeDBiP07867.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002333. Lipase_hep.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 2 hits.
PTHR11610:SF2. PTHR11610:SF2. 2 hits.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00824. HEPLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771N → K in AAA41335 (PubMed:3470738).Curated
Sequence conflicti302 – 3021Q → H in AAA41335 (PubMed:3470738).Curated
Sequence conflicti308 – 3081S → T in AAA41335 (PubMed:3470738).Curated
Sequence conflicti335 – 3351V → A in AAA41335 (PubMed:3470738).Curated
Sequence conflicti369 – 3691M → I in AAA41335 (PubMed:3470738).Curated
Sequence conflicti408 – 4081N → D in AAA41335 (PubMed:3470738).Curated
Sequence conflicti451 – 4511V → L in AAA41335 (PubMed:3470738).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP07867.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07867. 1 interaction.
STRINGi10116.ENSRNOP00000047403.

Chemistry

SwissLipidsiSLP:000000571.

Protein family/group databases

ESTHERiratno-1hlip. Hepatic_Lipase.

Proteomic databases

PaxDbiP07867.
PeptideAtlasiP07867.
PRIDEiP07867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3009. rat.

Organism-specific databases

RGDi3009. Lipc.

Phylogenomic databases

eggNOGiENOG410IIHP. Eukaryota.
ENOG4110MCZ. LUCA.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.
InParanoidiP07867.
PhylomeDBiP07867.

Miscellaneous databases

PROiP07867.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002333. Lipase_hep.
IPR016272. Lipase_LIPH.
IPR013818. Lipase_N.
IPR001024. PLAT/LH2_dom.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 2 hits.
PTHR11610:SF2. PTHR11610:SF2. 2 hits.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00824. HEPLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIPC_RAT
AccessioniPrimary (citable) accession number: P07867
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: July 6, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.