ID LIP1_DROME Reviewed; 439 AA.
AC O46107; Q9VKR6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Lipase 1;
DE Short=DmLip1;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=Lip1; ORFNames=CG7279;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP 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; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Could be a digestive enzyme. {ECO:0000269|PubMed:9566193}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In 14 hours embryos expression is seen in the
CC foregut/midgut boundary. {ECO:0000269|PubMed:9566193}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 14 hours embryos through to
CC adulthood. There is a weak maternal contribution to early embryos.
CC {ECO:0000269|PubMed:9566193}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y14366; CAA74736.1; ALT_INIT; mRNA.
DR EMBL; AE014134; AAF52994.1; -; Genomic_DNA.
DR EMBL; AY075506; AAL68315.1; -; mRNA.
DR RefSeq; NP_001285811.1; NM_001298882.1.
DR RefSeq; NP_523540.1; NM_078816.4.
DR AlphaFoldDB; O46107; -.
DR SMR; O46107; -.
DR STRING; 7227.FBpp0079713; -.
DR ESTHER; drome-lip1; Acidic_Lipase.
DR MEROPS; S33.A88; -.
DR GlyCosmos; O46107; 5 sites, No reported glycans.
DR GlyGen; O46107; 5 sites.
DR PaxDb; 7227-FBpp0079713; -.
DR DNASU; 43973; -.
DR EnsemblMetazoa; FBtr0080124; FBpp0079713; FBgn0023496.
DR EnsemblMetazoa; FBtr0340248; FBpp0309221; FBgn0023496.
DR GeneID; 43973; -.
DR KEGG; dme:Dmel_CG7279; -.
DR AGR; FB:FBgn0023496; -.
DR CTD; 43973; -.
DR FlyBase; FBgn0023496; Lip1.
DR VEuPathDB; VectorBase:FBgn0023496; -.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_0_3_1; -.
DR InParanoid; O46107; -.
DR OMA; LCVFINR; -.
DR OrthoDB; 3259424at2759; -.
DR PhylomeDB; O46107; -.
DR Reactome; R-DME-192456; Digestion of dietary lipid.
DR Reactome; R-DME-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 43973; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43973; -.
DR PRO; PR:O46107; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0023496; Expressed in primary trachea (Drosophila) and 16 other cell types or tissues.
DR ExpressionAtlas; O46107; baseline and differential.
DR Genevisible; O46107; DM.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:FlyBase.
DR GO; GO:0007586; P:digestion; IEP:UniProtKB.
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:SF147; 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 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..439
FT /note="Lipase 1"
FT /id="PRO_0000017810"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 393
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 10
FT /note="L -> I (in Ref. 1; CAA74736)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="Y -> F (in Ref. 1; CAA74736)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="Q -> E (in Ref. 1; CAA74736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50661 MW; 9E32E20BEAE93E3F CRC64;
MRCSLRMQLL LLLGLCVFIS RIQGQLIGGE EDEEDEEEEE EEEESVEDET PEDRLQRKNI
KQDSTLSVDK LIAKYGYESE VHHVTTEDGY ILTMHRIRKQ GAPPFLLQHG LVDSSAGFVV
MGPNVSLAYL LADHNYDVWL GNARGNRYSR NHTTLDPDES KFWDFSWHEI GMYDLPAMID
HVLKVTGFPK LHYAGHSQGC TSFFVMCSMR PAYNDKVVSM QALAPAVYAK ETEDHPYIRA
ISLYFNSLVG SSIREMFNGE FRFLCRMTEE TERLCIEAVF GIVGRNWNEF NRKMFPVILG
HYPAGVAAKQ VKHFIQIIKS GRFAPYSYSS NKNMQLYRDH LPPRYNLSLV TVPTFVYYST
NDLLCHPKDV ESMCDDLGNV TGKYLVPQKE FNHMDFLWAI DVRKMLYRRM LQVLGKVPEG
SPEEANRSRR EIRGKFIRS
//
