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Reviewed, UniProtKB/Swiss-Prot P11602 (LIPL_CHICK)

Last modified October 13, 2009. Version 84. 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

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Names and origin

Protein namesRecommended name:
    Lipoprotein lipase
      Short name=LPL
    EC=3.1.1.34
Gene names
Name: LPL
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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-anchor › GPI-anchor.

Post-translational modification

N-glycan at Asn-70 is a triantennary complex oligosaccharide containing sialic acid, galactose, mannose, and N-acetylglucosamine, the reducing GlcNAc being sulfated at C6.

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Contains 1 PLAT domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 490465Lipoprotein lipase Ref.1
PRO_0000017782

Regions

Domain341 – 464124PLAT
Region319 – 33113Heparin-binding Potential

Sites

Active site1591Nucleophile By similarity
Active site1831Charge relay system By similarity
Active site2681Charge relay system By similarity

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) (complex) Ref.3
Glycosylation3541N-linked (GlcNAc...) Ref.3
Glycosylation3861N-linked (GlcNAc...) Ref.3
Disulfide bond54 ↔ 67 By similarity
Disulfide bond243 ↔ 266 By similarity
Disulfide bond291 ↔ 310 By similarity
Disulfide bond302 ↔ 305 By similarity
Disulfide bond445 ↔ 465 By similarity

Experimental info

Sequence conflict3771P → A in CAA43037. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P11602-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: C014D23363E81FF3

FASTA49055,132
        10         20         30         40         50         60 
MERGRGMGKT ALLAVLCLCL RGAAGSDPEA EMNFEGIESK FSLRTPAEPD EDVCYLVPGQ 

        70         80         90        100        110        120 
MDSLAQCNFN HTSKTFVVIH GWTVTGMYES WVPKLVDALY KREPDSNVIV VDWLVRAQQH 

       130        140        150        160        170        180 
YPVSAAYTKL VGKDVAMFID WMEEKFNYPL NNVHLLGYSL GAHAAGIAGS LTKKKVNRIT 

       190        200        210        220        230        240 
GLDPAGPTFE YADAPIRLSP DDADFVDVLH TYTRGSPDRS IGIQKPVGHI DIYPNGGGFQ 

       250        260        270        280        290        300 
PGCNLGEALR LIAEKGFSDV DQLVKCSHER SIHLFIDSLL YEEKPSMAYR CNTKEAFEKG 

       310        320        330        340        350        360 
LCLSCRKNRC NNLGYKVNRV RTKRNTKMYL KTRAQMPYKV FHYQVKIHFF GKTNVTKVDQ 

       370        380        390        400        410        420 
PFLISLYGTL DESENIPFTL PEVSSNKTFS FLIYTEVDIG DLLMLKLQWE KDTFFSWSDW 

       430        440        450        460        470        480 
WTPFAFTIQR VRVKSGETQK KVVFCSRDGS SRLGKGEEAA IFVKCLEQPV SRKRGGAKKA 

       490 
SKENSAHESA

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References

[1]"Avian adipose lipoprotein lipase: cDNA sequence and reciprocal regulation of mRNA levels in adipose and heart."
Cooper D.A., Stein J.C., Strieleman P.J., Bensadoun A.
Biochim. Biophys. Acta 1008:92-101(1989) [PubMed: 2719965] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Leghorn Cornell K.
Tissue: Adipose tissue.
[2]"The structure and complete nucleotide sequence of the avian lipoprotein lipase gene."
Cooper D.A., Lu S.C., Viswanath R., Freiman R.N., Bensadoun A.
Biochim. Biophys. Acta 1129:166-171(1992) [PubMed: 1730055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: White leghorn.
[3]"Occurrence of sulfate in an asparagine-linked complex oligosaccharide of chicken adipose lipoprotein lipase."
Hoogewerf A.J., Bensadoun A.
J. Biol. Chem. 266:1048-1057(1991) [PubMed: 1985932] [Abstract]
Cited for: GLYCOSYLATION AT ASN-70; ASN-354 AND ASN-386, STRUCTURE OF CARBOHYDRATE.

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Cross-references

Sequence databases

X14670 mRNA. Translation: CAA32800.1.
X60547 Genomic DNA. Translation: CAA43037.1.
IPIIPI00582446.
PIRS04331.
RefSeqNP_990613.1.
UniGeneGga.1152

3D structure databases

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

Protein-protein interaction databases

STRINGP11602.

Genome annotation databases

EnsemblENSGALT00000037774; ENSGALP00000036979; ENSGALG00000015425; Gallus gallus. [Genome view]
GeneID396219.
KEGGgga:396219.

Organism-specific databases

CTD396219.

Phylogenomic databases

HOGENOMP11602.
HOVERGENP11602.

Enzyme and pathway databases

BRENDA3.1.1.34. 4.

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]
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...

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Entry information

Entry nameLIPL_CHICK
AccessionPrimary (citable) accession number: P11602
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 13, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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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