EST5_RAT
ID EST5_RAT Reviewed; 561 AA.
AC Q63010; Q6AYA3; Q9QUX6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Liver carboxylesterase B-1;
DE EC=3.1.1.1;
DE AltName: Full=Liver microsomal carboxylesterase;
DE Flags: Precursor;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7961958; DOI=10.1016/s0021-9258(18)43935-x;
RA Yan B., Yang D., Brady M., Parkinson A.;
RT "Rat kidney carboxylesterase. Cloning, sequencing, cellular localization,
RT and relationship to rat liver hydrolase.";
RL J. Biol. Chem. 269:29688-29696(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Kidney;
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 [3]
RP PROTEIN SEQUENCE OF 19-40, NUCLEOTIDE SEQUENCE [MRNA] OF 113-121; 138-149;
RP 216-224; 350-356 AND 464-469, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=8597091; DOI=10.1016/0378-4274(95)03493-5;
RA Satoh T., Hosokawa M.;
RT "Molecular aspects of carboxylesterase isoforms in comparison with other
RT esterases.";
RL Toxicol. Lett. 82:439-445(1995).
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8597091}.
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; U10698; AAA64639.1; -; mRNA.
DR EMBL; BC079129; AAH79129.1; -; mRNA.
DR PIR; S71597; S71597.
DR RefSeq; NP_001019536.1; NM_001024365.1.
DR AlphaFoldDB; Q63010; -.
DR SMR; Q63010; -.
DR ELM; Q63010; -.
DR STRING; 10116.ENSRNOP00000024187; -.
DR BindingDB; Q63010; -.
DR ChEMBL; CHEMBL2366498; -.
DR ESTHER; ratno-lmcxe; Carb_B_Chordata.
DR MEROPS; S09.969; -.
DR GlyGen; Q63010; 1 site.
DR iPTMnet; Q63010; -.
DR PhosphoSitePlus; Q63010; -.
DR PaxDb; Q63010; -.
DR PRIDE; Q63010; -.
DR GeneID; 501232; -.
DR KEGG; rno:501232; -.
DR CTD; 501232; -.
DR eggNOG; KOG1516; Eukaryota.
DR PhylomeDB; Q63010; -.
DR PRO; PR:Q63010; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
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..18
FT /evidence="ECO:0000269|PubMed:8597091"
FT CHAIN 19..561
FT /note="Liver carboxylesterase B-1"
FT /id="PRO_0000008582"
FT MOTIF 558..561
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 221
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 353
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..116
FT /evidence="ECO:0000250"
FT DISULFID 273..284
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="M -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="A -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="V -> A (in Ref. 2; AAH79129)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="A -> G (in Ref. 2; AAH79129)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="R -> G (in Ref. 2; AAH79129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 62495 MW; 013C1C13ACEBC6C9 CRC64;
MCLRSLFLVS LATCVVCGNP SSPPVVDTMK GKVLGKYASL EGVTQSVAVF LGVPFAKPPL
GSLRFAPPQP AEPWSFVKNT TTYPPMCSQD ATKGQRMNDL LTNRKEKVHL QFSEDCLYLN
IYTPADFTKD SRMPVMVWIH GGGLTQGGAS TYDGQVLSAY ENVVVVAIQY RLGIWGFFST
GDEHSRGNWG HLDQVAALHW VQDNIANFGG DPGSVTIFGE SAGGFSVSVL VLSPLSKNLY
HRAISESGVV LITELFTKDV RPAAKQIADM AGCKTTTSAI IVHCLRQKTE EELLEIMEKM
NLIKLSSQRD TKESYHFLST VIDDVVLPKD PKEILAEKNF NTVPYIVGIN KQECGWLLPT
MMRFVPPDVK LDKKMAIMLL EKFASIYGIP EDIIPVAIEK YRKGSDDPIK IRDGILAFIG
DVLFCIPSVM VSRDHRDAGA PTYVYEYQYY PSFSSPQRPK DVVGDHADDV YSVFGAPILR
DGASEEEIKL SKMVMKFWAN FARNGNPNAR GLPHWPQYDQ KEEYLQIGAT TQQSQRLKAE
EVAFWTQLLA KRQPQPHHNE L
