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LIPL3_CAEEL
ID   LIPL3_CAEEL             Reviewed;         404 AA.
AC   O16956;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Lipase lipl-3 {ECO:0000255|PIRNR:PIRNR000862};
DE            EC=3.1.1.- {ECO:0000305|PubMed:23604316};
DE   AltName: Full=Lipase-like 3 {ECO:0000312|WormBase:R11G11.14};
DE   Flags: Precursor;
GN   Name=lipl-3 {ECO:0000312|WormBase:R11G11.14};
GN   ORFNames=R11G11.14 {ECO:0000312|WormBase:R11G11.14};
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-1, 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; CCD64488.1; -; Genomic_DNA.
DR   PIR; H88930; H88930.
DR   RefSeq; NP_503233.1; NM_070832.3.
DR   AlphaFoldDB; O16956; -.
DR   SMR; O16956; -.
DR   STRING; 6239.R11G11.14; -.
DR   ESTHER; caeel-R11G11.14; Acidic_Lipase.
DR   MEROPS; S33.B10; -.
DR   PaxDb; O16956; -.
DR   PeptideAtlas; O16956; -.
DR   EnsemblMetazoa; R11G11.14.1; R11G11.14.1; WBGene00020016.
DR   GeneID; 178572; -.
DR   KEGG; cel:CELE_R11G11.14; -.
DR   UCSC; R11G11.14; c. elegans.
DR   CTD; 178572; -.
DR   WormBase; R11G11.14; CE28762; WBGene00020016; lipl-3.
DR   eggNOG; KOG2624; Eukaryota.
DR   GeneTree; ENSGT00940000169551; -.
DR   HOGENOM; CLU_010974_0_0_1; -.
DR   InParanoid; O16956; -.
DR   OMA; LCASTDW; -.
DR   OrthoDB; 651396at2759; -.
DR   PhylomeDB; O16956; -.
DR   Reactome; R-CEL-192456; Digestion of dietary lipid.
DR   Reactome; R-CEL-6809371; Formation of the cornified envelope.
DR   PRO; PR:O16956; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00020016; 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..404
FT                   /note="Lipase lipl-3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004157979"
FT   ACT_SITE        168
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        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   404 AA;  45779 MW;  A87561AE0B2FED46 CRC64;
     MCSSLCALLL VILAVHNVHA KSDPELHMTT PQIIERWGYP AMIYSVTTDD GYILELHRIP
     HGKTNVTWPN GKQPVVFMQH GLLCASTDWT MNLPEQSAAF IFADAGFDVW LGNMRGNTYS
     MKHKNLKASH SDFWEWSWDE MATYDLPAMI DKVLEVTGQE SLYYMGHSQG TLTMFSHLSK
     DDGIFAKKIK KFFALAPVGS VKDIKGFLSF FAHYFSLEFD GWFDVFGAGE FLPNNWAMKL
     AAKDICGGLK IESDLCDNVC FLIAGPESDQ WNSTRVPVYA SHDPAGTATQ NIVHWIQMVR
     HGGVPAYDWG SKENKKKYGQ ANPPEYDFTA IKGTQIYLYW SDADWLADKT DITNYLLTRL
     NPAIIAQNNY FTDYNHFDFV FGLRAPNDIY LPIVDICTKD YNGK
 
 
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