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Database: UniProt
Entry: A0A0M4F5F0_DROBS
LinkDB: A0A0M4F5F0_DROBS
Original site: A0A0M4F5F0_DROBS 
ID   A0A0M4F5F0_DROBS        Unreviewed;       422 AA.
AC   A0A0M4F5F0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Lipase {ECO:0000256|PIRNR:PIRNR000862};
GN   ORFNames=Dbus_chr3Rg1507 {ECO:0000313|EMBL:ALC46757.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC46757.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC46757.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC46757.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|PIRNR:PIRNR000862}.
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DR   EMBL; CP012526; ALC46757.1; -; Genomic_DNA.
DR   RefSeq; XP_017844835.1; XM_017989346.1.
DR   AlphaFoldDB; A0A0M4F5F0; -.
DR   SMR; A0A0M4F5F0; -.
DR   STRING; 30019.A0A0M4F5F0; -.
DR   GeneID; 108601448; -.
DR   OMA; GHRNTYS; -.
DR   OrthoDB; 3259424at2759; -.
DR   Proteomes; UP000494163; Chromosome 3r sequence.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR006693; AB_hydrolase_lipase.
DR   InterPro; IPR025483; Lipase_euk.
DR   PANTHER; PTHR11005:SF100; LIPASE-RELATED; 1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF04083; Abhydro_lipase; 1.
DR   PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid degradation {ECO:0000256|PIRNR:PIRNR000862};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000862};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..422
FT                   /note="Lipase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005794040"
FT   DOMAIN          54..113
FT                   /note="Partial AB-hydrolase lipase"
FT                   /evidence="ECO:0000259|Pfam:PF04083"
FT   ACT_SITE        191
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        363
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT   ACT_SITE        393
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ   SEQUENCE   422 AA;  48680 MW;  FC5D135BEFFD0CAE CRC64;
     MQYKLILALI FLFGYVWSVQ TAAVDVAPVD IDFYKLYNDP DAHLAFRERR TTRDRMAAHG
     YPAEHHHVVT EDGYILGIFR IPYSHKLKNQ DKKRPVVLIQ HGLFSCSDAW ILSGPNDALP
     YLLADAGFDV WIGNARGTTY SRNHTTLSTQ HPYFWRFDWH EIGVYDMSAM IDYALKTNGQ
     GQKSLHYVGH SQGTTVYFAL MSTVPEYNKK IKTANLFAPI AIMKNMRNKL VRKAAPYLGH
     HNTYSLLFSS QEFIPHNSFI SIMFFNLCEP DLNFRIVCNN VVGRLYDANR VNMTAMPEGM
     ATHPAGCSTN QILHYLQEQQ SGHFRQYDHG PAKNLLVYKS EQPPDYPVEK ITSELHMWYS
     DNDIMAAVED VLALAKRLPN HKLYHMEDPD WDHGDFALNK DVRKYLNEPV IEIMLKYEEA
     HN
//
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