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Entry version 115 (26 Feb 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Liver carboxylesterase

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Active towards triacylglycerides containing short-chain fatty acids from C2 to C6, and 13-monoacylglycerols containing fatty acids from C2 to C12. Inactive on long-chain triacylglycerols and diacylglycerol. Hydrolyzes aromatic and alkyl esters and vitamin A acetate. The hydrolysis rate depends upon the amino acid promoiety and the esterification site of the prodrug. Aromatic promoieties are favored, highest rates are observed with phenylalanyl progdrugs, hydrolysis of valyl and isoleucyl prodrugs is less efficient. With floxuridine prodrugs, activity is higher on 5' monoesters than on 3' monoesters. With gemcitabine prodrugs, activity is higher on 3' monoesters than on 5' monoesters.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by CHAPS at concentrations of up to 130 mM, higher concentrations reduce activity. In the presence of CHAPS, activity is stimulated by non-ionic detergents. Inhibited by the esterase inhibitors diisopropylfluorophosphate and phenylmethylsulfonyl fluoride.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=27.5 µM for retinyl palmitate3 Publications
  2. KM=0.46 mM for 5'-L-phenylalanyl-floxuridine3 Publications
  3. KM=0.44 mM for 5'-D-phenylalanyl-floxuridine3 Publications
  4. KM=1.40 mM for 3'-D-phenylalanyl-floxuridine3 Publications
  5. KM=0.74 mM for 3'-L-phenylalanyl-floxuridine3 Publications
  6. KM=1.87 mM for 5'-L-prolyl-floxuridine3 Publications
  7. KM=0.97 mM for 5'-L-leucyl-floxuridine3 Publications
  8. KM=4.85 mM for 3'-L-prolyl-floxuridine3 Publications
  9. KM=1.46 mM for 3'-L-leucyl-floxuridine3 Publications
  10. KM=3.08 mM for 3'-L-lysyl-floxuridine3 Publications
  11. KM=6.25 mM for 5'-L-lysyl-floxuridine3 Publications
  12. KM=1.11 mM for 3'-L-isoleucyl-floxuridine3 Publications
  13. KM=3.00 mM for 5'-L-aspartyl-floxuridine3 Publications
  14. KM=0.93 mM for 3'-L-aspartyl-floxuridine3 Publications
  15. KM=4.12 mM for 5'-D-valyl-floxuridine3 Publications
  16. KM=2.87 mM for 3'-L-valyl-floxuridine3 Publications
  17. KM=3.58 mM for 5'-L-valyl-floxuridine3 Publications
  18. KM=2.94 mM for 5'-L-isoleucyl-floxuridine3 Publications
  19. KM=11.23 mM for 3'-D-valyl-floxuridine3 Publications
  20. KM=0.51 mM for 3'-L-phenylalanyl-gemcitabine3 Publications
  21. KM=0.97 mM for 3'-D-phenylalanyl-gemcitabine3 Publications
  22. KM=0.17 mM for 5'-L-phenylalanyl-gemcitabine3 Publications
  23. KM=0.22 mM for 5'-D-phenylalanyl-gemcitabine3 Publications
  24. KM=0.90 mM for 3'-L-valyl-gemcitabine3 Publications
  25. KM=0.94 mM for 3'-L-isoleucyl-gemcitabine3 Publications
  26. KM=1.43 mM for 3'-D-valyl-gemcitabine3 Publications
  27. KM=0.85 mM for 5'-L-isoleucyl-gemcitabine3 Publications
  28. KM=1.16 mM for 5'-D-valyl-gemcitabine3 Publications
  29. KM=0.96 mM for 5'-L-valyl-gemcitabine3 Publications
  30. KM=0.91 mM for 5'-L-phenylalanyl-BDCRB3 Publications
  31. KM=0.90 mM for 5'-D-phenylalanyl-BDCRB3 Publications
  32. KM=0.14 mM for pNPB3 Publications
  33. KM=0.52 mM for pNPA3 Publications
  34. KM=1.18 mM for PHEE3 Publications
  35. KM=0.08 mM for PHBE3 Publications
  36. KM=0.40 mM for AcPHEE3 Publications
  37. KM=0.63 mM for 5' cinn-floxuridine3 Publications
  38. KM=4.21 mM for CPT-113 Publications
  39. KM=8.81 mM for VACV3 Publications
  1. Vmax=530 nmol/h/mg enzyme with retinyl palmitate as substrate3 Publications
  2. Vmax=1.82 nmol/min/µg enzyme with 5'-L-phenylalanyl-floxuridine as substrate3 Publications
  3. Vmax=1.63 nmol/min/µg enzyme with 5'-D-phenylalanyl-floxuridine as substrate3 Publications
  4. Vmax=4.05 nmol/min/µg enzyme with 3'-D-phenylalanyl-floxuridine as substrate3 Publications
  5. Vmax=1.55 nmol/min/µg enzyme with 3'-L-phenylalanyl-floxuridine as substrate3 Publications
  6. Vmax=1.97 nmol/min/µg enzyme with 5'-L-prolyl-floxuridine as substrate3 Publications
  7. Vmax=0.92 nmol/min/µg enzyme with 5'-L-leucyl-floxuridine as substrate3 Publications
  8. Vmax=4.53 nmol/min/µg enzyme with 3'-L-prolyl-floxuridine as substrate3 Publications
  9. Vmax=0.70 nmol/min/µg enzyme with 3'-L-leucyl-floxuridine as substrate3 Publications
  10. Vmax=0.59 nmol/min/µg enzyme with 3'-L-lysyl-floxuridine as substrate3 Publications
  11. Vmax=1.11 nmol/min/µg enzyme with 5'-L-lysyl-floxuridine as substrate3 Publications
  12. Vmax=0.16 nmol/min/µg enzyme with 3'-L-isoleucyl-floxuridine as substrate3 Publications
  13. Vmax=0.33 nmol/min/µg enzyme with 5'-L-aspartyl-floxuridine as substrate3 Publications
  14. Vmax=0.10 nmol/min/µg enzyme with 3'-L-aspartyl-floxuridine as substrate3 Publications
  15. Vmax=0.30 nmol/min/µg enzyme with 5'-D-valyl-floxuridine as substrate3 Publications
  16. Vmax=0.19 nmol/min/µg enzyme with 3'-L-valyl-floxuridine as substrate3 Publications
  17. Vmax=0.21 nmol/min/µg enzyme with 5'-L-valyl-floxuridine as substrate3 Publications
  18. Vmax=0.15 nmol/min/µg enzyme with 5'-L-isoleucyl-floxuridine as substrate3 Publications
  19. Vmax=0.27 nmol/min/µg enzyme with 3'-D-valyl-floxuridine as substrate3 Publications
  20. Vmax=283.52 nmol/min/µg enzyme with 3'-L-phenylalanyl-gemcitabine as substrate3 Publications
  21. Vmax=406.92 nmol/min/µg enzyme with 3'-D-phenylalanyl-gemcitabine as substrate3 Publications
  22. Vmax=3.25 nmol/min/µg enzyme with 5'-L-phenylalanyl-gemcitabine as substrate3 Publications
  23. Vmax=3.19 nmol/min/µg enzyme with 5'-D-phenylalanyl-gemcitabine as substrate3 Publications
  24. Vmax=0.35 nmol/min/µg enzyme with 3'-L-valyl-gemcitabine as substrate3 Publications
  25. Vmax=0.24 nmol/min/µg enzyme with 3'-L-isoleucyl-gemcitabine as substrate3 Publications
  26. Vmax=0.32 nmol/min/µg enzyme with 3'-D-valyl-gemcitabine as substrate3 Publications
  27. Vmax=0.09 nmol/min/µg enzyme with 5'-L-isoleucyl-gemcitabine as substrate3 Publications
  28. Vmax=0.13 nmol/min/µg enzyme with 5'-D-valyl-gemcitabine as substrate3 Publications
  29. Vmax=0.12 nmol/min/µg enzyme with 5'-L-valyl-gemcitabine as substrate3 Publications
  30. Vmax=2.33 nmol/min/µg enzyme with 5'-L-phenylalanyl-BDCRB as substrate3 Publications
  31. Vmax=1.60 nmol/min/µg enzyme with 5'-D-phenylalanyl-BDCRB as substrate3 Publications
  32. Vmax=82.25 nmol/min/µg enzyme with pNPB as substrate3 Publications
  33. Vmax=60.45 nmol/min/µg enzyme with pNPA as substrate3 Publications
  34. Vmax=11859.78 nmol/min/µg enzyme with PHEE as substrate3 Publications
  35. Vmax=7.24 nmol/min/µg enzyme with PHBE as substrate3 Publications
  36. Vmax=1.29 nmol/min/µg enzyme with AcPHEE as substrate3 Publications
  37. Vmax=4.00 nmol/min/µg enzyme with 5' cinn-floxuridine as substrate3 Publications
  38. Vmax=0.03 nmol/min/µg enzyme with CPT-11 as substrate3 Publications

pH dependencei

Optimum pH is 8.0 with tributylglycerol as substrate, and 8.2 with retinyl palmitate as substrate. Active from pH 4.5-9.5 with retinyl palmitate as substrate.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei222Acyl-ester intermediatePROSITE-ProRule annotation1
Active sitei354Charge relay systemBy similarity1
Active sitei467Charge relay systemBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q29550

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
pig-EST1 Carb_B_Chordata

MEROPS protease database

More...
MEROPSi
S09.981

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Liver carboxylesterase (EC:3.1.1.1)
Alternative name(s):
Proline-beta-naphthylamidase
Retinyl ester hydrolase
Short name:
REH
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008227 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3383

DrugCentral

More...
DrugCentrali
Q29550

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18By similarityAdd BLAST18
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000857719 – 566Liver carboxylesteraseAdd BLAST548

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi80N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi88 ↔ 117By similarity
Disulfide bondi274 ↔ 285By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei379PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q29550

PeptideAtlas

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PeptideAtlasi
Q29550

PRoteomics IDEntifications database

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PRIDEi
Q29550

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

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STRINGi
9823.ENSSSCP00000003045

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q29550

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q29550

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi563 – 566Prevents secretion from ERSequence analysis4

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1516 Eukaryota
COG2272 LUCA

Database of Orthologous Groups

More...
OrthoDBi
754103at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029058 AB_hydrolase
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00135 COesterase, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53474 SSF53474, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q29550-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWLLPLVLTS LASSATWAGQ PASPPVVDTA QGRVLGKYVS LEGLAQPVAV
60 70 80 90 100
FLGVPFAKPP LGSLRFAPPQ PAEPWSFVKN TTSYPPMCCQ DPVVEQMTSD
110 120 130 140 150
LFTNGKERLT LEFSEDCLYL NIYTPADLTK RGRLPVMVWI HGGGLVLGGA
160 170 180 190 200
PMYDGVVLAA HENVVVVAIQ YRLGIWGFFS TGDEHSRGNW GHLDQVAALH
210 220 230 240 250
WVQENIANFG GDPGSVTIFG ESAGGESVSV LVLSPLAKNL FHRAISESGV
260 270 280 290 300
ALTVALVRKD MKAAAKQIAV LAGCKTTTSA VFVHCLRQKS EDELLDLTLK
310 320 330 340 350
MKFLTLDFHG DQRESHPFLP TVVDGVLLPK MPEEILAEKD FNTVPYIVGI
360 370 380 390 400
NKQEFGWLLP TMMGFPLSEG KLDQKTATSL LWKSYPIANI PEELTPVATD
410 420 430 440 450
KYLGGTDDPV KKKDLFLDLM GDVVFGVPSV TVARQHRDAG APTYMYEFQY
460 470 480 490 500
RPSFSSDKKP KTVIGDHGDE IFSVFGFPLL KGDAPEEEVS LSKTVMKFWA
510 520 530 540 550
NFARSGNPNG EGLPHWPMYD QEEGYLQIGV NTQAAKRLKG EEVAFWNDLL
560
SKEAAKKPPK IKHAEL
Length:566
Mass (Da):62,016
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBE046545307DEDE5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti18Missing in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti25P → D AA sequence (PubMed:9490062).Curated1
Sequence conflicti94 – 95VE → AG in AAC70013 (PubMed:9799112).Curated2
Sequence conflicti110 – 111TL → IP in AAC70013 (PubMed:9799112).Curated2
Sequence conflicti130K → R in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti147L → V in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti151 – 152PM → ST in AAC70013 (PubMed:9799112).Curated2
Sequence conflicti156 – 157VV → LA in AAC70013 (PubMed:9799112).Curated2
Sequence conflicti213P → T in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti254 – 255VA → AG in AAC70013 (PubMed:9799112).Curated2
Sequence conflicti308F → L in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti312Q → P in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti320 – 321PT → AF AA sequence (PubMed:9490062).Curated2
Sequence conflicti323V → N AA sequence (PubMed:9490062).Curated1
Sequence conflicti384S → R AA sequence (PubMed:9490062).Curated1
Sequence conflicti385Y → F in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti388A → T in AAC70013 (PubMed:9799112).Curated1
Sequence conflicti399T → A AA sequence (PubMed:9490062).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X63323 mRNA Translation: CAA44929.1
AF064741 mRNA Translation: AAC70013.1

Protein sequence database of the Protein Information Resource

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PIRi
S19307

NCBI Reference Sequences

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RefSeqi
NP_001302695.1, NM_001315766.1
XP_013850047.1, XM_013994593.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
100736962

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:100736962

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63323 mRNA Translation: CAA44929.1
AF064741 mRNA Translation: AAC70013.1
PIRiS19307
RefSeqiNP_001302695.1, NM_001315766.1
XP_013850047.1, XM_013994593.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FV4X-ray2.40A/B/C/D/E/F19-562[»]
SMRiQ29550
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003045

Chemistry databases

BindingDBiQ29550
ChEMBLiCHEMBL3383
DrugCentraliQ29550

Protein family/group databases

ESTHERipig-EST1 Carb_B_Chordata
MEROPSiS09.981

Proteomic databases

PaxDbiQ29550
PeptideAtlasiQ29550
PRIDEiQ29550

Genome annotation databases

GeneIDi100736962
KEGGissc:100736962

Phylogenomic databases

eggNOGiKOG1516 Eukaryota
COG2272 LUCA
OrthoDBi754103at2759

Enzyme and pathway databases

SABIO-RKiQ29550

Miscellaneous databases

Protein Ontology

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PROi
PR:Q29550

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS
PfamiView protein in Pfam
PF00135 COesterase, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEST1_PIG
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q29550
Secondary accession number(s): O97582, P82128
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 26, 2020
This is version 115 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
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