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Entry version 159 (02 Jun 2021)
Sequence version 1 (01 Jun 2001)
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Protein

Acyl-coenzyme A thioesterase 8

Gene

Acot8

Organism
Mus musculus (Mouse)
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

Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:11673457).

Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (PubMed:11673457).

Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:11673457).

Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (PubMed:11673457).

ACOT8 is also able to hydrolyze CoA esters of dicarboxylic acids (PubMed:16141203).

It is involved in the metabolic regulation of peroxisome proliferation (By similarity).

By similarity2 Publications

Miscellaneous

Constitutes about 1% of total peroxisomal protein.

<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

Inhibited by CoASH (IC50=10-15 µM). Also inhibited by cysteine-reactive agents.1 Publication

<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

In summary, KM for medium- to long-chain acyl CoAs is in the order 1.4-6.7 µM, and with short-chain acyl CoAs range from 8 to 30 µM. KM for bile acid-CoA esters is in the range 6-15 µM.1 Publication
  1. KM=29.4 µM for acetyl-CoA1 Publication
  2. KM=8.0 µM for propionyl-CoA1 Publication
  3. KM=22.6 µM for butyryl-CoA1 Publication
  4. KM=23.4 µM for hexanoyl-CoA1 Publication
  5. KM=6.9 µM for octanoyl-CoA1 Publication
  6. KM=2.9 µM for decanoyl-CoA1 Publication
  7. KM=2.8 µM for lauroyl-CoA1 Publication
  8. KM=2.5 µM for myristoyl-CoA1 Publication
  9. KM=3.5 µM for myristoleoyl-CoA1 Publication
  10. KM=1.7 µM for palmitoyl-CoA1 Publication
  11. KM=1.4 µM for palmitoleoyl-CoA1 Publication
  12. KM=2.7 µM for stearoyl-CoA1 Publication
  13. KM=1.6 µM for oleoyl-CoA1 Publication
  14. KM=2.3 µM for linoleoyl-CoA1 Publication
  15. KM=4.2 µM for arachidoyl-CoA1 Publication
  16. KM=6.7 µM for arachidonoyl-CoA1 Publication
  17. KM=6.3 µM for 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA1 Publication
  18. KM=14.6 µM for choloyl-CoA1 Publication
  19. KM=8.8 µM for chenodeoxycholoyl-CoA1 Publication
  20. KM=5.5 µM for 4,8-dimethylnonanoyl-CoA1 Publication
  21. KM=0.92 µM for prostaglandin F2alpha-CoA1 Publication
  22. KM=1.9 µM for 2-methyloctadecanoyl-CoA1 Publication
  23. KM=22.9 µM for (3S)-hydroxy-3-methylglutaryl-CoA1 Publication
  24. KM=12.9 µM for malonyl-CoA1 Publication
  25. KM=22.9 µM for acetoacetyl-CoA1 Publication
  26. KM=34.7 µM for succinyl-CoA1 Publication
  27. KM=15.9 µM for glutaryl-CoA1 Publication
  28. KM=21.8 µM for hexanedioyl-CoA1 Publication
  29. KM=19.8 µM for octanoyl-CoA1 Publication
  30. KM=10.5 µM for decanedioyl-CoA1 Publication
  31. KM=14.1 µM for dodecanedioyl-CoA1 Publication
  1. Vmax=4.6 µmol/min/mg enzyme with acetyl-CoA as substrate1 Publication
  2. Vmax=3.45 µmol/min/mg enzyme with propionyl-CoA as substrate1 Publication
  3. Vmax=2.6 µmol/min/mg enzyme with butyryl-CoA as substrate1 Publication
  4. Vmax=5.6 µmol/min/mg enzyme with hexanoyl-CoA as substrate1 Publication
  5. Vmax=3.9 µmol/min/mg enzyme with octanoyl-CoA as substrate1 Publication
  6. Vmax=3.8 µmol/min/mg enzyme with decanoyl-CoA as substrate1 Publication
  7. Vmax=3.0 µmol/min/mg enzyme with lauroyl-CoA as substrate1 Publication
  8. Vmax=3.6 µmol/min/mg enzyme with myristoyl-CoA as substrate1 Publication
  9. Vmax=3.2 µmol/min/mg enzyme with myristoleoyl-CoA as substrate1 Publication
  10. Vmax=1.7 µmol/min/mg enzyme with palmitoyl-CoA as substrate1 Publication
  11. Vmax=2.7 µmol/min/mg enzyme with palmitoleoyl-CoA as substrate1 Publication
  12. Vmax=3.2 µmol/min/mg enzyme with stearoyl-CoA as substrate1 Publication
  13. Vmax=3.1 µmol/min/mg enzyme with oleoyl-CoA as substrate1 Publication
  14. Vmax=2.3 µmol/min/mg enzyme with linoleoyl-CoA as substrate1 Publication
  15. Vmax=2.2 µmol/min/mg enzyme with arachidoyl-CoA as substrate1 Publication
  16. Vmax=1.6 µmol/min/mg enzyme with arachidonoyl-CoA as substrate1 Publication
  17. Vmax=8.1 µmol/min/mg enzyme with 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA as substrate1 Publication
  18. Vmax=17.9 µmol/min/mg enzyme with choloyl-CoA as substrate1 Publication
  19. Vmax=17.1 µmol/min/mg enzyme with chenodeoxycholoyl-CoA as substrate1 Publication
  20. Vmax=10.69 µmol/min/mg enzyme with 4,8-dimethylnonanoyl-CoA as substrate1 Publication
  21. Vmax=2.25 µmol/min/mg enzyme with prostaglandin F2alpha-CoA as substrate1 Publication
  22. Vmax=1.65 µmol/min/mg enzyme with 2-methyloctadecanoyl-CoA as substrate1 Publication
  23. Vmax=2.85 µmol/min/mg enzyme with (3S)-hydroxy-3-methylglutaryl-CoA as substrate1 Publication
  24. Vmax=1.19 µmol/min/mg enzyme with malonyl-CoA as substrate1 Publication
  25. Vmax=6.0 µmol/min/mg enzyme with acetoacetyl-CoA as substrate1 Publication
  26. Vmax=0.82 µmol/min/mg enzyme with succinyl-CoA as substrate1 Publication
  27. Vmax=2.35 µmol/min/mg enzyme with glutaryl-CoA as substrate1 Publication
  28. Vmax=3.4 µmol/min/mg enzyme with hexanedioyl-CoA as substrate1 Publication
  29. Vmax=4.13 µmol/min/mg enzyme with octanoyl-CoA as substrate1 Publication
  30. Vmax=3.82 µmol/min/mg enzyme with decanedioyl-CoA as substrate1 Publication
  31. Vmax=5.03 µmol/min/mg enzyme with dodecanedioyl-CoA as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

