EST3_PONAB
ID EST3_PONAB Reviewed; 569 AA.
AC Q5RCL7; Q5RFG4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Carboxylesterase 3;
DE EC=3.1.1.1;
DE AltName: Full=Liver carboxylesterase 31 homolog;
DE Flags: Precursor;
GN Name=CES3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; CR857194; CAH89493.1; -; mRNA.
DR EMBL; CR858253; CAH90490.1; -; mRNA.
DR RefSeq; NP_001125256.1; NM_001131784.1.
DR RefSeq; NP_001128738.1; NM_001135266.1.
DR AlphaFoldDB; Q5RCL7; -.
DR SMR; Q5RCL7; -.
DR STRING; 9601.ENSPPYP00000008401; -.
DR ESTHER; ponab-est3; Carb_B_Chordata.
DR GeneID; 100172153; -.
DR GeneID; 100189629; -.
DR KEGG; pon:100172153; -.
DR CTD; 23491; -.
DR eggNOG; KOG1516; Eukaryota.
DR InParanoid; Q5RCL7; -.
DR Proteomes; UP000001595; 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 Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..569
FT /note="Carboxylesterase 3"
FT /id="PRO_0000305192"
FT MOTIF 566..569
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 458
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..122
FT /evidence="ECO:0000250"
FT DISULFID 279..290
FT /evidence="ECO:0000250"
FT CONFLICT 333
FT /note="H -> R (in Ref. 1; CAH89493)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="C -> F (in Ref. 1; CAH89493)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="V -> F (in Ref. 1; CAH89493)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="E -> G (in Ref. 1; CAH89493)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="W -> R (in Ref. 1; CAH90490)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="H -> Q (in Ref. 1; CAH89493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 62439 MW; 2720B9C19D028373 CRC64;
MRLHRLRARL NAVAFGLLLL LVHGQGPEIV QPEVDTTLGR VRGRQVGVKG TDRLVNVFLG
IPFAQPPLGP DRFSAPHPAQ PWEGVRDASA APPMCLQDVE SMNNSRFVLN GKQQIFSVSE
DCLVLNIYSP AEATAGAGRP VMVWVHGGAL ITGAATSYDG SALAAYGDVV VVTVQYRLGV
LGFFSTGDEH APGNQGFLDV VAALRWVQGN ITPFGGDLNC VTVFGGSAGG SIVSGLVLSP
MAAGLFHRAI TQSGVITTPG IIESHPWPLA QKITNTLACS SSSPAEMVQC LRQKEGEELV
LSKKLKSTIY PLTVDGTVFP KSPKELLKEK PFHSVPFLMG VNNHEFSWLI PRGWGLLDTM
EQMSREDMLA ISTPVLTSLD VPPEMMPTVI DEYLGSNSDA QAKCLAFQEF MGDVFINVPT
VSFSRYLRDS GSPVFFYEFQ HRPSSFAKIK PAWVKADHAA EGAFVFGGPF LMDESSRLAF
PEATEEEKQL SLTMMAQWTH FARTGDPNSK GLPPWPRFNQ AEQYLEINPV PRAGQKFRET
RMQFWSETLP SKIQQWHQKQ KNRKAQEDL