ABH52_CAEEL
ID ABH52_CAEEL Reviewed; 444 AA.
AC H2KZ86; Q8I7H5;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Abhydrolase domain-containing protein abhd-5.2 {ECO:0000305};
GN Name=abhd-5.2 {ECO:0000312|WormBase:C37H5.3a};
GN Synonyms=cgi-58 {ECO:0000303|PubMed:26083785};
GN ORFNames=C37H5.3 {ECO:0000312|WormBase:C37H5.3a};
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, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26083785; DOI=10.1371/journal.pgen.1005284;
RA Xie M., Roy R.;
RT "The causative gene in Chanarian Dorfman syndrome regulates lipid droplet
RT homeostasis in C. elegans.";
RL PLoS Genet. 11:E1005284-E1005284(2015).
RN [3]
RP ERRATUM OF PUBMED:26083785.
RX PubMed=28002418; DOI=10.1371/journal.pgen.1006524;
RA Xie M., Roy R.;
RL PLoS Genet. 12:E1006524-E1006524(2016).
CC -!- FUNCTION: Acts coordinately with phospholipase atgl-1 within the
CC lipolytic cascade to distribute stored energy to tissues to maintain
CC energy levels during the dauer phase. Localizes atgl-1 to lipid
CC droplets, possibly to facilitate triglyceride hydrolysis. Regulates
CC lipid droplet size, lipid content, the exchange of lipids between lipid
CC droplets and fusion of lipid droplets during the dauer phase.
CC {ECO:0000269|PubMed:26083785}.
CC -!- SUBUNIT: Interacts with atgl-1; the interaction tethers atgl-1 to lipid
CC droplets. {ECO:0000269|PubMed:26083785}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:26083785}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C37H5.3a};
CC IsoId=H2KZ86-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C37H5.3b};
CC IsoId=H2KZ86-2; Sequence=VSP_059282;
CC -!- TISSUE SPECIFICITY: Expressed in the hypodermis and intestine.
CC {ECO:0000269|PubMed:26083785}.
CC -!- DISRUPTION PHENOTYPE: Increased survival of dauer larvae and reduced
CC lipase activity in a daf-2 constitutive dauer phase mutant background.
CC {ECO:0000269|PubMed:26083785}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284605; CCD66981.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD66982.1; -; Genomic_DNA.
DR RefSeq; NP_504297.1; NM_071896.4. [H2KZ86-1]
DR RefSeq; NP_872178.1; NM_182378.1. [H2KZ86-2]
DR AlphaFoldDB; H2KZ86; -.
DR SMR; H2KZ86; -.
DR STRING; 6239.C37H5.3a; -.
DR ESTHER; caeel-C37H5.3; CGI-58_ABHD5_ABHD4.
DR PaxDb; H2KZ86; -.
DR PeptideAtlas; H2KZ86; -.
DR EnsemblMetazoa; C37H5.3a.1; C37H5.3a.1; WBGene00016507. [H2KZ86-1]
DR EnsemblMetazoa; C37H5.3b.1; C37H5.3b.1; WBGene00016507. [H2KZ86-2]
DR GeneID; 178877; -.
DR KEGG; cel:CELE_C37H5.3; -.
DR UCSC; C37H5.3a; c. elegans.
DR CTD; 178877; -.
DR WormBase; C37H5.3a; CE08627; WBGene00016507; abhd-5.2. [H2KZ86-1]
DR WormBase; C37H5.3b; CE32824; WBGene00016507; abhd-5.2. [H2KZ86-2]
DR eggNOG; KOG4409; Eukaryota.
DR GeneTree; ENSGT00940000170137; -.
DR InParanoid; H2KZ86; -.
DR OMA; AKEQSSW; -.
DR OrthoDB; 1555935at2759; -.
DR PhylomeDB; H2KZ86; -.
DR PRO; PR:H2KZ86; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00016507; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
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 Alternative splicing; Hydrolase; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Reference proteome.
FT CHAIN 1..444
FT /note="Abhydrolase domain-containing protein abhd-5.2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442797"
FT DOMAIN 162..409
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..101
FT /note="MFQKTDFLSKIFSSSSHPLTGSQNIVVKDPQTLDFAMQSQNEIVCSLRERSH
FT MNTMSYAQTQMMAIDEIRAFQSEGHLHLKYISLIIAMMAETAVVTSRSW -> MSIFEY
FT TWYLSWIPSR (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059282"
SQ SEQUENCE 444 AA; 50488 MW; 8481B760D3B5247D CRC64;
MFQKTDFLSK IFSSSSHPLT GSQNIVVKDP QTLDFAMQSQ NEIVCSLRER SHMNTMSYAQ
TQMMAIDEIR AFQSEGHLHL KYISLIIAMM AETAVVTSRS WFPYFSCPSK SQRLAEAEGR
ILSALGIKYL ARLIQIPFKN TEISTITVNC ESEQPIVKAK YPIVLIHGFG AGVALWGSAI
KRLAQFQTVH AFDLPGFGRS SRPKFSSDPE TAETEMIDSI EQWRDKMNLE KMNLVGHSFG
GYLATSYALK YPKRVENLIL ADPWGFNEMD PEFAQKLTSR QKNIFWVIQQ FNPLAVLRLV
GGYGPSLVRR LRPDLALKYS EDVYDYIYLA NSRDPTGEEV FKCLSENLGW AKQPMSKRFH
ELDNTVPVTF IHGERSWIDW RTTRRLFGEL EHVESHIMDS AGHHVYADDA DKFVQLVIGS
LKDGKTGELV PEEVNLEEEI VTPI
