ID   EST1_CAEBR              Reviewed;         562 AA.
AC   Q04456; A8X267;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=CBG06418;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(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; M96144; AAA28056.1; -; Genomic_DNA.
DR   EMBL; HE601320; CAP26727.1; -; Genomic_DNA.
DR   PIR; S27782; S27782.
DR   RefSeq; XP_002647363.1; XM_002647317.1.
DR   AlphaFoldDB; Q04456; -.
DR   SMR; Q04456; -.
DR   STRING; 6238.Q04456; -.
DR   ESTHER; caebr-ges1e; Carb_B_Nematoda.
DR   EnsemblMetazoa; CBG06418.1; CBG06418.1; WBGene00028697.
DR   GeneID; 8589362; -.
DR   KEGG; cbr:CBG_06418; -.
DR   CTD; 8589362; -.
DR   WormBase; CBG06418; CBP15596; WBGene00028697; Cbr-ges-1.
DR   eggNOG; KOG1516; Eukaryota.
DR   HOGENOM; CLU_006586_13_3_1; -.
DR   InParanoid; Q04456; -.
DR   OMA; HANEYHY; -.
DR   OrthoDB; 4386at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:EnsemblMetazoa.
DR   GO; GO:0106435; F:carboxylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:EnsemblMetazoa.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   PANTHER; PTHR11559; CARBOXYLESTERASE; 1.
DR   PANTHER; PTHR11559:SF407; GUT ESTERASE 1; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Hydrolase; Reference proteome;
KW   Serine esterase; Signal.
FT   SIGNAL          1..16
FT   CHAIN           17..562
FT                   /note="Gut esterase 1"
FT                   /id="PRO_0000008550"
FT   MOTIF           559..562
FT                   /note="Prevents secretion from ER"
FT   ACT_SITE        199
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        320
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        451
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        251..259
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   562 AA;  63819 MW;  7FA312F3B2587E53 CRC64;
     MRVLLASLLI FGACWAGPVV NTNYGKVEGF EYGAAEVFLA IPFAKPPVDN LRFEKPEAPE
     PWEDVYQATQ FRNDCTPHYR LVAQFSSYSG EDCLTLNVIK PKTIEKKLPV LFWVHGGGYE
     IGSGSQHGYE FFADRYTSQG VIVVTIQYRL GFMGFFSEGT SDAPGNYGLF DQAAALRFVK
     ENIGNFGGDP DDITIWGYSA GAASVSQLTM SPYTHDLYSK AIIMSASSFV GWATGPNVID
     TSKQLAEILG CPWPGAKECM KKKTLHEIFD AVETQGWTTG TIDILRWSPV IDGDYLPKNP
     ENLINDAPIK PTLIGMSNKE GSYFATMNMG RVIADFGLSP EEIPKVDEDF ISEIIDRKLL
     YNNRYGENRQ KVWDQILDYY TKQGKPERDL NGFYVDRYAE LLSDITFNVP ILREITARVE
     RKTPVWTYRF DHYNEQIWKK YIPEQAKGSP HANEYHYLFN MPVMAQIDFK KEPESWLQRD
     LIDMVVSFAK TGVPHIQDVE WRPVSDPDDV NFLNFQSSGV SVKHGLFQEP LDFWNNLRER
     EGFDLVDPAY SKTTSNSEKD EL
//