ID   LID1_CAEEL              Reviewed;         360 AA.
AC   O02218;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Abhydrolase domain-containing protein lid-1 {ECO:0000305};
DE   AltName: Full=Lipid droplet protein 1 {ECO:0000312|WormBase:C25A1.12a};
GN   Name=lid-1 {ECO:0000312|WormBase:C25A1.12a};
GN   ORFNames=C25A1.12 {ECO:0000312|WormBase:C25A1.12a};
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, INTERACTION WITH ATGL-1, SUBCELLULAR LOCATION, DOMAIN, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=25202121; DOI=10.1128/mcb.00722-14;
RA   Lee J.H., Kong J., Jang J.Y., Han J.S., Ji Y., Lee J., Kim J.B.;
RT   "Lipid droplet protein LID-1 mediates ATGL-1-dependent lipolysis during
RT   fasting in Caenorhabditis elegans.";
RL   Mol. Cell. Biol. 34:4165-4176(2014).
CC   -!- FUNCTION: Acts coordinately with atgl-1 within the lipolytic cascade to
CC       distribute stored energy to tissues during nutritional deprivation.
CC       {ECO:0000269|PubMed:25202121}.
CC   -!- SUBUNIT: Interacts with atgl-1. {ECO:0000269|PubMed:25202121}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:25202121}.
CC       Note=Forms ring-like structures on the surface of lipid droplets.
CC       {ECO:0000269|PubMed:25202121}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown suppresses fasting-
CC       induced oxygen consumption. {ECO:0000269|PubMed:25202121}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX284601; CAB02763.2; -; Genomic_DNA.
DR   RefSeq; NP_492685.2; NM_060284.3.
DR   AlphaFoldDB; O02218; -.
DR   SMR; O02218; -.
DR   STRING; 6239.C25A1.12; -.
DR   ESTHER; caeel-C25A1.12; CGI-58_ABHD5_ABHD4.
DR   MEROPS; S33.975; -.
DR   EPD; O02218; -.
DR   PaxDb; O02218; -.
DR   PeptideAtlas; O02218; -.
DR   EnsemblMetazoa; C25A1.12a.1; C25A1.12a.1; WBGene00007711.
DR   GeneID; 172888; -.
DR   KEGG; cel:CELE_C25A1.12; -.
DR   UCSC; C25A1.12; c. elegans.
DR   CTD; 172888; -.
DR   WormBase; C25A1.12a; CE41871; WBGene00007711; lid-1.
DR   eggNOG; KOG4409; Eukaryota.
DR   HOGENOM; CLU_017361_0_0_1; -.
DR   InParanoid; O02218; -.
DR   OMA; ARDPIMD; -.
DR   PhylomeDB; O02218; -.
DR   Reactome; R-CEL-1482839; Acyl chain remodelling of PE.
DR   PRO; PR:O02218; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00007711; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; O02218; baseline and differential.
DR   GO; GO:0005811; C:lipid droplet; IDA:WormBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Lipid degradation; Lipid droplet; Lipid metabolism; Reference proteome.
FT   CHAIN           1..360
FT                   /note="Abhydrolase domain-containing protein lid-1"
FT                   /id="PRO_0000435426"
FT   DOMAIN          73..203
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   360 AA;  40389 MW;  43268DA2F7591516 CRC64;
     MAIATTKTAL TTIMNWMTFT DDSKEQLKIV EGRLFQSCEV SYEAKYVPVR FKRGEVYTVT
     VRPREAENLN GEAIVFIPGL GAGVAMFTAN FNSCAKNHAV HSFDPLGFGR SSRSRFSDDN
     AIAELEMVEV MEDWRKAMGI EKMYIIGHAF GGYLASAYAL ENPSRVAHLI LVDPWGFAEK
     VETTEKLIKP YAWMSFLGGV AGYFNPFSPM RWMGPYAPAI VKKLRPDLLL RFPGLHDYDI
     YKYVYYLNLP NPTGETAFMN MTLPVGWAKR PMIKRFNGID KNVGVSFIYG SKSWIDPGPA
     IDIQSTRENA YVDIKIVRGA GTHVYADDPA AFNEIVSDVV EGRLSNPSND FEIEECCHSD