Hepatic triacylglycerol lipase precursor

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P07867 (LIPC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. History...

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

Documents (1) |

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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	494 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	cellular response to hormone stimulus Inferred from expression pattern PubMed 12234100. Source: RGD chylomicron remnant clearance Inferred from direct assay PubMed 8192680. Source: RGD chylomicron remodeling Inferred from direct assay PubMed 7897313. Source: RGD circadian rhythm Inferred from expression pattern PubMed 9728079. Source: RGD developmental growth Inferred from expression pattern PubMed 1391269. Source: RGD fatty acid metabolic process Inferred from direct assay PubMed 10734075. Source: RGD glycerophospholipid catabolic process Inferred from direct assay PubMed 9048565. Source: RGD heparan sulfate proteoglycan biosynthetic process Inferred from direct assay PubMed 15102889. Source: RGD high-density lipoprotein particle remodeling Inferred from direct assay PubMed 8157689. Source: RGD liver development Inferred from expression pattern PubMed 11004003. Source: RGD low-density lipoprotein particle clearance Inferred from direct assay PubMed 8071607. Source: RGD low-density lipoprotein particle remodeling Inferred from direct assay PubMed 8071607. Source: RGD mRNA metabolic process Inferred from mutant phenotype PubMed 9822677. Source: RGD neutral lipid catabolic process Inferred from direct assay PubMed 1865764. Source: RGD phosphatidic acid metabolic process Inferred from direct assay PubMed 2223857. Source: RGD phosphatidylcholine metabolic process Inferred from direct assay PubMed 2223857. Source: RGD phosphatidylethanolamine metabolic process Inferred from direct assay PubMed 2223857. Source: RGD phosphatidylserine metabolic process Inferred from direct assay PubMed 2223857. Source: RGD protein oligomerization Inferred from direct assay PubMed 9540793. Source: RGD response to acetate Inferred from expression pattern PubMed 11427199. Source: RGD response to amino acid stimulus Inferred from expression pattern PubMed 19212806. Source: RGD response to calcium ion Inferred from expression pattern PubMed 9480878. Source: RGD response to carbohydrate stimulus Inferred from expression pattern PubMed 15744060. Source: RGD response to copper ion Inferred from expression pattern PubMed 3420106. Source: RGD response to drug Inferred from expression pattern PubMed 8322779. Source: RGD response to fatty acid Inferred from expression pattern PubMed 2086700. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern PubMed 15271879. Source: RGD response to hypoxia Inferred from expression pattern PubMed 15271879. Source: RGD response to magnesium ion Inferred from expression pattern PubMed 2046484. Source: RGD response to nutrient levels Inferred from expression pattern PubMed 19165521. Source: RGD response to peptide hormone stimulus Inferred from expression pattern PubMed 16546477. Source: RGD triglyceride metabolic process Inferred from direct assay PubMed 10734075. Source: RGD very-low-density lipoprotein particle remodeling Inferred from direct assay PubMed 6791934. Source: RGD
Cellular_component	cell surface Inferred from direct assay PubMed 384999. Source: RGD early endosome Inferred from direct assay PubMed 14701798. Source: RGD extracellular space Inferred from direct assay PubMed 18691644. Source: RGD high-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW late endosome Inferred from direct assay PubMed 14701798. Source: RGD microvillus Inferred from direct assay PubMed 9020876. Source: RGD
Molecular_function	acylglycerol lipase activity Inferred from direct assay PubMed 6696938. Source: RGD apolipoprotein binding Inferred from direct assay PubMed 9685400. Source: RGD carboxylesterase activity Inferred from direct assay PubMed 1940628. Source: RGD heparan sulfate proteoglycan binding Inferred from mutant phenotype PubMed 15102889. Source: RGD heparin binding Inferred from direct assay PubMed 10681410. Source: RGD lipid binding Inferred from direct assay PubMed 1865764. Source: RGD low-density lipoprotein particle binding Inferred from direct assay PubMed 9685400. Source: BHF-UCL lysophospholipase activity Inferred from direct assay PubMed 1531641. Source: RGD phosphatidylcholine 1-acylhydrolase activity Inferred from direct assay PubMed 1531641. Source: RGD retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC transferase activity, transferring acyl groups Inferred from direct assay PubMed 9048565. Source: RGD triglyceride lipase activity Inferred from direct assay PubMed 10734075 PubMed 15102889 PubMed 1865764. Source: RGD
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 – 494

472

Hepatic triacylglycerol lipase

PRO_0000017771

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

277

N → K in AAA41335. Ref.2

Sequence conflict

302

Q → H in AAA41335. Ref.2

Sequence conflict

308

S → T in AAA41335. Ref.2

Sequence conflict

335

V → A in AAA41335. Ref.2

Sequence conflict

369

M → I in AAA41335. Ref.2

Sequence conflict

408

N → D in AAA41335. Ref.2

Sequence conflict

451

V → L in AAA41335. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P07867 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 2A9461B1F80845EA
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FASTA

494

55,623

        10         20         30         40         50         60 
MGNHLQISVS LVLCIFIQSS ACGQGVGTEP FGRNLGATEE RKPLQKPEIR FLLFKDESDR 

        70         80         90        100        110        120 
LGCQLRPQHP ETLQECGFNS SHPLVMIIHG WSVDGLLETW IWKIVGALKS RQSQPVNVGL 

       130        140        150        160        170        180 
VDWISLAYQH YAIAVRNTRV VGQEVAALLL WLEESMKFSR SKVHLIGYSL GAHVSGFAGS 

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

       250        260        270        280        290        300 
HYDFYPNGGS FQPGCHFLEL YKHIAEHGLN AITQTINCAH ERSVHLFIDS LQHSNLQNTG 

       310        320        330        340        350        360 
FQCSNMDSFS QGLCLNCKKG RCNSLGYDIR RIGHVKSKTL FLITRAQSPF KVYHYQFKIQ 

       370        380        390        400        410        420 
FINQMEKPME PTFTMTLLGT KEEIKKIPIT LGEGITSNKT YSLLITLNKD IGELIMLKFK 

       430        440        450        460        470        480 
WENSAVWANV WNTVQTIMLW DTEPHYAGLI VKTIWVKAGE TQQRMTFCPD NVDDLQLHPT 

       490 
QEKVFVKCDL KSKD

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References

[1]	"Isolation and characterization of clones for the rat hepatic lipase gene upstream regulatory region." Sensel M.G., Legrand-Lorans A., Wang M.E., Bensadoun A. Biochim. Biophys. Acta 1048:297-302(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"Cloning of rat hepatic lipase cDNA: evidence for a lipase gene family." Komaromy M.C., Schotz M.C. Proc. Natl. Acad. Sci. U.S.A. 84:1526-1530(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X17366 mRNA. Translation: CAA35241.1. X17367 Genomic DNA. Translation: CAA35242.1. M16235 mRNA. Translation: AAA41335.1.
IPI	IPI00393187.
PIR	A27442.
UniGene	Rn.1195.
3D structure databases
ProteinModelPortal	P07867.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000062312.
Proteomic databases
PaxDb	P07867.
PRIDE	P07867.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:3009. rat.
Organism-specific databases
RGD	3009. Lipc.
Phylogenomic databases
eggNOG	NOG81747.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	P07867.
Gene expression databases
ArrayExpress	P07867.
Genevestigator	P07867.
GermOnline	ENSRNOG00000015747. Rattus norvegicus.
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...

Entry information

Entry name

LIPC_RAT

Accession

Primary (citable) accession number: P07867

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1990
Last modified:	April 3, 2013
This is version 117 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

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

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents