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Protein

Carboxylesterase 1E

Gene

Ces1e

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs.

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 sitei353 – 3531Charge relay systemBy similarity
Active sitei466 – 4661Charge relay systemBy similarity

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: RGD
  • palmitoyl-CoA hydrolase activity Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.1.1. 5301.

Protein family/group databases

ESTHERiratno-Ces1e. Carb_B_Chordata.

Chemistry

SwissLipidsiSLP:000001459.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxylesterase 1E (EC:3.1.1.1)
Alternative name(s):
Carboxyesterase ES-3
ES-HTEL
Egasyn
Liver carboxylesterase 3
pI 5.5 esterase
Gene namesi
Name:Ces1e
Synonyms:Ces1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621508. Ces1e.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 561543Carboxylesterase 1EPRO_0000008580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi87 ↔ 116By similarity
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi273 ↔ 284By similarity
Modified residuei484 – 4841PhosphoserineBy similarity
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PeptideAtlasiQ63108.
PRIDEiQ63108.

PTM databases

iPTMnetiQ63108.

Interactioni

Protein-protein interaction databases

MINTiMINT-4565322.

Structurei

3D structure databases

ProteinModelPortaliQ63108.
SMRiQ63108. Positions 21-550.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi558 – 5614Prevents secretion from ERSequence analysis

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ63108.
PhylomeDBiQ63108.

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.

Q63108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCLYALILVF LAAFTAGGHP SSLPVVDTLQ GKVLGKYVSL EGFTQPVAVF
60 70 80 90 100
LGVPFAKPPL GSLRFAPPQP AEPWSFVKNT TSYPPMCSQD PVAGQIVNDL
110 120 130 140 150
LTNWEENISL QFSEDCLYLN IYTPADLTKR DRLPVMVWIH GGGLVLGGAS
160 170 180 190 200
TYDGLALSTH ENVVVVVIQY RLGIWGFFST GDEHSRGNWG HLDQVAALHW
210 220 230 240 250
VQDNIDNFGG DPGSVTIFGE SAGGESVSVL VLSPLAKNLF HKAISESGVA
260 270 280 290 300
LTAGLVKKNT RPLAEKIAVV SGCKSTTSAS MVHCLRQKTE EELLETTLKL
310 320 330 340 350
NLFSLDLHGD SRQSYPFVPT VLDGVVLPKM PEEILAEKDF NTVPYIVGIN
360 370 380 390 400
KQEFGWILPT MMNYPPSDMK LDPMTATSLL KKSSFLLNLP EEAIPVAVEK
410 420 430 440 450
YLRHTDDPDR NKDQLLELIG DVIFGVPSVI VSRGHRDAGA RTYMYEFQYR
460 470 480 490 500
PSFSSKMKPS TVVGDHGDEI YSVFGAPILR GGTSKEEINL SKMMMKFWAN
510 520 530 540 550
FARNGNPNGQ GLPHWPEYDQ KEGYLQIGAT TQQAQKLKEK EVAFWSELLA
560
MKPLHAGHTE L
Length:561
Mass (Da):61,715
Last modified:November 1, 1996 - v1
Checksum:i1E14D66DF089B86F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81395 mRNA. Translation: CAA57158.1.
PIRiJC2447.
UniGeneiRn.161717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81395 mRNA. Translation: CAA57158.1.
PIRiJC2447.
UniGeneiRn.161717.

3D structure databases

ProteinModelPortaliQ63108.
SMRiQ63108. Positions 21-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4565322.

Chemistry

ChEMBLiCHEMBL2771.
SwissLipidsiSLP:000001459.

Protein family/group databases

ESTHERiratno-Ces1e. Carb_B_Chordata.

PTM databases

iPTMnetiQ63108.

Proteomic databases

PeptideAtlasiQ63108.
PRIDEiQ63108.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi621508. Ces1e.

Phylogenomic databases

HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ63108.
PhylomeDBiQ63108.

Enzyme and pathway databases

BRENDAi3.1.1.1. 5301.

Miscellaneous databases

PROiQ63108.

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

  1. "Cloning and sequencing of rat liver carboxylesterase ES-3 (egasyn)."
    Robbi M., Beaufay H.
    Biochem. Biophys. Res. Commun. 203:1404-1411(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.

Entry informationi

Entry nameiEST1E_RAT
AccessioniPrimary (citable) accession number: Q63108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.