EST1_MESAU
ID EST1_MESAU Reviewed; 561 AA.
AC Q64419;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Liver carboxylesterase;
DE EC=3.1.1.1;
DE Flags: Precursor;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Syrian golden; TISSUE=Liver;
RX PubMed=8043605; DOI=10.1016/0167-4838(94)90063-9;
RA Sone T., Isobe M., Takabatake E., Wang C.Y.;
RT "Cloning and sequence analysis of a hamster liver cDNA encoding a novel
RT putative carboxylesterase.";
RL Biochim. Biophys. Acta 1207:138-142(1994).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs.
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. Note=Microsomal
CC membrane, lumen of endoplasmic reticulum.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; D28566; BAA05913.1; -; mRNA.
DR PIR; S47655; S47655.
DR RefSeq; NP_001297488.1; NM_001310559.1.
DR AlphaFoldDB; Q64419; -.
DR SMR; Q64419; -.
DR ESTHER; mesau-cxest; Carb_B_Chordata.
DR MEROPS; S09.956; -.
DR GeneID; 106022736; -.
DR OrthoDB; 754103at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..561
FT /note="Liver carboxylesterase"
FT /id="PRO_0000008573"
FT MOTIF 558..561
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 227
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 459
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..122
FT /evidence="ECO:0000250"
FT DISULFID 280..291
FT /evidence="ECO:0000250"
SQ SEQUENCE 561 AA; 62331 MW; 48EA11E422475321 CRC64;
MPLNRFPCWR YAVACGLLLL LVHVHGQDSV SPIRNTHTGQ VRGKLVYVKE GVTGVYAFLG
IPFAKPPVGP LRFAPPEPPE PWSGVRDGTS EPAMCLQTDF MRPQISKERK IILPTISMSE
DCLYLNIYTP AHAHEGSNLP VMVWIHGGAL VMGMASMNDG SLLAATEDIV IVSIQYRLGI
LGFFSTGDEH ARGNWGYLDQ VAALHWVQQN IASFGGNPGQ VTIFGVSAGG TSVSSLVVSP
MSKGLFHGAI MQSGVALLPD LISDTPEAVY TPVVANQSGC EAKDSEALVH CLREKTEAEI
LAINQVFIMT PGVVDGIFLP RHPQELLASV DFHPVPSIIG VDSDECGWGV PLFMGLDHVI
KNITRETLPA FLKSRAEHMM LPPECSDLLM QEYMGDVEDP QTLQAQFREL MKDFMFVIPA
LKVAYFQRSH APVYFYEFQH QSSFIKNKDA RPSHVRADHG DHVAFVFGSD FWGLKIDLTE
EEKLLNKRMM KYWANFARHG NPNSEGLPYW PELVHDDQYL KLDIQPAVGR ALKSRKLHFW
TKILPQKIQE LKGAQGKHSE L