ID   EST1_CAEEL              Reviewed;         562 AA.
AC   Q04457; O16702;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Gut esterase 1;
DE            EC=3.1.1.1;
DE   AltName: Full=Non-specific carboxylesterase;
DE   Flags: Precursor;
GN   Name=ges-1; ORFNames=R12A1.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 17-54.
RX   PubMed=8445654; DOI=10.1006/jmbi.1993.1094;
RA   Kennedy B.P., Aamodt E.J., Allen F.L., Chung M.A., Heschl M.F.P.,
RA   McGhee J.D.;
RT   "The gut esterase gene (ges-1) from the nematodes Caenorhabditis elegans
RT   and Caenorhabditis briggsae.";
RL   J. Mol. Biol. 229:890-908(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-73, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=12754521; DOI=10.1038/nbt829;
RA   Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA   Kasai K., Takahashi N., Isobe T.;
RT   "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT   identify N-linked glycoproteins.";
RL   Nat. Biotechnol. 21:667-672(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC         Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- TISSUE SPECIFICITY: Expressed only in the intestine.
CC   -!- DEVELOPMENTAL STAGE: Appears in mid-proliferation phase when the
CC       developing gut has four to eight cells.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M96145; AAA28057.1; -; Genomic_DNA.
DR   EMBL; FO081062; CCD68892.1; -; Genomic_DNA.
DR   PIR; S27800; S27800.
DR   PIR; T32061; T32061.
DR   RefSeq; NP_503411.1; NM_071010.5.
DR   AlphaFoldDB; Q04457; -.
DR   SMR; Q04457; -.
DR   BioGRID; 43700; 1.
DR   STRING; 6239.R12A1.4; -.
DR   ESTHER; caeel-ges1e; Carb_B_Nematoda.
DR   iPTMnet; Q04457; -.
DR   EPD; Q04457; -.
DR   PaxDb; Q04457; -.
DR   PeptideAtlas; Q04457; -.
DR   EnsemblMetazoa; R12A1.4.1; R12A1.4.1; WBGene00001578.
DR   GeneID; 178633; -.
DR   KEGG; cel:CELE_R12A1.4; -.
DR   UCSC; R12A1.4.1; c. elegans.
DR   CTD; 178633; -.
DR   WormBase; R12A1.4; CE28763; WBGene00001578; ges-1.
DR   eggNOG; KOG1516; Eukaryota.
DR   GeneTree; ENSGT00940000164234; -.
DR   HOGENOM; CLU_006586_13_3_1; -.
DR   InParanoid; Q04457; -.
DR   OMA; HANEYHY; -.
DR   OrthoDB; 754103at2759; -.
DR   PhylomeDB; Q04457; -.
DR   Reactome; R-CEL-112311; Neurotransmitter clearance.
DR   Reactome; R-CEL-1483191; Synthesis of PC.
DR   Reactome; R-CEL-211945; Phase I - Functionalization of compounds.
DR   Reactome; R-CEL-8964038; LDL clearance.
DR   Reactome; R-CEL-9749641; Aspirin ADME.
DR   PRO; PR:Q04457; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00001578; Expressed in larva and 3 other tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:WormBase.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:WormBase.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044248; P:cellular catabolic process; IDA:WormBase.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Hydrolase; Reference proteome; Serine esterase; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:8445654"
FT   CHAIN           17..562
FT                   /note="Gut esterase 1"
FT                   /id="PRO_0000008549"
FT   MOTIF           559..562
FT                   /note="Prevents secretion from ER"
FT   ACT_SITE        198
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        319
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        452
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine; atypical"
FT                   /evidence="ECO:0000269|PubMed:12754521"
FT   DISULFID        75..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        250..258
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   562 AA;  63722 MW;  1366AA79ED84D96A CRC64;
     MRIFLVSVIL INACWAGPIV ETNYGKVEGI EYEGAEVFLA IPFAKPPVDD LRFEKPVAPD
     PWEDVYPATQ YRNDCTPHYR LVAQFSSYSG EDCLTLNIIK PKKAEKLPVL FWIHGGGYEI
     GSASQHGYEF FAKRYASQGV IVATVQYRLG FMGFFSEGTS DVQGNWGLFD QAAALEFVKS
     NIENFGGDPN QITIWGYSAG AASVSQLTMS PYTRDSYSKA IIMSASSFVG WATGPNVVET
     SKQLAEILGC PWPGAKECMK KKSLHEIFDA IEVQGWTTGT IDILRWSPVI DGDFMTKNPE
     ELIKESPVKP TLIGMSNKEG SYFAALNMGR VIADFGLSPE DMPKVDEEFI SEIIGRKLLY
     NNRYGENREK VWNDILDFYV KQGKPAEVKD LNGFYVDRYS ELLSDITFNV PILREITSRV
     ERKTPVWTYR MDHYDKNIWK KHIPEQARGS PHANEYHYLF DMPVMAKIDM KKEPDSWIQN
     DLIDMVISFA KTGVPQIEDV EWRPVSDPDD VNFLNIRSDG VSIEHGLFQE PLAFWNELRQ
     REGFDLIDPT NSAMHSSNKD EL