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Protein

Lysosomal acid lipase/cholesteryl ester hydrolase

Gene

Lipa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation (By similarity).By similarity

Catalytic activityi

A steryl ester + H2O = a sterol + a fatty acid.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei172 – 1721Charge relay systemPROSITE-ProRule annotation
Active sitei372 – 3721Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell morphogenesis Source: MGI
  • cell proliferation Source: MGI
  • cytokine production Source: MGI
  • fatty acid metabolic process Source: Ensembl
  • homeostasis of number of cells within a tissue Source: MGI
  • inflammatory response Source: MGI
  • lipid catabolic process Source: UniProtKB-KW
  • lung development Source: MGI
  • sterol metabolic process Source: Ensembl
  • tissue remodeling Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERimouse-1llip. Acidic_Lipase.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysosomal acid lipase/cholesteryl ester hydrolase (EC:3.1.1.13)
Short name:
Acid cholesteryl ester hydrolase
Short name:
LAL
Alternative name(s):
Cholesteryl esterase
Lipase A
Sterol esterase
Gene namesi
Name:Lipa
Synonyms:Lip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:96789. Lipa.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 397372Lysosomal acid lipase/cholesteryl ester hydrolasePRO_0000017800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)Sequence analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence analysis
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9Z0M5.
MaxQBiQ9Z0M5.
PaxDbiQ9Z0M5.
PRIDEiQ9Z0M5.

PTM databases

iPTMnetiQ9Z0M5.
PhosphoSiteiQ9Z0M5.

Expressioni

Tissue specificityi

Expressed at low levels in most tissues. High level expression is found in hepatocytes and splenic and thymic cells. Very high level expression is observed in cells of the small intestinal villi, the zona fasciculata and reticularis of the adrenal cortex, pancreatic acini, and renal tubular epithelium.

Gene expression databases

BgeeiQ9Z0M5.
CleanExiMM_LIPA.
GenevisibleiQ9Z0M5. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9Z0M5. 2 interactions.
MINTiMINT-4114169.
STRINGi10090.ENSMUSP00000053270.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0M5.
SMRiQ9Z0M5. Positions 22-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiQ9Z0M5.
KOiK01052.
OMAiVCTHVIM.
OrthoDBiEOG71RXJN.
TreeFamiTF315485.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z0M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLQGLVFVF TIGILLSRVP TGTVSAVDPE VNMNVTEIIM RWGYPGEEHS
60 70 80 90 100
VLTGDGYILS IHRIPRGRKN HFGKGPRPVV YLQHGLLADS SNWVTNIDNS
110 120 130 140 150
SLGFLLADAG FDVWMGNSRG NTWSLKHKTL SVSQDEFWAF SFDEMAKYDL
160 170 180 190 200
PASINYILNK TGQEQIYYVG HSQGCTIGFI AFSQMPELAK KIKMFLVLAP
210 220 230 240 250
VLSLNFASGP LLQLGRLPDP LLKDMFGQKQ FLPQSAMLKW LSIHVCTHVI
260 270 280 290 300
MKELCANVFF LLCGFNEKNL NMSRVDVYTT HCPAGTSVQN MLHWGQVFKY
310 320 330 340 350
RKLQAFDWGS SEKNYFHYNQ SFPPSYNIKN MRLPTALWSG GRDWLADIND
360 370 380 390
ITILLTQIPK LVYHKNIPEW DHLDFIWGLD APWKLYDEII SLMKKYQ
Length:397
Mass (Da):45,325
Last modified:July 27, 2011 - v2
Checksum:i866B123A1A058134
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681R → W in CAA83494 (PubMed:8725147).Curated
Sequence conflicti109 – 1091A → R in CAA83494 (PubMed:8725147).Curated
Sequence conflicti285 – 2873GTS → ELL in CAA83494 (PubMed:8725147).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31689 mRNA. Translation: CAA83494.1.
AK088659 mRNA. Translation: BAC40484.1.
AK149791 mRNA. Translation: BAE29088.1.
AK164007 mRNA. Translation: BAE37585.1.
CH466534 Genomic DNA. Translation: EDL41750.1.
CCDSiCCDS29760.1.
RefSeqiNP_001104570.1. NM_001111100.1.
NP_067435.3. NM_021460.3.
UniGeneiMm.157545.

Genome annotation databases

EnsembliENSMUST00000049572; ENSMUSP00000053270; ENSMUSG00000024781.
ENSMUST00000178114; ENSMUSP00000136967; ENSMUSG00000024781.
GeneIDi16889.
KEGGimmu:16889.
UCSCiuc008hgm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31689 mRNA. Translation: CAA83494.1.
AK088659 mRNA. Translation: BAC40484.1.
AK149791 mRNA. Translation: BAE29088.1.
AK164007 mRNA. Translation: BAE37585.1.
CH466534 Genomic DNA. Translation: EDL41750.1.
CCDSiCCDS29760.1.
RefSeqiNP_001104570.1. NM_001111100.1.
NP_067435.3. NM_021460.3.
UniGeneiMm.157545.

3D structure databases

ProteinModelPortaliQ9Z0M5.
SMRiQ9Z0M5. Positions 22-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z0M5. 2 interactions.
MINTiMINT-4114169.
STRINGi10090.ENSMUSP00000053270.

Protein family/group databases

ESTHERimouse-1llip. Acidic_Lipase.

PTM databases

iPTMnetiQ9Z0M5.
PhosphoSiteiQ9Z0M5.

Proteomic databases

EPDiQ9Z0M5.
MaxQBiQ9Z0M5.
PaxDbiQ9Z0M5.
PRIDEiQ9Z0M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049572; ENSMUSP00000053270; ENSMUSG00000024781.
ENSMUST00000178114; ENSMUSP00000136967; ENSMUSG00000024781.
GeneIDi16889.
KEGGimmu:16889.
UCSCiuc008hgm.2. mouse.

Organism-specific databases

CTDi3988.
MGIiMGI:96789. Lipa.

Phylogenomic databases

eggNOGiKOG2624. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00550000074328.
HOGENOMiHOG000240694.
HOVERGENiHBG006265.
InParanoidiQ9Z0M5.
KOiK01052.
OMAiVCTHVIM.
OrthoDBiEOG71RXJN.
TreeFamiTF315485.

Miscellaneous databases

ChiTaRSiLipa. mouse.
PROiQ9Z0M5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z0M5.
CleanExiMM_LIPA.
GenevisibleiQ9Z0M5. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR025483. Lipase_euk.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000862. Steryl_ester_lip. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tissue and cellular specific expression of murine lysosomal acid lipase mRNA and protein."
    Du H., Witte D.P., Grabowski G.A.
    J. Lipid Res. 37:937-949(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  2. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow and Thymus.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung and Spleen.

Entry informationi

Entry nameiLICH_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0M5
Secondary accession number(s): Q8C2G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.