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Protein

Liver carboxylesterase B-1

Gene
N/A
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei221Acyl-ester intermediatePROSITE-ProRule annotation1
Active sitei353Charge relay systemBy similarity1
Active sitei466Charge relay systemBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERiratno-lmcxe. Carb_B_Chordata.
MEROPSiS09.969.

Names & Taxonomyi

Protein namesi
Recommended name:
Liver carboxylesterase B-1 (EC:3.1.1.1)
Alternative name(s):
Liver microsomal carboxylesterase
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2366498.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_000000858219 – 561Liver carboxylesterase B-1Add BLAST543

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi87 ↔ 116By similarity
Disulfide bondi273 ↔ 284By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ63010.
PRIDEiQ63010.

PTM databases

iPTMnetiQ63010.
PhosphoSitePlusiQ63010.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

MINTiMINT-4997337.
STRINGi10116.ENSRNOP00000024187.

Structurei

3D structure databases

ProteinModelPortaliQ63010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi558 – 561Prevents secretion from ERPROSITE-ProRule annotation4

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOVERGENiHBG008839.
PhylomeDBiQ63010.

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.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q63010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCLRSLFLVS LATCVVCGNP SSPPVVDTMK GKVLGKYASL EGVTQSVAVF
60 70 80 90 100
LGVPFAKPPL GSLRFAPPQP AEPWSFVKNT TTYPPMCSQD ATKGQRMNDL
110 120 130 140 150
LTNRKEKVHL QFSEDCLYLN IYTPADFTKD SRMPVMVWIH GGGLTQGGAS
160 170 180 190 200
TYDGQVLSAY ENVVVVAIQY RLGIWGFFST GDEHSRGNWG HLDQVAALHW
210 220 230 240 250
VQDNIANFGG DPGSVTIFGE SAGGFSVSVL VLSPLSKNLY HRAISESGVV
260 270 280 290 300
LITELFTKDV RPAAKQIADM AGCKTTTSAI IVHCLRQKTE EELLEIMEKM
310 320 330 340 350
NLIKLSSQRD TKESYHFLST VIDDVVLPKD PKEILAEKNF NTVPYIVGIN
360 370 380 390 400
KQECGWLLPT MMRFVPPDVK LDKKMAIMLL EKFASIYGIP EDIIPVAIEK
410 420 430 440 450
YRKGSDDPIK IRDGILAFIG DVLFCIPSVM VSRDHRDAGA PTYVYEYQYY
460 470 480 490 500
PSFSSPQRPK DVVGDHADDV YSVFGAPILR DGASEEEIKL SKMVMKFWAN
510 520 530 540 550
FARNGNPNAR GLPHWPQYDQ KEEYLQIGAT TQQSQRLKAE EVAFWTQLLA
560
KRQPQPHHNE L
Length:561
Mass (Da):62,495
Last modified:November 1, 1996 - v1
Checksum:i013C1C13ACEBC6C9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19N → D AA sequence (PubMed:8597091).Curated1
Sequence conflicti29M → V AA sequence (PubMed:8597091).Curated1
Sequence conflicti38A → V AA sequence (PubMed:8597091).Curated1
Sequence conflicti422V → A in AAH79129 (PubMed:15489334).Curated1
Sequence conflicti509A → G in AAH79129 (PubMed:15489334).Curated1
Sequence conflicti536R → G in AAH79129 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10698 mRNA. Translation: AAA64639.1.
BC079129 mRNA. Translation: AAH79129.1.
PIRiS71597.
RefSeqiNP_001019536.1. NM_001024365.1.
UniGeneiRn.202952.
Rn.82692.

Genome annotation databases

GeneIDi501232.
KEGGirno:501232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10698 mRNA. Translation: AAA64639.1.
BC079129 mRNA. Translation: AAH79129.1.
PIRiS71597.
RefSeqiNP_001019536.1. NM_001024365.1.
UniGeneiRn.202952.
Rn.82692.

3D structure databases

ProteinModelPortaliQ63010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997337.
STRINGi10116.ENSRNOP00000024187.

Chemistry databases

ChEMBLiCHEMBL2366498.

Protein family/group databases

ESTHERiratno-lmcxe. Carb_B_Chordata.
MEROPSiS09.969.

PTM databases

iPTMnetiQ63010.
PhosphoSitePlusiQ63010.

Proteomic databases

PaxDbiQ63010.
PRIDEiQ63010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi501232.
KEGGirno:501232.

Organism-specific databases

CTDi501232.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOVERGENiHBG008839.
PhylomeDBiQ63010.

Miscellaneous databases

PROiQ63010.

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.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEST5_RAT
AccessioniPrimary (citable) accession number: Q63010
Secondary accession number(s): Q6AYA3, Q9QUX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 107 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, 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.