LICH_RAT
ID LICH_RAT Reviewed; 397 AA.
AC Q64194;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Lysosomal acid lipase/cholesteryl ester hydrolase;
DE Short=Acid cholesteryl ester hydrolase;
DE Short=LAL;
DE EC=3.1.1.13 {ECO:0000250|UniProtKB:P38571};
DE AltName: Full=Cholesteryl esterase;
DE AltName: Full=Lipase A;
DE AltName: Full=Sterol esterase;
DE Flags: Precursor;
GN Name=Lipa; Synonyms=Lal, Lip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8576647;
RA Nakagawa H., Matsubara S., Kuriyama M., Yoshidome H., Fujiyama J.,
RA Yoshida H., Osame M.;
RT "Cloning of rat lysosomal acid lipase cDNA and identification of the
RT mutation in the rat model of Wolman's disease.";
RL J. Lipid Res. 36:2212-2218(1995).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=4062953;
RA Amanuma K., Okada J., Imanaka T., Ohkuma S., Takano T.;
RT "Subcellular localization of acid lipase in rat liver.";
RL Biochem. Int. 11:349-355(1985).
CC -!- FUNCTION: Catalyzes the deacylation of triacylglyceryl and cholesteryl
CC ester core lipids of endocytosed low density lipoproteins to generate
CC free fatty acids and cholesterol. {ECO:0000250|UniProtKB:P38571}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+);
CC Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13;
CC Evidence={ECO:0000250|UniProtKB:P38571};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate +
CC cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:P38571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000250|UniProtKB:P38571};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P38571}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:4062953}.
CC -!- PTM: Glycosylation is not essential for catalytic activity.
CC {ECO:0000250|UniProtKB:P38571}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; S81497; AAB36043.2; -; mRNA.
DR AlphaFoldDB; Q64194; -.
DR SMR; Q64194; -.
DR IntAct; Q64194; 1.
DR STRING; 10116.ENSRNOP00000025845; -.
DR ChEMBL; CHEMBL2352; -.
DR ESTHER; ratno-1llip; Acidic_Lipase.
DR GlyGen; Q64194; 5 sites.
DR jPOST; Q64194; -.
DR PaxDb; Q64194; -.
DR PRIDE; Q64194; -.
DR RGD; 3008; Lipa.
DR eggNOG; KOG2624; Eukaryota.
DR InParanoid; Q64194; -.
DR PhylomeDB; Q64194; -.
DR Reactome; R-RNO-8964038; LDL clearance.
DR PRO; PR:Q64194; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016298; F:lipase activity; IDA:RGD.
DR GO; GO:0004771; F:sterol esterase activity; IDA:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0016125; P:sterol metabolic process; IDA:RGD.
DR GO; GO:0048771; P:tissue remodeling; ISO:RGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR025483; Lipase_euk.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..72
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38571"
FT /id="PRO_0000450228"
FT CHAIN 73..397
FT /note="Lysosomal acid lipase/cholesteryl ester hydrolase"
FT /id="PRO_0000017801"
FT DOMAIN 84..378
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 45186 MW; 97A38595A0523947 CRC64;
MQLLGRVICF VVGILLSGGP TGTISAVDPE ANMNVTEIIM HWGYPEHSVQ TGDGYILGVH
RIPHGRKNQF DKGPKPVVYL QWRHGFLADS SNWVTNIDNN SLGFILADAG FDVWMGNSRG
NTWSRKHKTL SVSQDEYWAF SFDEMAKYDL PASINYILNK TGQEQLYNVG HSQGCTIGFI
AFSQMPELAK KVKMFFALAP VLSLNFASGP MVKLGRLPDL LLEDLFGQKQ FLPQSAMVKW
LSTHICTHVI MKELCANIFF LICGFNEKNL NMSRVDVYTT HCPAGTSVQN MVHWTQVVKY
HKLQAFDWGS SDKNYFHYNQ SYPPLYSIKD MQLPTALWSG GKDWLADTSD INILLTEIPT
LVYHKNIPEW DHLDFIWGLD APWRLYNEVV SLMKKYQ
