Lipoprotein lipase precursor - Gallus gallus (Chicken)

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P11602 (LIPL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. 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:
Lipoprotein lipase
Short name=LPL
EC=3.1.1.34

Gene names

Name:

LPL

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium By similarity.
Catalytic activity	Triacylglycerol + H₂O = diacylglycerol + a carboxylate.
Subunit structure	Homodimer By similarity. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids By similarity.
Subcellular location	Cell membrane By similarity; Lipid-anchor › GPI-anchor By similarity. Secreted By similarity. Note: Locates to the plasma membrane of microvilli of hepatocytes with triacyl-glycerol-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles By similarity.
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. Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity By similarity.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Cell membrane Chylomicron Membrane Secreted VLDL
Domain	Signal
Ligand	Heparin-binding
Molecular function	Hydrolase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Nitration
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of cholesterol storage Inferred from electronic annotation. Source: Compara positive regulation of macrophage derived foam cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of sequestering of triglyceride Inferred from electronic annotation. Source: Compara triglyceride catabolic process Inferred from electronic annotation. Source: Compara triglyceride homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell surface Inferred from electronic annotation. Source: Compara chylomicron Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell very-low-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW lipoprotein lipase activity Inferred from electronic annotation. Source: EC triglyceride lipase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

Chain

26 – 490

465

Lipoprotein lipase Ref.1

PRO_0000017782

Regions

Domain

341 – 464

124

PLAT

Region

346 – 441

Heparin-binding

Sites

Active site

159

Nucleophile By similarity

Active site

183

Charge relay system By similarity

Active site

268

Charge relay system By similarity

Amino acid modifications

Modified residue

121

Nitrated tyrosine By similarity

Modified residue

191

Nitrated tyrosine By similarity

Modified residue

343

Nitrated tyrosine By similarity

Glycosylation

N-linked (GlcNAc...) (complex) Ref.3

Glycosylation

354

N-linked (GlcNAc...) Ref.3

Glycosylation

386

N-linked (GlcNAc...) Ref.3

Disulfide bond

54 ↔ 67

By similarity

Disulfide bond

243 ↔ 266

By similarity

Disulfide bond

291 ↔ 310

By similarity

Disulfide bond

302 ↔ 305

By similarity

Disulfide bond

445 ↔ 465

By similarity

Experimental info

Mutagenesis

306

R → Q: Some loss of heparin-binding ability; when associated with Q-307 and Q-309. Ref.4

Mutagenesis

307

K → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-309. Ref.4

Mutagenesis

309

R → Q: Some loss of heparin-binding ability; when associated with Q-306 and Q-307. Ref.4

Mutagenesis

346

K → N: Reduced heparin-binding ability and some decrease in specific enzymatic activity. Ref.4

Mutagenesis

430

R → N: Reduced heparin-binding ability and some reduction in specific enzymatic activity. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-432 and N-434. Ref.4

Mutagenesis

432

R → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-434. Ref.4

Mutagenesis

434

K → N: Reduced heparin-binding ability. Almost complete loss of heparin binding and greatly reduced specific enzymatic activity; when associated with N-430 and N-432. Ref.4

Mutagenesis

440

K → N: No change in heparin-binding activity nor in specific enzymatic activity. Reduced heparin-binding activity and decreased specific enzymatic activity; when associated with N-441. Ref.4

Mutagenesis

441

K → N: Reduced heparin-binding activity and decreased specific enzymatic activity. No further reduction of heparin-binding nor of specific enzymatic activity; when associated with N-440. Ref.4

Sequence conflict

377

P → A in CAA43037. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P11602 [UniParc].

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

FASTA

490

55,132

        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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: White leghorn. 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-70; ASN-354 AND ASN-386, STRUCTURE OF CARBOHYDRATES.
[4]	"Identification of a heparin-binding domain in the distal carboxyl-terminal region of lipoprotein lipase by site-directed mutagenesis." Sendak R.A., Bensadoun A. J. Lipid Res. 39:1310-1315(1998) [PubMed] [Europe PMC] [Abstract] Cited for: HEPARIN-BINDING DOMAIN, MUTAGENESIS OF ARG-306; LYS-307; ARG-309; LYS-346; ARG-430; ARG-432; LYS-434; LYS-440 AND LYS-441.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14670 mRNA. Translation: CAA32800.1. X60547 Genomic DNA. Translation: CAA43037.1.
IPI	IPI00582446.
PIR	S04331.
RefSeq	NP_990613.1. NM_205282.1.
UniGene	Gga.1152.
3D structure databases
ProteinModelPortal	P11602.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000036979.
Proteomic databases
PaxDb	P11602.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396219.
KEGG	gga:396219.
Organism-specific databases
CTD	4023.
Phylogenomic databases
eggNOG	NOG40923.
HOGENOM	HOG000038553.
HOVERGEN	HBG002259.
InParanoid	P11602.
KO	K01059.
OrthoDB	EOG480HWP.
Gene expression databases
ArrayExpress	P11602.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR000734. Lipase. IPR008976. Lipase_LipOase. IPR013818. Lipase_N. IPR002330. Lipo_Lipase. IPR001024. LipOase_LH2. IPR016272. Lipoprotein_lipase_LIPH. [Graphical view]
PANTHER	PTHR11610. PTHR11610. 1 hit. PTHR11610:SF3. PTHR11610:SF3. 1 hit.
Pfam	PF00151. Lipase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PIRSF	PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTS	PR00822. LIPOLIPASE. PR00821. TAGLIPASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
SUPFAM	SSF49723. Lipase_LipOase. 1 hit.
TIGRFAMs	TIGR03230. lipo_lipase. 1 hit.
PROSITE	PS00120. LIPASE_SER. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20816271.

Entry information

Entry name

LIPL_CHICK

Accession

Primary (citable) accession number: P11602

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 107 of the entry and version 1 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

Other

Entry information

Relevant documents