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 sitei233Charge relay systemBy similarity1
Active sitei255Charge relay systemBy similarity1
Active sitei305Charge 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
Biological processFatty acid metabolism, Lipid metabolism, Peroxisome biogenesis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.2.2, 3474
3.1.2.20, 3474
3.1.2.27, 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-193368, Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-MMU-2046106, alpha-linolenic acid (ALA) metabolism
R-MMU-389887, Beta-oxidation of pristanoyl-CoA
R-MMU-390247, Beta-oxidation of very long chain fatty acids
R-MMU-9033241, Peroxisomal protein import

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00199

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000534

<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:
Acyl-coenzyme A thioesterase 8 (EC:3.1.2.11 Publication, EC:3.1.2.111 Publication, EC:3.1.2.21 Publication, EC:3.1.2.31 Publication, EC:3.1.2.51 Publication)
Short name:
Acyl-CoA thioesterase 8
Alternative name(s):
Choloyl-coenzyme A thioesterase (EC:3.1.2.271 Publication)
Peroxisomal acyl-CoA thioesterase 21 Publication
Short name:
PTE-21 Publication
Peroxisomal acyl-coenzyme A thioester hydrolase 1
Short name:
PTE-1
Peroxisomal long-chain acyl-CoA thioesterase 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Acot8
Synonyms:Pte1
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Chromosome 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:2158201, Acot8

<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

Keywords - Cellular componenti

Peroxisome

<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 describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002021531 – 320Acyl-coenzyme A thioesterase 8Add BLAST320

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P58137

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P58137

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

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PaxDbi
P58137

PeptideAtlas

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PeptideAtlasi
P58137

PRoteomics IDEntifications database

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PRIDEi
P58137

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
285654

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P58137

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P58137

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced in the liver, by peroxisome proliferator or fasting via the peroxisome proliferator-activated receptors (PPARs). Diurnal regulation of its expression.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000017307, Expressed in spermatid and 303 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P58137, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P58137, MM

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
228440, 14 interactors

Protein interaction database and analysis system

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IntActi
P58137, 1 interactor

Molecular INTeraction database

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MINTi
P58137

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000099383

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P58137, protein

<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

3D structure databases

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

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SMRi
P58137

Database of comparative protein structure models

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ModBasei
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>Motifi318 – 320Microbody targeting signalSequence analysis3

<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

Belongs to the C/M/P thioester hydrolase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3016, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000004207

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_032690_1_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P58137

Identification of Orthologs from Complete Genome Data

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OMAi
HAMWWHR

Database of Orthologous Groups

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OrthoDBi
826588at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P58137

