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Reviewed, UniProtKB/Swiss-Prot P11152 (LIPL_MOUSE)

Last modified October 13, 2009. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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). 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. Ref.8

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 – 2727 Potential
Chain28 – 474447Lipoprotein lipase
PRO_0000017776

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...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
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 conflict1291K → Y Ref.1
Sequence conflict1471N → K in AAA39441. Ref.2
Sequence conflict3541N → D in BAB22256. Ref.3
Sequence conflict4101M → I in BAB22256. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P11152-1 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: E7AF969E716E1CCD

FASTA47453,126
        10         20         30         40         50         60 
MESKALLLVV LGVWLQSLTA FRGGVAAADA GRDFSDIESK FALRTPEDTA EDTCHLIPGL 

        70         80         90        100        110        120 
ADSVSNCHFN HSSKTFVVIH GWTVTGMYES WVPKLVAALY KREPDSNVIV VDWLYRAQQH 

       130        140        150        160        170        180 
YPVSAGYTKL VGNDVARFIN WMEEEFNYPL DNVHLLGYSL GAHAAGVAGS LTNKKVNRIT 

       190        200        210        220        230        240 
GLDPAGPNFE YAEAPSRLSP DDADFVDVLH TFTRGSPGRS IGIQKPVGHV DIYPNGGTFQ 

       250        260        270        280        290        300 
PGCNIGEAIR VIAERGLGDV DQLVKCSHER SIHLFIDSLL NEENPSKAYR CNSKEAFEKG 

       310        320        330        340        350        360 
LCLSCRKNRC NNLGYEINKV RAKRSSKMYL KTRSQMPYKV FHYQVKIHFS GTENGKQHNQ 

       370        380        390        400        410        420 
AFEISLYGTV AESENIPFTL PEVSTNKTYS FLIYTEVDIG ELLMMKLKWM SDSYFSWPDW 

       430        440        450        460        470 
WSSPSFVIER IRVKAGETQK KVIFCAREKV SHLQKGKDSA VFVKCHDKSL KKSG 

« Hide

References

« Hide 'large scale' references
[1]"Lipoprotein lipase and hepatic lipase mRNA tissue specific expression, developmental regulation, and evolution."
Semenkovich C.F., Chen S.H., Wims M., Luo C.C., Li W.H., Chan L.
J. Lipid Res. 30:423-431(1989) [PubMed: 2723548] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[2]"The structure of the mouse lipoprotein lipase gene: a B1 repetitive element is inserted into the 3' untranslated region of the mRNA."
Zechner R., Newman T.C., Steiner E., Breslow J.L.
Genomics 11:62-76(1991) [PubMed: 1765386] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head and Kidney.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Adipogenesis in a myeloid supporting bone marrow stromal cell line."
Gimble J.M., Hua X., Youkhana K., Bass H.W., Medina K., Sullivan M., Greenberger J.S., Wang C.S.
J. Cell. Biochem. 50:73-82(1992) [PubMed: 1339460] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-183.
[6]"Cloning and characterization of the promoter of the murine lipoprotein lipase-encoding gene: structural and functional analysis."
Hua X., Enerbaeck S., Hudson J., Youkhana K., Gimble J.M.
Gene 107:247-258(1991) [PubMed: 1748295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
Strain: BALB/c.
Tissue: Liver.
[7]"The sequence of cDNA encoding lipoprotein lipase. A member of a lipase gene family."
Kirchgessner T.G., Svenson K.L., Lusis A.J., Schotz M.C.
J. Biol. Chem. 262:8463-8466(1987) [PubMed: 3597382] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-474.
[8]"Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons."
Beigneux A.P., Davies B.S.J., Gin P., Weinstein M.M., Farber E., Qiao X., Peale F., Bunting S., Walzem R.L., Wong J.S., Blaner W.S., Ding Z.-M., Melford K., Wongsiriroj N., Shu X., de Sauvage F., Ryan R.O., Fong L.G., Bensadoun A., Young S.G.
Cell Metab. 5:279-291(2007) [PubMed: 17403372] [Abstract]
Cited for: INTERACTION WITH GPIHBP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

M60847 expand/collapse EMBL AC list , M60838, M60839, M60840, M60842, M60843, M60844, M60845, M60846 Genomic DNA. Translation: AAA39441.1.
AK002645 mRNA. Translation: BAB22256.1.
AK017272 mRNA. No translation available.
BC003305 mRNA. Translation: AAH03305.1.
M65258 mRNA. Translation: AAA39442.1.
J03302 mRNA. Translation: AAA39440.1.
M63335 Genomic DNA. Translation: AAC04464.1.
IPIIPI00319188.
PIRA40570.
RefSeqNP_032535.2.
XP_001476512.1.
UniGeneMm.1514

3D structure databases

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

Protein-protein interaction databases

STRINGP11152.

Proteomic databases

PRIDEP11152.

Genome annotation databases

EnsemblENSMUST00000015712; ENSMUSP00000015712; ENSMUSG00000015568; Mus musculus. [Genome view]
GeneID16956.
669888.
KEGGmmu:16956.
mmu:669888.

Organism-specific databases

MGIMGI:96820. Lpl.

Phylogenomic databases

HOGENOMP11152.
HOVERGENP11152.

Enzyme and pathway databases

BRENDA3.1.1.34. 244.

Gene expression databases

ArrayExpressP11152.
BgeeP11152.
CleanExMM_LPL.
GenevestigatorP11152.
GermOnlineENSMUSG00000015568. Mus musculus.

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...

Other Resources

NextBio436339.
SOURCESearch...

Entry information

Entry nameLIPL_MOUSE
AccessionPrimary (citable) accession number: P11152
Secondary accession number(s): Q05956, Q9D3M9, Q9DCM8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1993
Last modified: October 13, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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