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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)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

  1. carboxylic ester hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

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
ProteomesiUP000002494 Componenti: Unplaced

Subcellular locationi

  1. Endoplasmic reticulum lumen

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

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 561543Liver carboxylesterase B-1PRO_0000008582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi87 ↔ 116By similarity
Disulfide bondi273 ↔ 284By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ63010.

PTM databases

PhosphoSiteiQ63010.

Expressioni

Gene expression databases

GenevestigatoriQ63010.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

MINTiMINT-4997337.
STRINGi10116.ENSRNOP00000024187.

Structurei

3D structure databases

ProteinModelPortaliQ63010.
SMRiQ63010. Positions 21-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi558 – 5614Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191N → D AA sequence (PubMed:8597091).Curated
Sequence conflicti29 – 291M → V AA sequence (PubMed:8597091).Curated
Sequence conflicti38 – 381A → V AA sequence (PubMed:8597091).Curated
Sequence conflicti422 – 4221V → A in AAH79129 (PubMed:15489334).Curated
Sequence conflicti509 – 5091A → G in AAH79129 (PubMed:15489334).Curated
Sequence conflicti536 – 5361R → G in AAH79129 (PubMed:15489334).Curated

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.

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.

3D structure databases

ProteinModelPortaliQ63010.
SMRiQ63010. Positions 21-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997337.
STRINGi10116.ENSRNOP00000024187.

Chemistry

ChEMBLiCHEMBL2366498.

Protein family/group databases

MEROPSiS09.969.

PTM databases

PhosphoSiteiQ63010.

Proteomic databases

PRIDEiQ63010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi501232.
KEGGirno:501232.

Organism-specific databases

CTDi501232.

Phylogenomic databases

HOVERGENiHBG008839.
PhylomeDBiQ63010.

Miscellaneous databases

NextBioi708661.
PROiQ63010.

Gene expression databases

GenevestigatoriQ63010.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Rat kidney carboxylesterase. Cloning, sequencing, cellular localization, and relationship to rat liver hydrolase."
    Yan B., Yang D., Brady M., Parkinson A.
    J. Biol. Chem. 269:29688-29696(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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: Brown Norway.
    Tissue: Kidney.
  3. "Molecular aspects of carboxylesterase isoforms in comparison with other esterases."
    Satoh T., Hosokawa M.
    Toxicol. Lett. 82:439-445(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-40, NUCLEOTIDE SEQUENCE [MRNA] OF 113-121; 138-149; 216-224; 350-356 AND 464-469, SUBUNIT.
    Tissue: Liver.

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: April 29, 2015
This is version 98 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

External Data

Dasty 3

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 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.