TreeFam database of animal gene trees

More...
TreeFami
TF315124

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.129.90, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR042171, Acyl-CoA_hotdog
IPR003703, Acyl_CoA_thio
IPR029069, HotDog_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11066, PTHR11066, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54637, SSF54637, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00189, tesB, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P58137-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAPEGLGDA HGDADRGDLS GDLRSVLVTS VLNLEPLDED LYRGRHYWVP
60 70 80 90 100
TSQRLFGGQI MGQALVAAAK SVSEDVHVHS LHCYFVRAGD PKVPVLYHVE
110 120 130 140 150
RIRTGASFSV RAVKAVQHGK AIFICQASFQ QMQPSPLQHQ FSMPSVPPPE
160 170 180 190 200
DLLDHEALID QYLRDPNLHK KYRVGLNRVA AQEVPIEIKV VNPPTLTQLQ
210 220 230 240 250
ALEPKQMFWV RARGYIGEGD IKMHCCVAAY ISDYAFLGTA LLPHQSKYKV
260 270 280 290 300
NFMASLDHSM WFHAPFRADH WMLYECESPW AGGSRGLVHG RLWRRDGVLA
310 320
VTCAQEGVIR LKPQVSESKL
Length:320
Mass (Da):35,827
Last modified:June 1, 2001 - 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:i94F6AFCFEEE2FA23
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q8BZR4Q8BZR4_MOUSE
Acyl-coenzyme A thioesterase 8
Acot8 Pte1
268Annotation score:

Annotation score:1 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>
G3UXJ8G3UXJ8_MOUSE
Acyl-coenzyme A thioesterase 8
Acot8
113Annotation score:

Annotation score:1 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 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 conflicti284S → F in AAL35333 (PubMed:11673457).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
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
AF441166 mRNA Translation: AAL35333.1
BC005792 mRNA Translation: AAH05792.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS17057.1

NCBI Reference Sequences

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RefSeqi
NP_573503.2, NM_133240.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000103094; ENSMUSP00000099383; ENSMUSG00000017307

Database of genes from NCBI RefSeq genomes

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GeneIDi
170789

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:170789

UCSC genome browser

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UCSCi
uc008nwf.2, mouse

<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
AF441166 mRNA Translation: AAL35333.1
BC005792 mRNA Translation: AAH05792.1
CCDSiCCDS17057.1
RefSeqiNP_573503.2, NM_133240.2

3D structure databases

SMRiP58137
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi228440, 14 interactors
IntActiP58137, 1 interactor
MINTiP58137
STRINGi10090.ENSMUSP00000099383

Chemistry databases

SwissLipidsiSLP:000000534

PTM databases

iPTMnetiP58137
PhosphoSitePlusiP58137

Proteomic databases

EPDiP58137
jPOSTiP58137
PaxDbiP58137
PeptideAtlasiP58137
PRIDEiP58137
ProteomicsDBi285654

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
4138, 242 antibodies

The DNASU plasmid repository

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DNASUi
170789

Genome annotation databases

EnsembliENSMUST00000103094; ENSMUSP00000099383; ENSMUSG00000017307
GeneIDi170789
KEGGimmu:170789
UCSCiuc008nwf.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
10005
MGIiMGI:2158201, Acot8

Phylogenomic databases

eggNOGiKOG3016, Eukaryota
GeneTreeiENSGT00390000004207
HOGENOMiCLU_032690_1_0_1
InParanoidiP58137
OMAiHAMWWHR
OrthoDBi826588at2759
PhylomeDBiP58137
TreeFamiTF315124

Enzyme and pathway databases

UniPathwayiUPA00199
BRENDAi3.1.2.2, 3474
3.1.2.20, 3474
3.1.2.27, 3474
ReactomeiR-MMU-193368, Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-MMU-2046106, alpha-linolenic acid (ALA) metabolism
R-MMU-389887, Beta-oxidation of pristanoyl-CoA
R-MMU-390247, Beta-oxidation of very long chain fatty acids
R-MMU-9033241, Peroxisomal protein import

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
170789, 0 hits in 53 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Acot8, mouse

Protein Ontology

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PROi
PR:P58137
RNActiP58137, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000017307, Expressed in spermatid and 303 other tissues
ExpressionAtlasiP58137, baseline and differential
GenevisibleiP58137, MM

Family and domain databases

Gene3Di3.10.129.90, 1 hit
InterProiView protein in InterPro
IPR042171, Acyl-CoA_hotdog
IPR003703, Acyl_CoA_thio
IPR029069, HotDog_dom_sf
PANTHERiPTHR11066, PTHR11066, 1 hit
SUPFAMiSSF54637, SSF54637, 2 hits
TIGRFAMsiTIGR00189, tesB, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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 nameiACOT8_MOUSE
<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: P58137
Secondary accession number(s): Q8VHM4
<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: June 1, 2001
Last sequence update: June 1, 2001
Last modified: June 2, 2021
This is version 159 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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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