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Reviewed, UniProtKB/Swiss-Prot O46559 (LIPC_RABIT)

Last modified January 19, 2010. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length499 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 By similarity.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentHDL
Secreted
   DomainSignal
   LigandHeparin-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componenthigh-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride lipase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 499477Hepatic triacylglycerol lipase
PRO_0000233341

Regions

Domain352 – 486135PLAT
Region181 – 19313Heparin-binding Potential

Sites

Active site1681Nucleophile By similarity
Active site1941Charge relay system By similarity
Active site2791Charge relay system By similarity

Amino acid modifications

Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O46559-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 4DA7D65EE815A0A5

FASTA49955,814
        10         20         30         40         50         60 
MGSPLCVPIF LAVCILIQSS THGQSLRPEP FGRRARVTAT KKTLLETETR FLLFKDKANK 

        70         80         90        100        110        120 
GCQIRLHHAD TLQECGFNSS LPLVMIVHGW SVDGLLESWI WQMVAALKSQ PARPVNVGLV 

       130        140        150        160        170        180 
DWISLAHSHY AVAVRNARLV GQEVAALLQW LEESAPFSRS NVHLIGYSLG AHVAGFAGSY 

       190        200        210        220        230        240 
ISGKHKIGRI TGLDAAGPLF EGTSASDRLS PDDATFVDAI HTFTREHMGL SVGIKQPVGH 

       250        260        270        280        290        300 
YDFYPNGGSF QPGCHFLELY KHIAQHGLNA LSQTIKCAHE RSVHLFIDSL LHPSMQSTAY 

       310        320        330        340        350        360 
QCSDMDSFSQ GLCLGCTKGR CNTLGYHIRQ EPLSKGKRLF LVTQAQSPFR VYHYQFKIQF 

       370        380        390        400        410        420 
INQIEKPLEP TFTMSLLGTK EEMQKIPITL GEGITSNKTY SFLITLNLDI GELMVIKFKW 

       430        440        450        460        470        480 
ENSAVWANVW NTVQTIIPWG IKPRNSGLIL KTIRVKAGET QQRMTFCSEN MDDLQLHPTQ 

       490 
EKNFVRCEVN PKKLKLKIK 

« Hide

References

[1]"Rabbit hepatic lipase cDNA sequence: low activity is associated with low messenger RNA levels."
Warren R.J., Ebert D.L., Mitchell A., Barter P.J.
J. Lipid Res. 32:1333-1339(1991) [PubMed: 1770315] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Warren R.J., Ebert D.L., Mitchell A., Barter P.J.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041202 mRNA. Translation: AAB96786.1.
RefSeqNP_001075501.1.
UniGeneOcu.2193

3D structure databases

SMRO46559. Positions 45-472.
ModBaseSearch...

Protein-protein interaction databases

STRINGO46559.

Genome annotation databases

GeneID100008678.

Organism-specific databases

CTD100008678.

Phylogenomic databases

eggNOGmaNOG15677.
HOVERGENO46559.

Enzyme and pathway databases

BRENDA3.1.1.3. 255.

Family and domain databases

InterProIPR000734. Lipase.
IPR002333. Lipase_hep.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
PANTHERPTHR11610. Lipase. 1 hit.
PTHR11610:SF2. Lipase_hep. 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]
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIPC_RABIT
AccessionPrimary (citable) accession number: O46559
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 1998
Last modified: January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents