EST1C_RAT
ID EST1C_RAT Reviewed; 549 AA.
AC P10959; Q5I0K0; Q63106; Q64626;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Carboxylesterase 1C;
DE EC=3.1.1.1;
DE AltName: Full=Carboxyesterase ES-1;
DE Short=E1;
DE AltName: Full=ES-THET;
DE AltName: Full=Esterase-2;
DE AltName: Full=Liver carboxylesterase 1;
DE AltName: Full=Neutral retinyl ester hydrolase;
DE Short=NREH;
DE AltName: Full=Retinyl ester hydrolase;
DE Short=REH;
DE Flags: Precursor;
GN Name=Ces1c; Synonyms=Es2;
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], AND PROTEIN SEQUENCE OF 19-48.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3235453; DOI=10.1093/oxfordjournals.jbchem.a122553;
RA Takagi Y., Morohashi K., Kawabata S., Go M., Omura T.;
RT "Molecular cloning and nucleotide sequence of cDNA of microsomal
RT carboxyesterase E1 of rat liver.";
RL J. Biochem. 104:801-806(1988).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-549, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2973315; DOI=10.1016/s0006-291x(88)80924-0;
RA Long R.M., Satoh H., Martin B.M., Kimura S., Gonzalez F.J., Pohl L.R.;
RT "Rat liver carboxylesterase: cDNA cloning, sequencing, and evidence for a
RT multigene family.";
RL Biochem. Biophys. Res. Commun. 156:866-873(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-549.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8006016; DOI=10.1016/s0021-9258(17)32528-0;
RA Alexson S.E.H., Finlay T.H., Hellman U., Svensson L.T., Diczfalusy R.,
RA Eggertsen G.;
RT "Molecular cloning and identification of a rat serum carboxylesterase
RT expressed in the liver.";
RL J. Biol. Chem. 269:17118-17124(1994).
RN [5]
RP PROTEIN SEQUENCE OF 65-78; 106-124; 326-338 AND 424-437, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9305911; DOI=10.1074/jbc.272.39.24488;
RA Sun G., Alexson S.E.H., Harrison E.H.;
RT "Purification and characterization of a neutral, bile salt-independent
RT retinyl ester hydrolase from rat liver microsomes. Relationship To rat
RT carboxylesterase ES-2.";
RL J. Biol. Chem. 272:24488-24493(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics and in the
CC activation of ester and amide prodrugs. Involved in the extracellular
CC metabolism of lung surfactant (By similarity). {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 ECO:0000269|PubMed:9305911};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=69 uM for retinyl palmitate {ECO:0000269|PubMed:9305911};
CC Vmax=3.1 nmol/min/mg enzyme with retinyl palmitate as substrate
CC {ECO:0000269|PubMed:9305911};
CC pH dependence:
CC Optimum pH is 7.0. Active from pH 4.0-8.0.
CC {ECO:0000269|PubMed:9305911};
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; D30620; BAA06310.1; -; mRNA.
DR EMBL; D00362; BAA20565.1; -; mRNA.
DR EMBL; BC088251; AAH88251.1; -; mRNA.
DR EMBL; M20629; AAA40871.1; -; mRNA.
DR EMBL; X78489; CAA55241.1; -; mRNA.
DR PIR; A31584; A31584.
DR PIR; JX0054; JX0054.
DR RefSeq; NP_058700.1; NM_017004.1.
DR AlphaFoldDB; P10959; -.
DR SMR; P10959; -.
DR STRING; 10116.ENSRNOP00000024622; -.
DR ESTHER; ratno-Ces1c; Carb_B_Chordata.
DR GlyGen; P10959; 6 sites.
DR iPTMnet; P10959; -.
DR PhosphoSitePlus; P10959; -.
DR PaxDb; P10959; -.
DR PRIDE; P10959; -.
DR GeneID; 24346; -.
DR KEGG; rno:24346; -.
DR CTD; 13884; -.
DR RGD; 2571; Ces1c.
DR eggNOG; KOG1516; Eukaryota.
DR InParanoid; P10959; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P10959; -.
DR BRENDA; 3.1.1.1; 5301.
DR PRO; PR:P10959; -.
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; IDA:RGD.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Phosphoprotein; Reference proteome;
KW Serine esterase; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:3235453"
FT CHAIN 19..549
FT /note="Carboxylesterase 1C"
FT /id="PRO_0000008579"
FT MOTIF 546..549
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 221
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 340
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 453
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
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 VARIANT 372
FT /note="P -> L"
FT CONFLICT 5
FT /note="A -> V (in Ref. 2; AAH88251)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="V -> A (in Ref. 2; AAH88251)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="A -> R (in Ref. 4; CAA55241)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> N (in Ref. 2; AAH88251)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..175
FT /note="IW -> FG (in Ref. 3; AAA40871)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="A -> V (in Ref. 2; AAH88251)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="V -> L (in Ref. 1; BAA06310/BAA20565)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..368
FT /note="FLK -> LLR (in Ref. 2; AAH88251)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="K -> N (in Ref. 1; BAA06310/BAA20565)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="K -> E (in Ref. 1; BAA06310/BAA20565 and 2;
FT AAH88251)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..513
FT /note="LQ -> FE (in Ref. 4; CAA55241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 60175 MW; 18D6A586DA50E662 CRC64;
MWLCALVWAS LAVCPIWGHP SSPPVVDTTK GKVLGKYVSL EGFTQPVAVF LGVPFAKPPL
GSLRFAPPEP AEPWSFVKNT TTYPPMCSQD GVVGKLLADM LSTGKESIPL EFSEDCLYLN
IYSPADLTKN SRLPVMVWIH GGGLIIGGAS PYSGLALSAH ENVVVVTIQY RLGIWGLFST
GDEHSRGNWA HLDQLAALRW VQDNIANFGG NPDSVTIFGE SAGGVSVSAL VLSPLAKNLF
HRAISESGVV LTTNLDKKNT QAVAQMIATL SGCNNTSSAA MVQCLRQKTE AELLELTVKL
DNTSMSTVID GVVLPKTPEE ILTEKSFNTV PYIVGFNKQE FGWIIPTMMG NLLSEGRMNE
KMASSFLKRF SPNLNISESV IPAIIEKYLR GTDDPAKKKE LLLDMFSDVF FGIPAVLMSR
SLRDAGAPTY MYEFQYRPSF VSDQRPQTVQ GDHGDEIFSV FGTPFLKEGA SEEETNLSKL
VMKFWANFAR NGNPNGEGLP HWPKYDQKEG YLQIGATTQQ AQKLKGEEVA FWTELLAKNP
PQTEHTEHT
