LICH_MACFA
ID LICH_MACFA Reviewed; 399 AA.
AC Q4R4S5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 63.
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; ORFNames=QflA-10548;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q64194}.
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; AB169819; BAE01900.1; -; mRNA.
DR AlphaFoldDB; Q4R4S5; -.
DR SMR; Q4R4S5; -.
DR STRING; 9541.XP_005565961.1; -.
DR ESTHER; macfa-q4r4s5; Acidic_Lipase.
DR eggNOG; KOG2624; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004771; F:sterol esterase activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:P38571"
FT PROPEP 28..76
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38571"
FT /id="PRO_0000450226"
FT CHAIN 77..399
FT /note="Lysosomal acid lipase/cholesteryl ester hydrolase"
FT /id="PRO_0000237614"
FT DOMAIN 80..380
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 374
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 399 AA; 45480 MW; A52F211193F23595 CRC64;
MKMRFLGLVV CLVLWTLHSE ASGGKLTAVN PETNMNVSEI ISYWGFPSEE YLVETEDGYI
LCLNRIPHGR KNHSDKGPKP VVFLQHGLLA DSSNWVTNLA NSSLGFILAD AGFDVWMGNS
RGNTWSRKHK TLSVSQDEFW AFSYDEMAKY DLPASINFIL NKTGQEQVYY VGHSQGTTIG
FIAFSQIPEL AKRIKMFFAL APVVSVDFCT SPMAKLGRLP DLLIKDLFGD KEFLPQSAFL
KWLGTHVCTH VILKELCGNL CFLLCGFNER NLNMSRVDVY TTHSPAGTSV QNMLHWSQAV
KFQKFQAFDW GSSAKNYFHY NQSYPPTYNV KDMLVPTAVW SGGHDWLADV YDINILLTQI
TNLVFHESIP EWEHLDFIWG LDAPWRLYNK IINLMKKYQ