Hepatic triacylglycerol lipase precursor

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P27656 (LIPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Cellular component	HDL Secreted
Domain	Signal
Ligand	Heparin-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol 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: Compara high-density lipoprotein particle remodeling Inferred from electronic annotation. Source: Compara low-density lipoprotein particle remodeling Inferred from electronic annotation. Source: Compara triglyceride catabolic process Inferred from electronic annotation. Source: Compara triglyceride homeostasis Inferred from electronic annotation. Source: Compara very-low-density lipoprotein particle remodeling Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from direct assay PubMed 15995171. Source: MGI high-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW lipase activity Inferred from direct assay PubMed 12975454 PubMed 15995171. Source: MGI retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

By similarity

Chain

23 – 510

488

Hepatic triacylglycerol lipase

PRO_0000017770

Regions

Domain

353 – 487

135

PLAT

Region

183 – 194

Heparin-binding Potential

Sites

Active site

169

Nucleophile By similarity

Active site

195

Charge relay system By similarity

Active site

280

Charge relay system By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

398

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

286

L → P in CAA41329. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P27656 [UniParc].

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

510

57,389

        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' referencesShow '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.
IPI	IPI00331108.
PIR	S15893.
RefSeq	NP_032306.2. NM_008280.2.
UniGene	Mm.390187.
3D structure databases
ProteinModelPortal	P27656.
SMR	P27656. Positions 37-471.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000034731.
PTM databases
PhosphoSite	P27656.
Proteomic databases
PaxDb	P27656.
PRIDE	P27656.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034731; ENSMUSP00000034731; ENSMUSG00000032207.
GeneID	15450.
KEGG	mmu:15450.
UCSC	uc009qos.1. mouse.
Organism-specific databases
CTD	3990.
MGI	MGI:96216. Lipc.
Phylogenomic databases
eggNOG	NOG81747.
GeneTree	ENSGT00560000077136.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	Q8VC44.
KO	K01046.
OMA	CHFLELY.
OrthoDB	EOG47D9G8.
Gene expression databases
ArrayExpress	P27656.
Bgee	P27656.
CleanEx	MM_LIPC.
Genevestigator	P27656.
GermOnline	ENSMUSG00000032207. Mus musculus.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR000734. Lipase. IPR002333. Lipase_hep. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view]
PANTHER	PTHR11610. PTHR11610. 1 hit. PTHR11610:SF2. PTHR11610:SF2. 1 hit.
Pfam	PF00151. Lipase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PIRSF	PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTS	PR00824. HEPLIPASE. PR00821. TAGLIPASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
SUPFAM	SSF49723. Lipase_LipOase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	288252.
SOURCE	Search...

Entry information

Entry name

LIPC_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents