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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)DescriptionActionsGraphical viewLength
Active sitei221Acyl-ester intermediatePROSITE-ProRule annotation1
Active sitei353Charge relay systemBy similarity1
Active sitei467Charge relay systemBy similarity1

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 databases

ChEMBLiCHEMBL2623.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 183 PublicationsAdd BLAST18
ChainiPRO_000000857819 – 565Liver carboxylesterase 1Add BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...)1 Publication1
Disulfide bondi87 ↔ 116
Disulfide bondi273 ↔ 284
Glycosylationi389N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP12337.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005826.

Chemistry databases

BindingDBiP12337.

Structurei

Secondary structure

1565
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Beta strandi47 – 56Combined sources10
Helixi61 – 63Combined sources3
Beta strandi86 – 88Combined sources3
Helixi91 – 101Combined sources11
Beta strandi103 – 106Combined sources4
Beta strandi112 – 114Combined sources3
Beta strandi118 – 123Combined sources6
Beta strandi133 – 139Combined sources7
Turni143 – 145Combined sources3
Helixi155 – 161Combined sources7
Beta strandi164 – 168Combined sources5
Helixi173 – 177Combined sources5
Helixi189 – 204Combined sources16
Helixi205 – 208Combined sources4
Beta strandi210 – 220Combined sources11
Helixi222 – 232Combined sources11
Helixi234 – 236Combined sources3
Turni237 – 239Combined sources3
Beta strandi241 – 247Combined sources7
Beta strandi253 – 256Combined sources4
Helixi261 – 271Combined sources11
Helixi278 – 287Combined sources10
Helixi290 – 300Combined sources11
Beta strandi324 – 326Combined sources3
Helixi331 – 337Combined sources7
Beta strandi345 – 351Combined sources7
Helixi376 – 383Combined sources8
Helixi385 – 388Combined sources4
Turni392 – 394Combined sources3
Helixi395 – 402Combined sources8
Helixi416 – 424Combined sources9
Helixi426 – 437Combined sources12
Turni438 – 440Combined sources3
Beta strandi443 – 448Combined sources6
Helixi469 – 474Combined sources6
Turni475 – 479Combined sources5
Beta strandi480 – 482Combined sources3
Helixi486 – 505Combined sources20
Beta strandi525 – 531Combined sources7
Beta strandi533 – 535Combined sources3
Helixi540 – 552Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP12337.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi565Prevents secretion from ERSequence analysis1

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)DescriptionActionsGraphical viewLength
Sequence conflicti30H → K AA sequence (PubMed:3343253).Curated1
Sequence conflicti89Q → S AA sequence (PubMed:3343253).Curated1
Sequence conflicti175 – 198WGFFS…QVAAL → GGFGFNIDELFLVAVN AA sequence (PubMed:3343253).CuratedAdd BLAST24
Sequence conflicti335 – 336LA → YE AA sequence (PubMed:3343253).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K4YX-ray2.50A23-556[»]
ProteinModelPortaliP12337.
SMRiP12337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005826.

Chemistry databases

BindingDBiP12337.
ChEMBLiCHEMBL2623.

Protein family/group databases

ESTHERirabit-1cxes. Carb_B_Chordata.
MEROPSiS09.981.

Proteomic databases

PRIDEiP12337.

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: November 2, 2016
This is version 120 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.