ID LIP3_DROME Reviewed; 394 AA.
AC O46108; Q4V3U9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Lipase 3;
DE Short=DmLip3;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=Lip3; ORFNames=CG8823;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=9566193; DOI=10.1006/jmbi.1997.1536;
RA Pistillo D., Manzi A., Tino A., Pilo Boyl P., Graziani F., Malva C.;
RT "The Drosophila melanogaster lipase homologs: a gene family with tissue and
RT developmental specific expression.";
RL J. Mol. Biol. 276:877-885(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- TISSUE SPECIFICITY: Fat body. {ECO:0000269|PubMed:9566193}.
CC -!- DEVELOPMENTAL STAGE: Only at larval stages.
CC {ECO:0000269|PubMed:9566193}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; Y14367; CAA74737.1; -; mRNA.
DR EMBL; AE014297; AAF54935.1; -; Genomic_DNA.
DR EMBL; BT023257; AAY55673.1; -; mRNA.
DR RefSeq; NP_477331.1; NM_057983.4.
DR AlphaFoldDB; O46108; -.
DR SMR; O46108; -.
DR BioGRID; 66726; 13.
DR IntAct; O46108; 12.
DR STRING; 7227.FBpp0082239; -.
DR ESTHER; drome-lip3; Acidic_Lipase.
DR GlyCosmos; O46108; 1 site, No reported glycans.
DR GlyGen; O46108; 1 site.
DR PaxDb; 7227-FBpp0082239; -.
DR DNASU; 41643; -.
DR EnsemblMetazoa; FBtr0082771; FBpp0082239; FBgn0023495.
DR GeneID; 41643; -.
DR KEGG; dme:Dmel_CG8823; -.
DR UCSC; CG8823-RA; d. melanogaster.
DR AGR; FB:FBgn0023495; -.
DR CTD; 41643; -.
DR FlyBase; FBgn0023495; Lip3.
DR VEuPathDB; VectorBase:FBgn0023495; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000165260; -.
DR HOGENOM; CLU_010974_0_3_1; -.
DR InParanoid; O46108; -.
DR OMA; LGIEMCQ; -.
DR OrthoDB; 3259424at2759; -.
DR PhylomeDB; O46108; -.
DR Reactome; R-DME-192456; Digestion of dietary lipid.
DR Reactome; R-DME-6809371; Formation of the cornified envelope.
DR SignaLink; O46108; -.
DR BioGRID-ORCS; 41643; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41643; -.
DR PRO; PR:O46108; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0023495; Expressed in midgut and 5 other cell types or tissues.
DR ExpressionAtlas; O46108; baseline and differential.
DR Genevisible; O46108; DM.
DR GO; GO:0004620; F:phospholipase activity; IMP:FlyBase.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:FlyBase.
DR GO; GO:0016042; P:lipid catabolic process; IDA:FlyBase.
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.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..394
FT /note="Lipase 3"
FT /id="PRO_0000017811"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 44901 MW; A718D1D743673802 CRC64;
MTRGALKVTI LLVGLGLVLA GSRPISDCGE RIEDDGYPME RHEVVTSDNY ILTMHRIPYS
PKTGESSNRP VAFLMHGMLS SSSDWVLMGP ERSLAYMLAD AGYDVWMGNA RGNTYSKAHK
YWPTYWQIFW NFSWNEIGMY DVPAMIDYVL AKTGQQQVQY VGHSQGTTVY LVMVSERPEY
NDKIKSAHLL GPAAYMGNMK SPLTRAFAPI LGQPNAIVEV CGSMEFMPSN KFKQDLGIEM
CQATSPYADM CANEIFLIGG YDTEQLDYEL LEHIKATSPA GASVNQNLHF CQEYNSGKFR
KFDYTALRNP YEYGSYFPPD YKLKNAKAPV LLYYGANDWM CDVSDVRKLR DELPNMALDY
LVPFEKWAHL DFIWGTEARK YVYDEVLKQM QSYE
//
