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Protein

Carboxylesterase 1C

Gene

Ces1c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Involved in the extracellular metabolism of lung surfactant.

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei342 – 3421Charge relay systemBy similarity
Active sitei455 – 4551Charge relay systemBy similarity

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: MGI
  • hydrolase activity, acting on ester bonds Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Protein family/group databases

ESTHERimouse-Ces1c. Carb_B_Chordata.
MEROPSiS09.996.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxylesterase 1C (EC:3.1.1.1)
Alternative name(s):
Liver carboxylesterase N
Lung surfactant convertase
PES-N
Gene namesi
Name:Ces1c
Synonyms:Es1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:95420. Ces1c.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 554536Carboxylesterase 1CPRO_0000008574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Disulfide bondi87 ↔ 116By similarity
Disulfide bondi273 ↔ 284By similarity
Glycosylationi274 – 2741N-linked (GlcNAc...)1 Publication
Glycosylationi304 – 3041N-linked (GlcNAc...)2 Publications
Glycosylationi377 – 3771N-linked (GlcNAc...)2 Publications
Modified residuei473 – 4731PhosphoserineBy similarity
Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP23953.
MaxQBiP23953.
PaxDbiP23953.
PRIDEiP23953.

PTM databases

iPTMnetiP23953.
PhosphoSiteiP23953.

Expressioni

Tissue specificityi

Expressed in lung, kidney and liver.1 Publication

Gene expression databases

BgeeiP23953.
CleanExiMM_ES1.
ExpressionAtlasiP23953. baseline and differential.
GenevisibleiP23953. MM.

Interactioni

Protein-protein interaction databases

IntActiP23953. 2 interactions.
MINTiMINT-1864941.
STRINGi10090.ENSMUSP00000034189.

Structurei

3D structure databases

ProteinModelPortaliP23953.
SMRiP23953. Positions 24-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi551 – 5544Prevents secretion from ERSequence analysis

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP23953.
KOiK01044.
OMAiSANHYAT.
OrthoDBiEOG7RBZ7R.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLHALVWAS LAVCPILGHS LLPPVVDTTQ GKVLGKYISL EGFEQPVAVF
60 70 80 90 100
LGVPFAKPPL GSLRFAPPQP AEPWSFVKNA TSYPPMCSQD AGWAKILSDM
110 120 130 140 150
FSTEKEILPL KISEDCLYLN IYSPADLTKS SQLPVMVWIH GGGLVIGGAS
160 170 180 190 200
PYNGLALSAH ENVVVVTIQY RLGIWGLFST GDEHSPGNWA HLDQLAALRW
210 220 230 240 250
VQDNIANFGG NPDSVTIFGE SSGGISVSVL VLSPLGKDLF HRAISESGVV
260 270 280 290 300
INTNVGKKNI QAVNEIIATL SQCNDTSSAA MVQCLRQKTE SELLEISGKL
310 320 330 340 350
VQYNISLSTM IDGVVLPKAP EEILAEKSFN TVPYIVGFNK QEFGWIIPMM
360 370 380 390 400
LQNLLPEGKM NEETASLLLR RFHSELNISE SMIPAVIEQY LRGVDDPAKK
410 420 430 440 450
SELILDMFGD IFFGIPAVLL SRSLRDAGVS TYMYEFRYRP SFVSDKRPQT
460 470 480 490 500
VEGDHGDEIF FVFGAPLLKE GASEEETNLS KMVMKFWANF ARNGNPNGEG
510 520 530 540 550
LPHWPEYDEQ EGYLQIGATT QQAQRLKAEE VAFWTELLAK NPPETDPTEH

TEHK
Length:554
Mass (Da):61,056
Last modified:July 27, 2011 - v4
Checksum:iFBB166E6F9D570CD
GO

