EST3B_MOUSE
ID EST3B_MOUSE Reviewed; 571 AA.
AC Q8VCU1; G5E8G7; G5E8K9; Q91XD5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Carboxylesterase 3B;
DE EC=3.1.1.1;
DE AltName: Full=Liver carboxylesterase 31-like;
DE Flags: Precursor;
GN Name=Ces3b; Synonyms=Gm4738;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VCU1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCU1-2; Sequence=VSP_028269;
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10812.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH19147.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC164311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11245.1; -; Genomic_DNA.
DR EMBL; CH466525; EDL11246.1; -; Genomic_DNA.
DR EMBL; BC010812; AAH10812.1; ALT_INIT; mRNA.
DR EMBL; BC019147; AAH19147.1; ALT_INIT; mRNA.
DR CCDS; CCDS22590.2; -. [Q8VCU1-1]
DR CCDS; CCDS52653.1; -. [Q8VCU1-2]
DR RefSeq; NP_001152887.1; NM_001159415.1. [Q8VCU1-2]
DR RefSeq; NP_653094.2; NM_144511.2. [Q8VCU1-1]
DR AlphaFoldDB; Q8VCU1; -.
DR SMR; Q8VCU1; -.
DR STRING; 10090.ENSMUSP00000090909; -.
DR ESTHER; mouse-Ces3b; Carb_B_Chordata.
DR MEROPS; S09.971; -.
DR GlyGen; Q8VCU1; 1 site.
DR iPTMnet; Q8VCU1; -.
DR PhosphoSitePlus; Q8VCU1; -.
DR SwissPalm; Q8VCU1; -.
DR jPOST; Q8VCU1; -.
DR MaxQB; Q8VCU1; -.
DR PaxDb; Q8VCU1; -.
DR PeptideAtlas; Q8VCU1; -.
DR PRIDE; Q8VCU1; -.
DR ProteomicsDB; 275893; -. [Q8VCU1-1]
DR ProteomicsDB; 275894; -. [Q8VCU1-2]
DR DNASU; 13909; -.
DR Ensembl; ENSMUST00000074403; ENSMUSP00000074004; ENSMUSG00000062181. [Q8VCU1-2]
DR Ensembl; ENSMUST00000093221; ENSMUSP00000090909; ENSMUSG00000062181. [Q8VCU1-1]
DR GeneID; 13909; -.
DR KEGG; mmu:13909; -.
DR UCSC; uc009nbn.2; mouse. [Q8VCU1-1]
DR UCSC; uc012gjc.1; mouse. [Q8VCU1-2]
DR CTD; 13909; -.
DR MGI; MGI:3644960; Ces3b.
DR VEuPathDB; HostDB:ENSMUSG00000062181; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000155200; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; Q8VCU1; -.
DR OMA; RNTENMI; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q8VCU1; -.
DR TreeFam; TF315470; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR Reactome; R-MMU-8964038; LDL clearance.
DR BioGRID-ORCS; 13909; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ces3b; mouse.
DR PRO; PR:Q8VCU1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VCU1; protein.
DR Bgee; ENSMUSG00000062181; Expressed in liver and 7 other tissues.
DR ExpressionAtlas; Q8VCU1; baseline and differential.
DR Genevisible; Q8VCU1; MM.
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 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..571
FT /note="Carboxylesterase 3B"
FT /id="PRO_0000305195"
FT MOTIF 568..571
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 232
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 460
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..127
FT /evidence="ECO:0000250"
FT DISULFID 284..295
FT /evidence="ECO:0000250"
FT VAR_SEQ 431..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028269"
SQ SEQUENCE 571 AA; 63353 MW; 0D0AEE2DC846CFB7 CRC64;
MTNMRTMIPA GSSVLVWVTC LLLAFVTTVT GPKVIQPEVD TPLGRVRGRQ VGVKDTDRMV
NVFLGIPFAQ APVGPLRFSA PLPPQPWEGV RDASINPPMC LQDVEKMINS RFGLNEKIKI
FPISEDCLTL NIYSPTEITA GDKRPVMVWI HGGSLLVGSS TSQDGSALAA YGDVVVVTVQ
YRLGIFGFLS TGDKHMPGNR GFLDVVAALR WVQGNIAPFG GDPNCVTIFG NSAGGMIVSS
LFLSPISAGL FHRAISQSGI VTTIMMEDMK PWPEAQNFAN SVACGSASPA ELVQCLLQKE
GKDLIKQKNV NISYIVNDSF FPQRPEKLLA DQQFPTVPYL LGVTNHEFGW LLLKSLNILD
KLEHLSREDL LEISRPFLAI MEVPPEIMPT VIDEYLDNGS DQSATRYAFQ ELLGDISFII
PTLNFSKYLR DAGCPVFLYE FQHTPSSFAK FKPAWVKADH ASENSFVFGG PFLTDESSLL
AFPEATEEEK QLSLTMMAQW SQFARTGNPN GKGLPPWPQL NQLEQYLEIG LESRTGVKLK
KGRLQFWTET LPRKIQEWHR EQRSRKVPEE L
