LIPL5_CAEEL
ID LIPL5_CAEEL Reviewed; 403 AA.
AC O61866; A0A0K3AW68; A0A0K3AYF1;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Lipase lipl-5 {ECO:0000255|PIRNR:PIRNR000862};
DE EC=3.1.1.- {ECO:0000305|PubMed:31340142, ECO:0000305|PubMed:31676440};
DE AltName: Full=Lipase-like 5 {ECO:0000312|WormBase:ZK6.7a};
DE Flags: Precursor;
GN Name=lipl-5 {ECO:0000312|WormBase:ZK6.7a};
GN ORFNames=ZK6.7 {ECO:0000312|WormBase:ZK6.7a};
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.
RX PubMed=31676440; DOI=10.1016/j.bbalip.2019.158539;
RA Macedo F., Martins G.L., Luevano-Martinez L.A., Viana G.M., Riske K.A.,
RA Inague A., Yoshinaga M.Y., Aguilaniu H., Miyamoto S., Glezer I.,
RA da Cunha F.M.;
RT "Lipase-like 5 enzyme controls mitochondrial activity in response to
RT starvation in Caenorhabditis elegans.";
RL Biochim. Biophys. Acta 1865:158539-158539(2019).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31340142; DOI=10.1016/j.celrep.2019.06.064;
RA Buis A., Bellemin S., Goudeau J., Monnier L., Loiseau N., Guillou H.,
RA Aguilaniu H.;
RT "Coelomocytes Regulate Starvation-Induced Fat Catabolism and Lifespan
RT Extension through the Lipase LIPL-5 in Caenorhabditis elegans.";
RL Cell Rep. 28:1041-1049.E4(2019).
CC -!- FUNCTION: Lipase involved in lipid homeostasis (PubMed:31676440).
CC Regulates mitochondrial lipid composition, in particular cardiolipins
CC and coenzyme Q-9 levels, in response to nutrient availability
CC (PubMed:31676440). Does not affect global triglyceride levels in
CC response to nutrient availability (PubMed:31676440). However, in
CC coelomocytes, specifically promotes triglyceride catabolism and
CC lifespan extension in response to nutrient deprivation
CC (PubMed:31340142). {ECO:0000269|PubMed:31340142,
CC ECO:0000269|PubMed:31676440}.
CC -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:31340142}.
CC Secreted {ECO:0000269|PubMed:31340142}. Note=Localizes to lysosomes in
CC coelomocytes. {ECO:0000269|PubMed:31340142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:ZK6.7a};
CC IsoId=O61866-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:ZK6.7c};
CC IsoId=O61866-2; Sequence=VSP_060546;
CC Name=d {ECO:0000312|WormBase:ZK6.7d};
CC IsoId=O61866-3; Sequence=VSP_060545;
CC -!- INDUCTION: Up-regulated by fasting. {ECO:0000269|PubMed:31340142}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown impairs triglyceride
CC catabolism and further increases lifespan extension in response to
CC bacteria (nutrient) deprivation. {ECO:0000269|PubMed:31340142}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000255|PIRNR:PIRNR000862}.
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DR EMBL; BX284605; CCD74353.1; -; Genomic_DNA.
DR EMBL; BX284605; CTQ86997.1; -; Genomic_DNA.
DR EMBL; BX284605; CTQ86998.1; -; Genomic_DNA.
DR PIR; T33198; T33198.
DR RefSeq; NP_001300298.1; NM_001313369.1.
DR RefSeq; NP_001300299.1; NM_001313370.1.
DR RefSeq; NP_503184.1; NM_070783.3. [O61866-1]
DR AlphaFoldDB; O61866; -.
DR SMR; O61866; -.
DR STRING; 6239.ZK6.7a; -.
DR ESTHER; caeel-1llip; Acidic_Lipase.
DR EPD; O61866; -.
DR PaxDb; O61866; -.
DR PeptideAtlas; O61866; -.
DR EnsemblMetazoa; ZK6.7a.1; ZK6.7a.1; WBGene00022642. [O61866-1]
DR EnsemblMetazoa; ZK6.7c.1; ZK6.7c.1; WBGene00022642. [O61866-2]
DR EnsemblMetazoa; ZK6.7d.1; ZK6.7d.1; WBGene00022642. [O61866-3]
DR GeneID; 178563; -.
DR KEGG; cel:CELE_ZK6.7; -.
DR UCSC; ZK6.7b; c. elegans. [O61866-1]
DR CTD; 178563; -.
DR WormBase; ZK6.7a; CE18444; WBGene00022642; lipl-5. [O61866-1]
DR WormBase; ZK6.7c; CE50798; WBGene00022642; lipl-5.
DR WormBase; ZK6.7d; CE50743; WBGene00022642; lipl-5.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000169551; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; O61866; -.
DR OMA; DGEHVDC; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; O61866; -.
DR Reactome; R-CEL-192456; Digestion of dietary lipid.
DR Reactome; R-CEL-6809371; Formation of the cornified envelope.
DR PRO; PR:O61866; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00022642; Expressed in adult organism and 2 other tissues.
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:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEP:WormBase.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IMP:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP: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 Alternative splicing; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lysosome; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..403
FT /note="Lipase lipl-5"
FT /evidence="ECO:0000255"
FT /id="PRO_5004159069"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR000862-1"
FT ACT_SITE 343
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PIRSR:PIRSR000862-1"
FT ACT_SITE 375
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PIRSR:PIRSR000862-1"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060545"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060546"
SQ SEQUENCE 403 AA; 45704 MW; 7F5622F820C5FE52 CRC64;
MWRFAVFLAA FFVQDVVGSH GDPELHMTTP QIIERWGYPA MIYTVATDDG YILEMHRIPF
GKTNVTWPNG KRPVVFMQHG LLCASSDWVV NLPDQSAGFL FADAGFDVWL GNMRGNTYSM
KHKDLKPSHS AFWDWSWDEM ATYDLNAMIN HVLEVTGQDS VYYMGHSQGT LTMFSHLSKD
DGSFAKKIKK FFALAPIGSV KHIKGFLSFF ANYFSLEFDG WFDIFGAGEF LPNNWAMKLA
AKDICGGLKV EADLCDNVLF LIAGPESDQW NQTRVPVYAT HDPAGTSTQN IVHWMQMVHH
GGVPAYDWGT KTNKKKYGQA NPPEYDFTAI KGTKIYLYWS DADWLADTPD VPDYLLTRLN
PAIVAQNNHL PDYNHLDFTW GLRAPDDIYR PAIKLCTDDY LGK
