LIPL1_CAEEL
ID LIPL1_CAEEL Reviewed; 405 AA.
AC Q93789;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Lipase lipl-1 {ECO:0000255|PIRNR:PIRNR000862};
DE EC=3.1.1.- {ECO:0000305|PubMed:23604316};
DE AltName: Full=Lipase-like 1 {ECO:0000312|WormBase:F54F3.3};
DE Flags: Precursor;
GN Name=lipl-1 {ECO:0000312|WormBase:F54F3.3};
GN ORFNames=F54F3.3 {ECO:0000312|WormBase:F54F3.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=23604316; DOI=10.1038/ncb2741;
RA O'Rourke E.J., Ruvkun G.;
RT "MXL-3 and HLH-30 transcriptionally link lipolysis and autophagy to
RT nutrient availability.";
RL Nat. Cell Biol. 15:668-676(2013).
RN [3] {ECO:0000305}
RP INDUCTION.
RX PubMed=29113111; DOI=10.3390/genes8110307;
RA Mejia-Martinez F., Franco-Juarez B., Moreno-Arriola E.,
RA Hernandez-Vazquez A., Martinez-Avila M., Gomez-Manzo S., Marcial-Quino J.,
RA Carvajal K., Velazquez-Arellano A., Ortega-Cuellar D.;
RT "The MXL-3/SBP-1 Axis Is Responsible for Glucose-Dependent Fat Accumulation
RT in C. elegans.";
RL Genes (Basel) 8:0-0(2017).
CC -!- FUNCTION: Lipase that, together with lipl-3, plays a role in the
CC response to nutrient deprivation by controlling lipid metabolism
CC (PubMed:23604316). Specifically, involved in the breakdown of lipids
CC during lipophagy, a process during which lipids contained in lipid
CC droplets that have been delivered to lysosomes by autophagy are
CC degraded (PubMed:23604316). {ECO:0000269|PubMed:23604316}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is acidic. {ECO:0000305|PubMed:23604316};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23604316}. Lysosome
CC lumen {ECO:0000269|PubMed:23604316}. Note=Secreted into the intestinal
CC lumen. {ECO:0000269|PubMed:23604316}.
CC -!- INDUCTION: Up-regulated in the intestine by fasting (PubMed:23604316).
CC Down-regulated in response to a high-glucose diet (PubMed:29113111).
CC {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:29113111}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000255|PIRNR:PIRNR000862}.
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DR EMBL; BX284605; CAB01973.1; -; Genomic_DNA.
DR PIR; T22675; T22675.
DR RefSeq; NP_506229.1; NM_073828.3.
DR AlphaFoldDB; Q93789; -.
DR SMR; Q93789; -.
DR STRING; 6239.F54F3.3; -.
DR ESTHER; caeel-F54F3.3; Acidic_Lipase.
DR MEROPS; S33.B09; -.
DR PaxDb; Q93789; -.
DR PeptideAtlas; Q93789; -.
DR EnsemblMetazoa; F54F3.3.1; F54F3.3.1; WBGene00010062.
DR GeneID; 179771; -.
DR KEGG; cel:CELE_F54F3.3; -.
DR UCSC; F54F3.3; c. elegans.
DR CTD; 179771; -.
DR WormBase; F54F3.3; CE18732; WBGene00010062; lipl-1.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000169551; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; Q93789; -.
DR OMA; HKYWPTY; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q93789; -.
DR Reactome; R-CEL-192456; Digestion of dietary lipid.
DR Reactome; R-CEL-6809371; Formation of the cornified envelope.
DR PRO; PR:Q93789; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010062; Expressed in larva and 1 other tissue.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:WormBase.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IGI:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR InterPro; IPR025483; Lipase_euk.
DR Pfam; PF04083; Abhydro_lipase; 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; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..405
FT /note="Lipase lipl-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004320188"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR000862-1"
FT ACT_SITE 344
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PIRSR:PIRSR000862-1"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PIRSR:PIRSR000862-1"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 405 AA; 45790 MW; FFCAA9E49A782A60 CRC64;
MRSWSTVMLA VLATAATVFG HDADPEMKMT TPQIIMRWGY PAMIYDVTTE DGYILELHRI
PYGKTNVTWP NGKKPVVFMQ HGLECSSSNW VVNLPTESAA FLFADAGYDV WLGNFRGNTY
SMKHKNLKPS HSAFWDWSWD EMQQYDLPAM IEKALEVTGQ DSLYYIGHSQ GTLTMFSRLS
EDKVGWGNKI KKFFALAPVG SVKHIKGALK FFADYFSLEF DGWFDVFGSG EFLPNNWIMK
LVSESVCAGL KVEAGVCDDV MFLIAGPESN QLNATRVPIY VAHTPAGTST QNIVHWIQMV
RHGGTPKYDY GEKGNKKHYG QANVPAYDFT TVNRPVYLYW GDSDWLADPT DVTDFLLTHL
NPSTVVQNNK LIDYNHLDFI WGLRAPKDIY EPIIDIVRND VLNGS
