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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
 
 
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