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Protein

Carboxylesterase 1C

Gene

Ces1c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.PROSITE-ProRule annotation1 Publication

Kineticsi

  1. KM=69 µM for retinyl palmitate1 Publication
  1. Vmax=3.1 nmol/min/mg enzyme with retinyl palmitate as substrate1 Publication

pH dependencei

Optimum pH is 7.0. Active from pH 4.0-8.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei340 – 3401Charge relay systemBy similarity
Active sitei453 – 4531Charge relay systemBy similarity

GO - Molecular functioni

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

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERiratno-Ces1c. Carb_B_Chordata.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxylesterase 1C (EC:3.1.1.1)
Alternative name(s):
Carboxyesterase ES-1
Short name:
E1
ES-THET
Esterase-2
Liver carboxylesterase 1
Neutral retinyl ester hydrolase
Short name:
NREH
Retinyl ester hydrolase
Short name:
REH
Gene namesi
Name:Ces1c
Synonyms:Es2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2571. Ces1c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 549531Carboxylesterase 1CPRO_0000008579Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi87 ↔ 116By similarity
Disulfide bondi273 ↔ 284By similarity
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence analysis
Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence analysis
Modified residuei471 – 4711PhosphoserineCombined sources
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP10959.
PRIDEiP10959.

PTM databases

iPTMnetiP10959.
PhosphoSiteiP10959.

Interactioni

Protein-protein interaction databases

MINTiMINT-4566562.
STRINGi10116.ENSRNOP00000024622.

Structurei

3D structure databases

ProteinModelPortaliP10959.
SMRiP10959. Positions 21-538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi546 – 5494Prevents secretion from ERSequence analysis

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOVERGENiHBG008839.
InParanoidiP10959.
KOiK01044.
PhylomeDBiP10959.

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.

P10959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLCALVWAS LAVCPIWGHP SSPPVVDTTK GKVLGKYVSL EGFTQPVAVF
60 70 80 90 100
LGVPFAKPPL GSLRFAPPEP AEPWSFVKNT TTYPPMCSQD GVVGKLLADM
110 120 130 140 150
LSTGKESIPL EFSEDCLYLN IYSPADLTKN SRLPVMVWIH GGGLIIGGAS
160 170 180 190 200
PYSGLALSAH ENVVVVTIQY RLGIWGLFST GDEHSRGNWA HLDQLAALRW
210 220 230 240 250
VQDNIANFGG NPDSVTIFGE SAGGVSVSAL VLSPLAKNLF HRAISESGVV
260 270 280 290 300
LTTNLDKKNT QAVAQMIATL SGCNNTSSAA MVQCLRQKTE AELLELTVKL
310 320 330 340 350
DNTSMSTVID GVVLPKTPEE ILTEKSFNTV PYIVGFNKQE FGWIIPTMMG
360 370 380 390 400
NLLSEGRMNE KMASSFLKRF SPNLNISESV IPAIIEKYLR GTDDPAKKKE
410 420 430 440 450
LLLDMFSDVF FGIPAVLMSR SLRDAGAPTY MYEFQYRPSF VSDQRPQTVQ
460 470 480 490 500
GDHGDEIFSV FGTPFLKEGA SEEETNLSKL VMKFWANFAR NGNPNGEGLP
510 520 530 540
HWPKYDQKEG YLQIGATTQQ AQKLKGEEVA FWTELLAKNP PQTEHTEHT
Length:549
Mass (Da):60,175
Last modified:November 1, 1997 - v3
Checksum:i18D6A586DA50E662
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → V in AAH88251 (PubMed:15489334).Curated
Sequence conflicti13 – 131V → A in AAH88251 (PubMed:15489334).Curated
Sequence conflicti48 – 481A → R in CAA55241 (PubMed:8006016).Curated
Sequence conflicti107 – 1071S → N in AAH88251 (PubMed:15489334).Curated
Sequence conflicti174 – 1752IW → FG in AAA40871 (PubMed:2973315).Curated
Sequence conflicti229 – 2291A → V in AAH88251 (PubMed:15489334).Curated
Sequence conflicti250 – 2501V → L in BAA06310 (PubMed:3235453).Curated
Sequence conflicti250 – 2501V → L in BAA20565 (PubMed:3235453).Curated
Sequence conflicti366 – 3683FLK → LLR in AAH88251 (PubMed:15489334).Curated
Sequence conflicti399 – 3991K → N in BAA06310 (PubMed:3235453).Curated
Sequence conflicti399 – 3991K → N in BAA20565 (PubMed:3235453).Curated
Sequence conflicti504 – 5041K → E in BAA06310 (PubMed:3235453).Curated
Sequence conflicti504 – 5041K → E in BAA20565 (PubMed:3235453).Curated
Sequence conflicti504 – 5041K → E in AAH88251 (PubMed:15489334).Curated
Sequence conflicti512 – 5132LQ → FE in CAA55241 (PubMed:8006016).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti372 – 3721P → L.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30620 mRNA. Translation: BAA06310.1.
D00362 mRNA. Translation: BAA20565.1.
BC088251 mRNA. Translation: AAH88251.1.
M20629 mRNA. Translation: AAA40871.1.
X78489 mRNA. Translation: CAA55241.1.
PIRiA31584.
JX0054.
RefSeqiNP_058700.1. NM_017004.1.
UniGeneiRn.2549.

Genome annotation databases

GeneIDi24346.
KEGGirno:24346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30620 mRNA. Translation: BAA06310.1.
D00362 mRNA. Translation: BAA20565.1.
BC088251 mRNA. Translation: AAH88251.1.
M20629 mRNA. Translation: AAA40871.1.
X78489 mRNA. Translation: CAA55241.1.
PIRiA31584.
JX0054.
RefSeqiNP_058700.1. NM_017004.1.
UniGeneiRn.2549.

3D structure databases

ProteinModelPortaliP10959.
SMRiP10959. Positions 21-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4566562.
STRINGi10116.ENSRNOP00000024622.

Protein family/group databases

ESTHERiratno-Ces1c. Carb_B_Chordata.

PTM databases

iPTMnetiP10959.
PhosphoSiteiP10959.

Proteomic databases

PaxDbiP10959.
PRIDEiP10959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24346.
KEGGirno:24346.

Organism-specific databases

CTDi13884.
RGDi2571. Ces1c.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOVERGENiHBG008839.
InParanoidiP10959.
KOiK01044.
PhylomeDBiP10959.

Miscellaneous databases

PROiP10959.

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...

Entry informationi

Entry nameiEST1C_RAT
AccessioniPrimary (citable) accession number: P10959
Secondary accession number(s): Q5I0K0, Q63106, Q64626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 126 of the entry and version 3 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. 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.