ID   LDAH_PONAB              Reviewed;         325 AA.
AC   Q5R7E8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Lipid droplet-associated hydrolase {ECO:0000250|UniProtKB:Q8BVA5};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:Q8BVA5};
DE   AltName: Full=Lipid droplet-associated serine hydrolase {ECO:0000250|UniProtKB:Q8BVA5};
GN   Name=LDAH {ECO:0000250|UniProtKB:Q8BVA5};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable serine lipid hydrolase associated with lipid
CC       droplets. Appears to lack cholesterol esterase activity. Appears to
CC       lack triglyceride lipase activity. Highly expressed in macrophage-rich
CC       areas in atherosclerotic lesions, suggesting that it could promote
CC       cholesterol ester turnover in macrophages.
CC       {ECO:0000250|UniProtKB:Q8BVA5}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q8BVA5}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8BVA5}. Note=Localizes to
CC       the endoplasmic reticulum in absence of lipid droplets and translocates
CC       to lipid droplets upon lipid storage induction.
CC       {ECO:0000250|UniProtKB:Q8BVA5}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. LDAH family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The catalytic activity is unsure despite catalytic sites being
CC       conserved. {ECO:0000250|UniProtKB:Q8BVA5}.
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DR   EMBL; CR860170; CAH92312.1; -; mRNA.
DR   RefSeq; NP_001126355.1; NM_001132883.1.
DR   AlphaFoldDB; Q5R7E8; -.
DR   STRING; 9601.ENSPPYP00000014085; -.
DR   ESTHER; ponab-cb043; LIDHydrolase.
DR   GeneID; 100173336; -.
DR   KEGG; pon:100173336; -.
DR   CTD; 60526; -.
DR   eggNOG; KOG3975; Eukaryota.
DR   OrthoDB; 1163030at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0004771; F:sterol esterase activity; ISS:UniProtKB.
DR   GO; GO:0019915; P:lipid storage; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR019363; LDAH.
DR   PANTHER; PTHR13390; PTHR13390; 1.
DR   Pfam; PF10230; LIDHydrolase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Hydrolase; Lipid droplet; Reference proteome.
FT   CHAIN           1..325
FT                   /note="Lipid droplet-associated hydrolase"
FT                   /id="PRO_0000300126"
FT   ACT_SITE        139
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        271
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6V9"
FT   ACT_SITE        300
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6V9"
SQ   SEQUENCE   325 AA;  37209 MW;  0FDD3277282FE853 CRC64;
     MDSELKEEIP VHEEFILCGG AETQVLKCGP WTDLFNDQSV KRPKLLIFII PGNPGFSAFY
     VPFAKALYSL TNRCFPVWTI SHAGHALAPK DKKILTTSED SNAQEIKDIY GLNGQIEHKL
     AFLRTHVPKD MKLVLIGHSV GSYFTLQMLK RVPELPVIRA FLLFPTIERM SESPNGRIAT
     PLLCWSRYVL YVTGYLLLKP CPEKIKSLLI RRGLQVMNLE NEFSPLNILE PFCLANAAHL
     GGQEMMEVVK RDDETIREHL CKLTFYYGTI DPWCPKEYYE DIKKDFPEGD IRLCEKNIPH
     AFIIHFNQEM ADMIADSLKD DLSKM