Reviewed, UniProtKB/Swiss-Prot P07867 (LIPC_RAT)

Names and origin

Protein names

Recommended name:
    Hepatic triacylglycerol lipase
      Short name=Hepatic lipase
      Short name=HL
    EC=3.1.1.3
Alternative name(s):
    Lipase member C

Gene names

Name:

Lipc

Organism

Rattus norvegicus (Rat)

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
Cellular component	HDL Secreted
Domain	Signal
Ligand	Heparin-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	cellular response to hormone stimulus Inferred from expression pattern. Source: RGD chylomicron remnant clearance Inferred from direct assay. Source: RGD chylomicron remodeling Inferred from direct assay. Source: RGD circadian rhythm Inferred from expression pattern. Source: RGD developmental growth Inferred from expression pattern. Source: RGD fatty acid metabolic process Inferred from direct assay. Source: RGD glycerophospholipid catabolic process Inferred from direct assay. Source: RGD heparan sulfate proteoglycan biosynthetic process Inferred from direct assay. Source: RGD high-density lipoprotein particle remodeling Inferred from direct assay. Source: RGD liver development Inferred from expression pattern. Source: RGD low-density lipoprotein particle clearance Inferred from direct assay. Source: RGD low-density lipoprotein particle remodeling Inferred from direct assay. Source: RGD mRNA metabolic process Inferred from mutant phenotype. Source: RGD neutral lipid catabolic process Inferred from direct assay. Source: RGD phosphatidic acid metabolic process Inferred from direct assay. Source: RGD phosphatidylcholine metabolic process Inferred from direct assay. Source: RGD phosphatidylethanolamine metabolic process Inferred from direct assay. Source: RGD phosphatidylserine metabolic process Inferred from direct assay. Source: RGD protein oligomerization Inferred from direct assay. Source: RGD response to acetate Inferred from expression pattern. Source: RGD response to amino acid stimulus Inferred from expression pattern. Source: RGD response to calcium ion Inferred from expression pattern. Source: RGD response to carbohydrate stimulus Inferred from expression pattern. Source: RGD response to copper ion Inferred from expression pattern. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to fatty acid Inferred from expression pattern. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern. Source: RGD response to hypoxia Inferred from expression pattern. Source: RGD response to magnesium ion Inferred from expression pattern. Source: RGD response to nutrient levels Inferred from expression pattern. Source: RGD response to organic cyclic substance Inferred from expression pattern. Source: RGD response to peptide hormone stimulus Inferred from expression pattern. Source: RGD response to protein stimulus Inferred from expression pattern. Source: RGD triglyceride metabolic process Inferred from direct assay. Source: RGD very-low-density lipoprotein particle remodeling Inferred from direct assay. Source: RGD
Cellular component	cell surface Inferred from direct assay. Source: RGD early endosome Inferred from direct assay. Source: RGD high-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW late endosome Inferred from direct assay. Source: RGD microvillus Inferred from direct assay. Source: RGD
Molecular function	acylglycerol lipase activity Inferred from direct assay. Source: RGD acyltransferase activity Inferred from direct assay. Source: RGD apolipoprotein binding Inferred from physical interaction. Source: UniProtKB heparan sulfate proteoglycan binding Inferred from mutant phenotype. Source: RGD heparin binding Inferred from direct assay. Source: RGD lipid binding Inferred from direct assay. Source: RGD low-density lipoprotein binding Inferred from direct assay. Source: UniProtKB lysophospholipase activity Inferred from direct assay. Source: RGD phospholipase A1 activity Inferred from direct assay. Source: RGD triglyceride lipase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Chain	23 – 494	472	Hepatic triacylglycerol lipase		PRO_0000017771
Regions
	Domain	353 – 487	135	PLAT
	Region	183 – 194	12	Heparin-binding Potential
Sites
	Active site	169	1	Nucleophile By similarity
	Active site	195	1	Charge relay system By similarity
	Active site	280	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	398	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	277	1	N → K in AAA41335. Ref.2
	Sequence conflict	302	1	Q → H in AAA41335. Ref.2
	Sequence conflict	308	1	S → T in AAA41335. Ref.2
	Sequence conflict	335	1	V → A in AAA41335. Ref.2
	Sequence conflict	369	1	M → I in AAA41335. Ref.2
	Sequence conflict	408	1	N → D in AAA41335. Ref.2
	Sequence conflict	451	1	V → L in AAA41335. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P07867-1 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: 2A9461B1F80845EA	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

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: 2322583] [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: 3470738] [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
SMR	P07867. Positions 27-471.
ModBase	Search...
Protein-protein interaction databases
STRING	P07867.
Genome annotation databases
Ensembl	ENSRNOT00000066166; ENSRNOP00000063453; ENSRNOG00000015747; Rattus norvegicus. [Genome view]
UCSC	NM_012597. rat.
Organism-specific databases
RGD	3009. Lipc.
Phylogenomic databases
eggNOG	roNOG15023.
HOVERGEN	P07867.
InParanoid	P07867.
Enzyme and pathway databases
BRENDA	3.1.1.3. 248.
Gene expression databases
ArrayExpress	P07867.
Genevestigator	P07867.
GermOnline	ENSRNOG00000015747. Rattus norvegicus.
Family and domain databases
InterPro	IPR000734. Lipase. IPR002333. Lipase_hep. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view]
PANTHER	PTHR11610. Lipase. 1 hit. PTHR11610:SF2. Lipase_hep. 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]
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:	January 19, 2010
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)