EST1F_RAT
ID EST1F_RAT Reviewed; 561 AA.
AC Q64573; A2VCW1; Q62679;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Liver carboxylesterase 1F {ECO:0000305};
DE EC=3.1.1.1;
DE AltName: Full=Carboxyesterase ES-4 {ECO:0000303|PubMed:12230550};
DE AltName: Full=Kidney microsomal carboxylesterase;
DE AltName: Full=Microsomal palmitoyl-CoA hydrolase;
DE Flags: Precursor;
GN Name=Ces1f {ECO:0000312|RGD:1642419};
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=8611161; DOI=10.1042/bj3130821;
RA Robbi M., van Schaftingen E., Beaufay H.;
RT "Cloning and sequencing of rat liver carboxylesterase ES-4 (microsomal
RT palmitoyl-CoA hydrolase).";
RL Biochem. J. 313:821-826(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12230550; DOI=10.1046/j.1432-1033.2002.03121.x;
RA Sanghani S.P., Davis W.I., Dumaual N.G., Mahrenholz A., Bosron W.F.;
RT "Identification of microsomal rat liver carboxylesterases and their
RT activity with retinyl palmitate.";
RL Eur. J. Biochem. 269:4387-4398(2002).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs. Hydrolyzes retinyl esters
CC (PubMed:12230550). Hydrolyzes p-nitrophenyl butyrate (PNPB),
CC triacylglycerol and monoacylglycerol. Shows higher activity against
CC PNPB, a short-chain fatty acid ester, than against triolein, a long-
CC chain fatty acid ester. Shows no detectable activity against
CC diacylglycerol, cholesterol ester or phospholipids. May play a role in
CC adipocyte lipolysis (By similarity). {ECO:0000250|UniProtKB:Q91WU0,
CC ECO:0000269|PubMed:12230550}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616; Evidence={ECO:0000269|PubMed:12230550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000305|PubMed:12230550};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 uM for retinyl palmitate {ECO:0000269|PubMed:12230550};
CC Note=kcat is 0.45 min(-1) with retinyl palmitate as substrate.
CC {ECO:0000269|PubMed:12230550};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q91WU0}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91WU0}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q91WU0}. Microsome
CC {ECO:0000269|PubMed:12230550}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney.
CC {ECO:0000269|PubMed:12230550}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X81825; CAA57419.1; -; mRNA.
DR EMBL; U10697; AAA64638.1; -; mRNA.
DR EMBL; BC128711; AAI28712.1; -; mRNA.
DR PIR; S62788; S62788.
DR RefSeq; NP_001096829.2; NM_001103359.2.
DR AlphaFoldDB; Q64573; -.
DR SMR; Q64573; -.
DR ESTHER; ratno-kmcxe; Carb_B_Chordata.
DR MEROPS; S09.965; -.
DR GlyGen; Q64573; 1 site.
DR PRIDE; Q64573; -.
DR Ensembl; ENSRNOT00000024187; ENSRNOP00000024187; ENSRNOG00000015438.
DR GeneID; 100125372; -.
DR KEGG; rno:100125372; -.
DR CTD; 234564; -.
DR RGD; 1642419; Ces1f.
DR GeneTree; ENSGT00940000154623; -.
DR InParanoid; Q64573; -.
DR OrthoDB; 754103at2759; -.
DR BRENDA; 3.1.1.1; 5301.
DR PRO; PR:Q64573; -.
DR Proteomes; UP000002494; Chromosome 19.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
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 GO; GO:0001523; P:retinoid metabolic process; TAS:UniProtKB.
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 Cytoplasm; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid droplet; Microsome; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..561
FT /note="Liver carboxylesterase 1F"
FT /id="PRO_0000008581"
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|UniProtKB:P23141"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..116
FT /evidence="ECO:0000250|UniProtKB:Q99K10"
FT DISULFID 273..284
FT /evidence="ECO:0000250|UniProtKB:Q99K10"
FT CONFLICT 7
FT /note="F -> I (in Ref. 1; CAA57419)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="L -> P (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="G -> A (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="P -> T (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
FT CONFLICT 310..311
FT /note="DN -> IT (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="T -> N (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
FT CONFLICT 425..426
FT /note="SI -> FY (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="G -> A (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="Q -> E (in Ref. 2; AAA64638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 62308 MW; EDF48D0F42F2AA1A CRC64;
MCLSFLFLVS LATCVVYGNP SSPPVVDTTK GKVLGKYVSL EGVTQSVAVF LGVPFAKPPL
GSLRFAPPQP AEPWSFVKNT TTYPPMCSQD AAKGQRMNDL LTNRKEKIHL EFSEDCLYLN
IYTPADFTKN SRLPVMVWIH GGGMTLGGAS TYDGRVLSAY ENVVVVAIQY RLGIWGFFST
GDEHSRGNWG HLDQVAALHW VQDNIANFGG DPGSVTIFGE SAGGFSVSVL VLSPLTKNLF
HRAISESGVV FLPGLLTKDV RPAAKQIADM AGCETTTSAI IVHCLRQKTE EELLEIMKKM
NLIKLSSQRD NKESYHFLST VVDNVVLPKD PKEILAEKNF NTVPYIVGIN KQECGWLLPT
MMGFVPADVE LDKKMAITLL EKFASLYGIP EDIIPVAIEK YRKGSDDSIK IRDGILAFIG
DVSFSIPSVM VSRDHRDAGA PTYMYEYQYY PSFSSPQRPK HVVGDHADDL YSVFGAPILR
DGASEEEIKL SKMVMKFWAN FARNGNPNGR GLPHWPQYDQ KEEYLQIGAT TQQSQRLKAE
EVAFWTQLLA KRQPQPHHNE L
