EST1C_MOUSE
ID EST1C_MOUSE Reviewed; 554 AA.
AC P23953; E9QQ07; O54936; P11374; Q8K125;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Carboxylesterase 1C;
DE EC=3.1.1.1;
DE AltName: Full=Liver carboxylesterase N;
DE AltName: Full=Lung surfactant convertase;
DE AltName: Full=PES-N;
DE Flags: Precursor;
GN Name=Ces1c; Synonyms=Es1;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=1840565; DOI=10.1016/0888-7543(91)90263-e;
RA Ovnic M., Tepperman K., Medda S., Elliott R.W., Stephenson D.A.,
RA Grant S.G., Ganschow R.E.;
RT "Characterization of a murine cDNA encoding a member of the
RT carboxylesterase multigene family.";
RL Genomics 9:344-354(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=CF-1; TISSUE=Lung;
RX PubMed=9815115; DOI=10.1152/ajplung.1998.275.5.l969;
RA Krishnasamy S., Teng A.L., Dhand R., Schultz R.M., Gross N.J.;
RT "Molecular cloning, characterization, and differential expression pattern
RT of mouse lung surfactant convertase.";
RL Am. J. Physiol. 275:L969-L975(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 487-554.
RX PubMed=2895647; DOI=10.1016/s0006-291x(88)80513-8;
RA Genetta T.L., D'Eustachio P., Kadner S.S., Finlay T.H.;
RT "cDNA cloning of esterase 1, the major esterase activity in mouse plasma.";
RL Biochem. Biophys. Res. Commun. 151:1364-1370(1988).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-304 AND ASN-377.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79; ASN-274; ASN-304 AND
RP ASN-377.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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. Involved in the extracellular
CC metabolism of lung surfactant.
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. Note=Microsomal
CC membrane, lumen of endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Expressed in lung, kidney and liver.
CC {ECO:0000269|PubMed:9815115}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37579.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA37579.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; M57960; AAA63297.1; -; mRNA.
DR EMBL; AF034435; AAC04708.1; -; mRNA.
DR EMBL; AC121985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028907; AAH28907.1; -; mRNA.
DR EMBL; M19677; AAA37579.1; ALT_SEQ; mRNA.
DR CCDS; CCDS22527.1; -.
DR PIR; A27686; A27686.
DR PIR; A39060; A39060.
DR RefSeq; NP_031980.2; NM_007954.4.
DR AlphaFoldDB; P23953; -.
DR SMR; P23953; -.
DR IntAct; P23953; 1.
DR MINT; P23953; -.
DR STRING; 10090.ENSMUSP00000034189; -.
DR ESTHER; mouse-Ces1c; Carb_B_Chordata.
DR MEROPS; S09.996; -.
DR GlyConnect; 779; 1 N-Linked glycan (1 site).
DR GlyGen; P23953; 5 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P23953; -.
DR PhosphoSitePlus; P23953; -.
DR CPTAC; non-CPTAC-3800; -.
DR jPOST; P23953; -.
DR MaxQB; P23953; -.
DR PaxDb; P23953; -.
DR PeptideAtlas; P23953; -.
DR PRIDE; P23953; -.
DR ProteomicsDB; 275891; -.
DR DNASU; 13884; -.
DR Ensembl; ENSMUST00000034189; ENSMUSP00000034189; ENSMUSG00000057400.
DR GeneID; 13884; -.
DR KEGG; mmu:13884; -.
DR UCSC; uc009mul.2; mouse.
DR CTD; 13884; -.
DR MGI; MGI:95420; Ces1c.
DR VEuPathDB; HostDB:ENSMUSG00000057400; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000154623; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; P23953; -.
DR OMA; FQHRSSA; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P23953; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 3474.
DR BioGRID-ORCS; 13884; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ces1c; mouse.
DR PRO; PR:P23953; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P23953; protein.
DR Bgee; ENSMUSG00000057400; Expressed in liver and 45 other tissues.
DR ExpressionAtlas; P23953; baseline and differential.
DR Genevisible; P23953; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:MGI.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:MGI.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004771; F:sterol esterase activity; ISO:MGI.
DR GO; GO:0071397; P:cellular response to cholesterol; ISO:MGI.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISO:MGI.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISO:MGI.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI.
DR GO; GO:0090205; P:positive regulation of cholesterol metabolic process; ISO:MGI.
DR GO; GO:0070857; P:regulation of bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0120188; P:regulation of bile acid secretion; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
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:0000250"
FT CHAIN 19..554
FT /note="Carboxylesterase 1C"
FT /id="PRO_0000008574"
FT MOTIF 551..554
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 342
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10959"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 478
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 5
FT /note="A -> V (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="I -> L (in Ref. 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> K (in Ref. 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> R (in Ref. 1; AAA63297 and 2; AAC04708)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="P -> Q (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="V -> L (in Ref. 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="M -> V (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Q -> K (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="A -> V (in Ref. 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="L -> M (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="Y -> S (in Ref. 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="T -> M (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="F -> S (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="Q -> K (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="L -> P (in Ref. 2; AAC04708 and 4; AAH28907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 61056 MW; FBB166E6F9D570CD CRC64;
MWLHALVWAS LAVCPILGHS LLPPVVDTTQ GKVLGKYISL EGFEQPVAVF LGVPFAKPPL
GSLRFAPPQP AEPWSFVKNA TSYPPMCSQD AGWAKILSDM FSTEKEILPL KISEDCLYLN
IYSPADLTKS SQLPVMVWIH GGGLVIGGAS PYNGLALSAH ENVVVVTIQY RLGIWGLFST
GDEHSPGNWA HLDQLAALRW VQDNIANFGG NPDSVTIFGE SSGGISVSVL VLSPLGKDLF
HRAISESGVV INTNVGKKNI QAVNEIIATL SQCNDTSSAA MVQCLRQKTE SELLEISGKL
VQYNISLSTM IDGVVLPKAP EEILAEKSFN TVPYIVGFNK QEFGWIIPMM LQNLLPEGKM
NEETASLLLR RFHSELNISE SMIPAVIEQY LRGVDDPAKK SELILDMFGD IFFGIPAVLL
SRSLRDAGVS TYMYEFRYRP SFVSDKRPQT VEGDHGDEIF FVFGAPLLKE GASEEETNLS
KMVMKFWANF ARNGNPNGEG LPHWPEYDEQ EGYLQIGATT QQAQRLKAEE VAFWTELLAK
NPPETDPTEH TEHK