Sequence cautioni

The sequence AAA37579.1 differs from that shown.Sequencing errors.Curated
The sequence AAA37579.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → V in AAC04708 (PubMed:9815115).Curated
Sequence conflicti5 – 51A → V in AAH28907 (PubMed:15489334).Curated
Sequence conflicti96 – 961I → L in AAH28907 (PubMed:15489334).Curated
Sequence conflicti104 – 1041E → K in AAH28907 (PubMed:15489334).Curated
Sequence conflicti149 – 1491A → R in AAA63297 (PubMed:1840565).Curated
Sequence conflicti149 – 1491A → R in AAC04708 (PubMed:9815115).Curated
Sequence conflicti186 – 1861P → Q in AAC04708 (PubMed:9815115).Curated
Sequence conflicti186 – 1861P → Q in AAH28907 (PubMed:15489334).Curated
Sequence conflicti255 – 2551V → L in AAH28907 (PubMed:15489334).Curated
Sequence conflicti310 – 3101M → V in AAC04708 (PubMed:9815115).Curated
Sequence conflicti310 – 3101M → V in AAH28907 (PubMed:15489334).Curated
Sequence conflicti389 – 3891Q → K in AAC04708 (PubMed:9815115).Curated
Sequence conflicti389 – 3891Q → K in AAH28907 (PubMed:15489334).Curated
Sequence conflicti398 – 3981A → V in AAH28907 (PubMed:15489334).Curated
Sequence conflicti420 – 4201L → M in AAC04708 (PubMed:9815115).Curated
Sequence conflicti420 – 4201L → M in AAH28907 (PubMed:15489334).Curated
Sequence conflicti432 – 4321Y → S in AAH28907 (PubMed:15489334).Curated
Sequence conflicti450 – 4501T → M in AAC04708 (PubMed:9815115).Curated
Sequence conflicti450 – 4501T → M in AAH28907 (PubMed:15489334).Curated
Sequence conflicti461 – 4611F → S in AAC04708 (PubMed:9815115).Curated
Sequence conflicti461 – 4611F → S in AAH28907 (PubMed:15489334).Curated
Sequence conflicti510 – 5101Q → K in AAC04708 (PubMed:9815115).Curated
Sequence conflicti510 – 5101Q → K in AAH28907 (PubMed:15489334).Curated
Sequence conflicti538 – 5381L → P in AAC04708 (PubMed:9815115).Curated
Sequence conflicti538 – 5381L → P in AAH28907 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57960 mRNA. Translation: AAA63297.1.
AF034435 mRNA. Translation: AAC04708.1.
AC121985 Genomic DNA. No translation available.
AC162949 Genomic DNA. No translation available.
BC028907 mRNA. Translation: AAH28907.1.
M19677 mRNA. Translation: AAA37579.1. Sequence problems.
CCDSiCCDS22527.1.
PIRiA27686.
A39060.
RefSeqiNP_031980.2. NM_007954.4.
UniGeneiMm.88078.

Genome annotation databases

EnsembliENSMUST00000034189; ENSMUSP00000034189; ENSMUSG00000057400.
GeneIDi13884.
KEGGimmu:13884.
UCSCiuc009mul.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57960 mRNA. Translation: AAA63297.1.
AF034435 mRNA. Translation: AAC04708.1.
AC121985 Genomic DNA. No translation available.
AC162949 Genomic DNA. No translation available.
BC028907 mRNA. Translation: AAH28907.1.
M19677 mRNA. Translation: AAA37579.1. Sequence problems.
CCDSiCCDS22527.1.
PIRiA27686.
A39060.
RefSeqiNP_031980.2. NM_007954.4.
UniGeneiMm.88078.

3D structure databases

ProteinModelPortaliP23953.
SMRiP23953. Positions 24-540.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23953. 2 interactions.
MINTiMINT-1864941.
STRINGi10090.ENSMUSP00000034189.

Protein family/group databases

ESTHERimouse-Ces1c. Carb_B_Chordata.
MEROPSiS09.996.

PTM databases

iPTMnetiP23953.
PhosphoSiteiP23953.

Proteomic databases

EPDiP23953.
MaxQBiP23953.
PaxDbiP23953.
PRIDEiP23953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034189; ENSMUSP00000034189; ENSMUSG00000057400.
GeneIDi13884.
KEGGimmu:13884.
UCSCiuc009mul.2. mouse.

Organism-specific databases

CTDi13884.
MGIiMGI:95420. Ces1c.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP23953.
KOiK01044.
OMAiSANHYAT.
OrthoDBiEOG7RBZ7R.
TreeFamiTF315470.

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Miscellaneous databases

PROiP23953.
SOURCEiSearch...

Gene expression databases

BgeeiP23953.
CleanExiMM_ES1.
ExpressionAtlasiP23953. baseline and differential.
GenevisibleiP23953. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a murine cDNA encoding a member of the carboxylesterase multigene family."
    Ovnic M., Tepperman K., Medda S., Elliott R.W., Stephenson D.A., Grant S.G., Ganschow R.E.
    Genomics 9:344-354(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "Molecular cloning, characterization, and differential expression pattern of mouse lung surfactant convertase."
    Krishnasamy S., Teng A.L., Dhand R., Schultz R.M., Gross N.J.
    Am. J. Physiol. 275:L969-L975(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
    Strain: CF-1.
    Tissue: Lung.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  5. "cDNA cloning of esterase 1, the major esterase activity in mouse plasma."
    Genetta T.L., D'Eustachio P., Kadner S.S., Finlay T.H.
    Biochem. Biophys. Res. Commun. 151:1364-1370(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 487-554.
  6. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-304 AND ASN-377.
    Strain: C57BL/6J.
    Tissue: Plasma.
  7. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
    Bernhard O.K., Kapp E.A., Simpson R.J.
    J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79; ASN-274; ASN-304 AND ASN-377.
    Strain: C57BL/6J.
    Tissue: Plasma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiEST1C_MOUSE
AccessioniPrimary (citable) accession number: P23953
Secondary accession number(s): E9QQ07
, O54936, P11374, Q8K125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.