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Reviewed, UniProtKB/Swiss-Prot P11153 (LIPL_CAVPO)

Last modified October 13, 2009. Version 80. 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:
    Lipoprotein lipase
      Short name=LPL
    EC=3.1.1.34
Gene names
Name: LPL
OrganismCavia porcellus (Guinea pig)
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). The enzyme functions in the presence of apolipoprotein C-2 on the luminal surface of vascular endothelium.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Subunit structure

Homodimer. Interacts with apolipoprotein C-2. Interacts with GPIHBP1.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 465448Lipoprotein lipase
PRO_0000017773

Regions

Domain331 – 454124PLAT
Region309 – 32113Heparin-binding Potential

Sites

Active site1491Nucleophile By similarity
Active site1731Charge relay system By similarity
Active site2581Charge relay system By similarity

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Disulfide bond44 ↔ 57 By similarity
Disulfide bond233 ↔ 256 By similarity
Disulfide bond281 ↔ 300 By similarity
Disulfide bond292 ↔ 295 By similarity
Disulfide bond435 ↔ 455 By similarity

Sequences

Sequence LengthMass (Da)Tools
P11153-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: E2515F36BEFD5F10

FASTA46552,781
        10         20         30         40         50         60 
MNIDRKILNK ALAKEKVANC QKDYTDIESK FARRTPENTV EDTCHLIPGV TESVANCHFN 

        70         80         90        100        110        120 
HSSKTFMVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLRRAQHH YPESADYTKL 

       130        140        150        160        170        180 
VGEDVARFIN WMEDEFKYSV DNVHLLGYSL GAHAAGVAGS RTNTKVSRIT GLDPAGPNFE 

       190        200        210        220        230        240 
YAEATSRLSP DDAQFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGSFQ PGCNIQDALR 

       250        260        270        280        290        300 
VISQKGFGDM DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG LCLSCRKNRC 

       310        320        330        340        350        360 
NNVGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIYFS GTETTTYTNQ AFEISLYGTV 

       370        380        390        400        410        420 
AESENIPFTL PEVSANNTYS FLIYTEVDIG ELLMLKLKWI TESYFSWSSW WGRPTFTIEK 

       430        440        450        460 
IRVKAGETQK KIVFCSREKV SKLQKGKEAP VFVKCHDKSL NKKSG 

« Hide

References

[1]"Molecular cloning and sequence analysis of cDNA encoding lipoprotein lipase of guinea pig."
Enerbaeck S., Semb H., Bengtsson-Olivecrona G., Carlsson P., Hermansson M.-L., Olivecrona T., Bjursell G.
Gene 58:1-12(1987) [PubMed: 3692172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic organization of the region encoding guinea pig lipoprotein lipase; evidence for exon fusion and unconventional splicing."
Enerbaeck S., Bjursell G.
Gene 84:391-397(1989) [PubMed: 2612912] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

M15483 mRNA. Translation: AAA37046.1.
M33381 expand/collapse EMBL AC list , M33377, M33378, M33379, M33380 Genomic DNA. Translation: AAA37039.1.
PIRA27330. JS0398.

3D structure databases

HSSPHSSP built from PDB template 1RP1 based on UniProtKB P06857.
ModBaseSearch...

Genome annotation databases

EnsemblENSCPOT00000004098; ENSCPOP00000003655; ENSCPOG00000004054; Cavia porcellus. [Genome view]
ENSCPOT00000004099; ENSCPOP00000003656; ENSCPOG00000004054; Cavia porcellus. [Genome view]

Phylogenomic databases

HOVERGENP11153.

Enzyme and pathway databases

BRENDA3.1.1.34. 44.

Family and domain databases

InterProIPR000734. Lipase.
IPR013818. Lipase_N.
IPR008262. Lipase_Ser_AS.
IPR002330. Lipo_Lipase.
IPR001024. LipOase_LH2.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
Gene3DG3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHERPTHR11610. Lipase. 1 hit.
PTHR11610:SF3. Lipase_lipo. 1 hit.
PfamPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00822. LIPOLIPASE.
PR00821. TAGLIPASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
TIGRFAMsTIGR03230. lipo_lipase. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIPL_CAVPO
AccessionPrimary (citable) accession number: P11153
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 13, 2009
This is version 80 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