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P23953 (EST1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxylesterase 1C

EC=3.1.1.1
Alternative name(s):
Liver carboxylesterase N
Lung surfactant convertase
PES-N
Gene names
Name:Ces1c
Synonyms:Es1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

A carboxylic ester + H2O = an alcohol + a carboxylate.

Subcellular location

Endoplasmic reticulum lumen. Note: Microsomal membrane, lumen of endoplasmic reticulum.

Tissue specificity

Expressed in lung, kidney and liver. Ref.2

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence caution

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

The sequence AAA37579.1 differs from that shown. Reason: Sequencing errors.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 554536Carboxylesterase 1C
PRO_0000008574

Regions

Motif551 – 5544Prevents secretion from ER Potential

Sites

Active site2211Acyl-ester intermediate By similarity
Active site3421Charge relay system By similarity
Active site4551Charge relay system By similarity

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Ref.7
Glycosylation2741N-linked (GlcNAc...) Ref.7
Glycosylation3041N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation3771N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation4781N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 116 By similarity
Disulfide bond273 ↔ 284 By similarity

Experimental info

Sequence conflict51A → V in AAC04708. Ref.2
Sequence conflict51A → V in AAH28907. Ref.4
Sequence conflict961I → L in AAH28907. Ref.4
Sequence conflict1041E → K in AAH28907. Ref.4
Sequence conflict1491A → R in AAA63297. Ref.1
Sequence conflict1491A → R in AAC04708. Ref.2
Sequence conflict1861P → Q in AAC04708. Ref.2
Sequence conflict1861P → Q in AAH28907. Ref.4
Sequence conflict2551V → L in AAH28907. Ref.4
Sequence conflict3101M → V in AAC04708. Ref.2
Sequence conflict3101M → V in AAH28907. Ref.4
Sequence conflict3891Q → K in AAC04708. Ref.2
Sequence conflict3891Q → K in AAH28907. Ref.4
Sequence conflict3981A → V in AAH28907. Ref.4
Sequence conflict4201L → M in AAC04708. Ref.2
Sequence conflict4201L → M in AAH28907. Ref.4
Sequence conflict4321Y → S in AAH28907. Ref.4
Sequence conflict4501T → M in AAC04708. Ref.2
Sequence conflict4501T → M in AAH28907. Ref.4
Sequence conflict4611F → S in AAC04708. Ref.2
Sequence conflict4611F → S in AAH28907. Ref.4
Sequence conflict5101Q → K in AAC04708. Ref.2
Sequence conflict5101Q → K in AAH28907. Ref.4
Sequence conflict5381L → P in AAC04708. Ref.2
Sequence conflict5381L → P in AAH28907. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P23953 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: FBB166E6F9D570CD

FASTA55461,056
        10         20         30         40         50         60 
MWLHALVWAS LAVCPILGHS LLPPVVDTTQ GKVLGKYISL EGFEQPVAVF LGVPFAKPPL 

        70         80         90        100        110        120 
GSLRFAPPQP AEPWSFVKNA TSYPPMCSQD AGWAKILSDM FSTEKEILPL KISEDCLYLN 

       130        140        150        160        170        180 
IYSPADLTKS SQLPVMVWIH GGGLVIGGAS PYNGLALSAH ENVVVVTIQY RLGIWGLFST 

       190        200        210        220        230        240 
GDEHSPGNWA HLDQLAALRW VQDNIANFGG NPDSVTIFGE SSGGISVSVL VLSPLGKDLF 

       250        260        270        280        290        300 
HRAISESGVV INTNVGKKNI QAVNEIIATL SQCNDTSSAA MVQCLRQKTE SELLEISGKL 

       310        320        330        340        350        360 
VQYNISLSTM IDGVVLPKAP EEILAEKSFN TVPYIVGFNK QEFGWIIPMM LQNLLPEGKM 

       370        380        390        400        410        420 
NEETASLLLR RFHSELNISE SMIPAVIEQY LRGVDDPAKK SELILDMFGD IFFGIPAVLL 

       430        440        450        460        470        480 
SRSLRDAGVS TYMYEFRYRP SFVSDKRPQT VEGDHGDEIF FVFGAPLLKE GASEEETNLS 

       490        500        510        520        530        540 
KMVMKFWANF ARNGNPNGEG LPHWPEYDEQ EGYLQIGATT QQAQRLKAEE VAFWTELLAK 

       550 
NPPETDPTEH TEHK 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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, MASS SPECTROMETRY.
Strain: C57BL/6.
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, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00138342.
PIRA27686.
A39060.
RefSeqNP_031980.2. NM_007954.4.
UniGeneMm.88078.

3D structure databases

ProteinModelPortalP23953.
SMRP23953. Positions 24-540.
ModBaseSearch...

Protein family/group databases

MEROPSS09.996.

PTM databases

PhosphoSiteP23953.

Proteomic databases

PaxDbP23953.
PRIDEP23953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034189; ENSMUSP00000034189; ENSMUSG00000057400.
GeneID13884.
KEGGmmu:13884.
UCSCuc009mul.2. mouse.

Organism-specific databases

CTD13884.
MGIMGI:95420. Ces1c.

Phylogenomic databases

eggNOGCOG2272.
GeneTreeENSGT00670000097643.
HOGENOMHOG000091866.
HOVERGENHBG008839.
InParanoidP23953.
KOK03927.
OMANEDEQEW.
OrthoDBEOG466VM9.

Gene expression databases

ArrayExpressP23953.
BgeeP23953.
CleanExMM_ES1.
GenevestigatorP23953.
GermOnlineENSMUSG00000057400. Mus musculus.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284812.
SOURCESearch...

Entry information

Entry nameEST1C_MOUSE
AccessionPrimary (citable) accession number: P23953
Secondary accession number(s): E9QQ07 expand/collapse secondary AC list , O54936, P11374, Q8K125
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families