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Protein

Liver carboxylesterase 1

Gene
N/A
Organism
Oryctolagus cuniculus (Rabbit)
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.1 Publication

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 sitei467 – 4671Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.1.1. 1749.
SABIO-RKP12337.

Protein family/group databases

ESTHERirabit-1cxes. Carb_B_Chordata.
MEROPSiS09.981.

Names & Taxonomyi

Protein namesi
Recommended name:
Liver carboxylesterase 1 (EC:3.1.1.1)
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2623.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18183 PublicationsAdd
BLAST
Chaini19 – 565547Liver carboxylesterase 1PRO_0000008578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Disulfide bondi87 ↔ 116
Disulfide bondi273 ↔ 284
Glycosylationi389 – 3891N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005826.

Chemistry

BindingDBiP12337.

Structurei

Secondary structure

1
565
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Beta strandi47 – 5610Combined sources
Helixi61 – 633Combined sources
Beta strandi86 – 883Combined sources
Helixi91 – 10111Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi133 – 1397Combined sources
Turni143 – 1453Combined sources
Helixi155 – 1617Combined sources
Beta strandi164 – 1685Combined sources
Helixi173 – 1775Combined sources
Helixi189 – 20416Combined sources
Helixi205 – 2084Combined sources
Beta strandi210 – 22011Combined sources
Helixi222 – 23211Combined sources
Helixi234 – 2363Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2477Combined sources
Beta strandi253 – 2564Combined sources
Helixi261 – 27111Combined sources
Helixi278 – 28710Combined sources
Helixi290 – 30011Combined sources
Beta strandi324 – 3263Combined sources
Helixi331 – 3377Combined sources
Beta strandi345 – 3517Combined sources
Helixi376 – 3838Combined sources
Helixi385 – 3884Combined sources
Turni392 – 3943Combined sources
Helixi395 – 4028Combined sources
Helixi416 – 4249Combined sources
Helixi426 – 43712Combined sources
Turni438 – 4403Combined sources
Beta strandi443 – 4486Combined sources
Helixi469 – 4746Combined sources
Turni475 – 4795Combined sources
Beta strandi480 – 4823Combined sources
Helixi486 – 50520Combined sources
Beta strandi525 – 5317Combined sources
Beta strandi533 – 5353Combined sources
Helixi540 – 55213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K4YX-ray2.50A23-556[»]
ProteinModelPortaliP12337.
SMRiP12337. Positions 23-556.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12337.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi565 – 5651Prevents secretion from ERSequence analysis

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
KOiK01044.

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.

P12337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLCALALAS LAACTAWGHP SAPPVVDTVH GKVLGKFVSL EGFAQPVAVF
60 70 80 90 100
LGVPFAKPPL GSLRFAPPQP AESWSHVKNT TSYPPMCSQD AVSGHMLSEL
110 120 130 140 150
FTNRKENIPL KFSEDCLYLN IYTPADLTKR GRLPVMVWIH GGGLMVGGAS
160 170 180 190 200
TYDGLALSAH ENVVVVTIQY RLGIWGFFST GDEHSRGNWG HLDQVAALRW
210 220 230 240 250
VQDNIANFGG DPGSVTIFGE SAGGQSVSIL LLSPLTKNLF HRAISESGVA
260 270 280 290 300
LLSSLFRKNT KSLAEKIAIE AGCKTTTSAV MVHCLRQKTE EELMEVTLKM
310 320 330 340 350
KFMALDLVGD PKENTAFLTT VIDGVLLPKA PAEILAEKKY NMLPYMVGIN
360 370 380 390 400
QQEFGWIIPM QMLGYPLSEG KLDQKTATEL LWKSYPIVNV SKELTPVATE
410 420 430 440 450
KYLGGTDDPV KKKDLFLDML ADLLFGVPSV NVARHHRDAG APTYMYEYRY
460 470 480 490 500
RPSFSSDMRP KTVIGDHGDE IFSVLGAPFL KEGATEEEIK LSKMVMKYWA
510 520 530 540 550
NFARNGNPNG EGLPQWPAYD YKEGYLQIGA TTQAAQKLKD KEVAFWTELW
560
AKEAARPRET EHIEL
Length:565
Mass (Da):62,292
Last modified:August 16, 2004 - v3
Checksum:i0ACD61400CC81D2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301H → K AA sequence (PubMed:3343253).Curated
Sequence conflicti89 – 891Q → S AA sequence (PubMed:3343253).Curated
Sequence conflicti175 – 19824WGFFS…QVAAL → GGFGFNIDELFLVAVN AA sequence (PubMed:3343253).CuratedAdd
BLAST
Sequence conflicti335 – 3362LA → YE AA sequence (PubMed:3343253).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036930 mRNA. Translation: AAC39258.1.
PIRiA29923.
RefSeqiNP_001076234.1. NM_001082765.2.
UniGeneiOcu.2266.

Genome annotation databases

GeneIDi100009551.
KEGGiocu:100009551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036930 mRNA. Translation: AAC39258.1.
PIRiA29923.
RefSeqiNP_001076234.1. NM_001082765.2.
UniGeneiOcu.2266.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K4YX-ray2.50A23-556[»]
ProteinModelPortaliP12337.
SMRiP12337. Positions 23-556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005826.

Chemistry

BindingDBiP12337.
ChEMBLiCHEMBL2623.

Protein family/group databases

ESTHERirabit-1cxes. Carb_B_Chordata.
MEROPSiS09.981.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009551.
KEGGiocu:100009551.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
KOiK01044.

Enzyme and pathway databases

BRENDAi3.1.1.1. 1749.
SABIO-RKP12337.

Miscellaneous databases

EvolutionaryTraceiP12337.
PROiP12337.

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 nameiEST1_RABIT
AccessioniPrimary (citable) accession number: P12337
Secondary accession number(s): O77540
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 118 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.