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P27656 (LIPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hepatic triacylglycerol lipase

Short name=HL
Short name=Hepatic lipase
EC=3.1.1.3
Alternative name(s):
Lipase member C
Gene names
Name:Lipc
Synonyms:Hpl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentHDL
Secreted
   DomainSignal
   LigandHeparin-binding
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol homeostasis

Inferred from genetic interaction PubMed 10357838. Source: MGI

cholesterol metabolic process

Inferred from genetic interaction PubMed 10357838. Source: MGI

cholesterol transport

Inferred from mutant phenotype PubMed 8798380. Source: MGI

fatty acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

triglyceride catabolic process

Inferred from electronic annotation. Source: Ensembl

triglyceride homeostasis

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from direct assay PubMed 15995171. Source: MGI

high-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipase activity

Inferred from direct assay PubMed 12975454PubMed 15995171. Source: MGI

protein binding

Inferred from physical interaction PubMed 19783858. Source: MGI

triglyceride lipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 510488Hepatic triacylglycerol lipase
PRO_0000017770

Regions

Domain353 – 487135PLAT
Region183 – 19412Heparin-binding Potential

Sites

Active site1691Nucleophile By similarity
Active site1951Charge relay system By similarity
Active site2801Charge relay system By similarity

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2861L → P in CAA41329. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P27656 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E30222652D782A05

FASTA51057,389
        10         20         30         40         50         60 
MGNPLQISIF LVFCIFIQSS ACGQGVGTEP FGRSLGATEA SKPLKKPETR FLLFQDENDR 

        70         80         90        100        110        120 
LGCRLRPQHP ETLQECGFNS SQPLIMIIHG WSVDGLLENW IWKIVSALKS RQSQPVNVGL 

       130        140        150        160        170        180 
VDWISLAYQH YTIAVQNTRI VGQDVAALLL WLEESAKFSR SKVHLIGYSL GAHVSGFAGS 

       190        200        210        220        230        240 
SMDGKNKIGR ITGLDPAGPM FEGTSPNERL SPDDANFVDA IHTFTREHMG LSVGIKQPIA 

       250        260        270        280        290        300 
HYDFYPNGGS FQPGCHFLEL YKHIAEHGLN AITQTIKCAH ERSVHLFIDS LQHSDLQSIG 

       310        320        330        340        350        360 
FQCSDMGSFS QGLCLSCKKG RCNTLGYDIR KDRSGKSKRL FLITRAQSPF KVYHYQFKIQ 

       370        380        390        400        410        420 
FINQIEKPVE PTFTMSLLGT KEEIKRIPIT LGEGITSNKT YSFLITLDKD IGELILLKFK 

       430        440        450        460        470        480 
WENSAVWANV WNTVQTIMLW GIEPHHSGLI LKTIWVKAGE TQQRMTFCPE NLDDLQLHPS 

       490        500        510 
QEKVFVNCEV KSKRLTESKE QMSQETHAKK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of mouse hepatic triacylglycerol lipase: gene expression in combined lipase-deficient (cld/cld) mice."
Oka K., Nakano T., Tkalcevic G.T., Scow R.O., Brown W.V.
Biochim. Biophys. Acta 1089:13-20(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of cDNA encoding the mouse hepatic triglyceride lipase and expression by in vitro translation."
Chang S.F., Netter H.J., Will H.
FEBS Lett. 289:69-72(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Liver.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY228765 mRNA. Translation: AAO73443.1.
X58426 mRNA. Translation: CAA41329.1.
CH466522 Genomic DNA. Translation: EDL26212.1.
BC021841 mRNA. Translation: AAH21841.1.
BC094050 mRNA. Translation: AAH94050.1.
CCDSCCDS23324.1.
PIRS15893.
RefSeqNP_032306.2. NM_008280.2.
UniGeneMm.390187.

3D structure databases

ProteinModelPortalP27656.
SMRP27656. Positions 37-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200409. 27 interactions.
STRING10090.ENSMUSP00000034731.

PTM databases

PhosphoSiteP27656.

Proteomic databases

PaxDbP27656.
PRIDEP27656.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034731; ENSMUSP00000034731; ENSMUSG00000032207.
GeneID15450.
KEGGmmu:15450.
UCSCuc009qos.1. mouse.

Organism-specific databases

CTD3990.
MGIMGI:96216. Lipc.

Phylogenomic databases

eggNOGNOG81747.
GeneTreeENSGT00750000117234.
HOGENOMHOG000038553.
HOVERGENHBG002259.
InParanoidQ8VC44.
KOK01046.
OMACHFLELY.
OrthoDBEOG757CX5.
TreeFamTF324997.

Gene expression databases

ArrayExpressP27656.
BgeeP27656.
CleanExMM_LIPC.
GenevestigatorP27656.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR002333. Lipase_hep.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF2. PTHR11610:SF2. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00824. HEPLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288252.
PROP27656.
SOURCESearch...

Entry information

Entry nameLIPC_MOUSE
AccessionPrimary (citable) accession number: P27656
Secondary accession number(s): Q8VC44
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot