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Entry version 71 (16 Jan 2019)
Sequence version 1 (05 Apr 2011)
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Protein

Acetyl-CoA carboxylase 2

Gene

Acacb

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

Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (By similarity). Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (By similarity). Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (PubMed:11283375, PubMed:12920182, PubMed:15677334, PubMed:18487439, PubMed:22362781). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA-dependent inhibition of carnitine palmitoyltransferase 1 (PubMed:10677481).1 PublicationBy similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ 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

Activity is increased by oligomerization. Activated by citrate. Citrate and MID1IP1 promote oligomerization. Inhibited by malonyl-CoA.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-CoA carboxylase 1 (Acaca), Acetyl-CoA carboxylase 2 (Acacb)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi557Manganese 1PROSITE-ProRule annotation1
Metal bindingi570Manganese 1PROSITE-ProRule annotation1
Metal bindingi570Manganese 2PROSITE-ProRule annotation1
Metal bindingi572Manganese 2PROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 sitei574By similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1924Coenzyme ABy similarity1
Binding sitei2228Coenzyme ABy similarity1
Binding sitei2230Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi434 – 491ATPPROSITE-ProRule annotationAdd BLAST58

<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 functionAllosteric enzyme, Ligase, Multifunctional enzyme
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.4.1.2 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-163765 ChREBP activates metabolic gene expression
R-MMU-196780 Biotin transport and metabolism
R-MMU-200425 Import of palmitoyl-CoA into the mitochondrial matrix

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

More...
UniPathwayi
UPA00655;UER00711

<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_and_taxonomy_section">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:
Acetyl-CoA carboxylase 2By similarity (EC:6.4.1.2By similarity)
Alternative name(s):
ACC-betaBy similarity
Including the following 1 domains:
Biotin carboxylaseBy similarity (EC:6.3.4.14)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:AcacbImported
Synonyms:Acc21 Publication, AccbImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 5

Organism-specific databases

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

More...
MGIi
MGI:2140940 Acacb

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Normal morphology, fertility, growth rate and lifespan but higher than normal food consumption and fatty acid oxidation rate and decreased fat content in adipose tissue and liver (PubMed:11283375). A high-fat/high-carbohydrate diet results in maintenance of normal insulin and glucose levels with less weight gain and less fat accumulation than wild-type mice (PubMed:12920182). Elevated levels of Ucp2 in adipose tissue and heart but not in skeletal muscle or liver, and elevated levels of Ucp3 in skeletal muscle but not in heart or brown adipose tissue (PubMed:12920182). Significant decrease in body weight, weight of epidydimal fat pads and levels of hepatic triglycerides under a range of dietary conditions including normal chow diet, fasting and refeeding a fat-free high-carbohydrate diet, and a high-fat/high-carbohydrate diet (PubMed:22362781). Up-regulation of lipogenic enzymes under de novo lipogenic conditions but reduced fat accumulation in liver (PubMed:22362781). Primary cultured adipocytes show increased fatty acid and glucose oxidation rates and increased lipolysis (PubMed:15677334). Reduced heart size, reduced Mlycd and malonyl-CoA levels in mutant hearts, reduced myocardial triglyceride levels, higher myocardial oleate and glucose oxidation rates, reduced levels of Ppara and reduced activation of Mtor (PubMed:18487439, PubMed:22730442). However, it has also been reported that mutants show no differences in body weight, food intake, body composition or glucose homeostasis as compared with controls fed on chow or a high-fat diet (PubMed:20368432).7 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi212S → A: No phosphorylation by AMPK, reduced fatty acid oxidation in skeletal muscle, increased lipid deposition in skeletal muscle, and development of insulin resistance. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3108631

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000430774? – 2448Acetyl-CoA carboxylase 21 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – ?Mitochondrion1 Publication

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei35PhosphoserineBy similarity1
Modified residuei47PhosphoserineCombined sources1
Modified residuei81PhosphoserineBy similarity1
Modified residuei85PhosphoserineBy similarity1
Modified residuei159PhosphoserineBy similarity1
Modified residuei165PhosphoserineBy similarity1
Modified residuei170PhosphoserineBy similarity1
Modified residuei182PhosphoserineBy similarity1
Modified residuei185PhosphoserineBy similarity1
Modified residuei190PhosphoserineBy similarity1
Modified residuei197PhosphothreonineCombined sources1
Modified residuei210PhosphoserineBy similarity1
Modified residuei212Phosphoserine; by AMPK1 Publication1
Modified residuei459PhosphoserineCombined sources1
Modified residuei743PhosphothreonineBy similarity1
Modified residuei919N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei1330PhosphoserineCombined sources1
Modified residuei1332PhosphoserineCombined sources1
Modified residuei1350PhosphoserineCombined sources1
Modified residuei1395PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by AMPK, leading to inactivation of the enzyme. Required for the maintenance of skeletal muscle lipid and glucose homeostasis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
E9Q4Z2

MaxQB - The MaxQuant DataBase

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MaxQBi
E9Q4Z2

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

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PaxDbi
E9Q4Z2

PeptideAtlas

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PeptideAtlasi
E9Q4Z2

PRoteomics IDEntifications database

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PRIDEi
E9Q4Z2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
E9Q4Z2

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

More...
PhosphoSitePlusi
E9Q4Z2

SwissPalm database of S-palmitoylation events

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SwissPalmi
E9Q4Z2

<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 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

Up-regulated by endocannabinoid anandamide/AEA.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000042010 Expressed in 128 organ(s), highest expression level in brown adipose tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
E9Q4Z2 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
E9Q4Z2 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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
221514, 1 interactor

Protein interaction database and analysis system

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IntActi
E9Q4Z2, 1 interactor

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000031583

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
E9Q4Z2

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
E9Q4Z2

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

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SMRi
E9Q4Z2

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini249 – 751Biotin carboxylationSequence analysisAdd BLAST503
Domaini408 – 599ATP-graspPROSITE-ProRule annotationAdd BLAST192
Domaini878 – 952Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1685 – 2015CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST331
Domaini2019 – 2335CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST317

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1685 – 2335CarboxyltransferasePROSITE-ProRule annotationAdd BLAST651

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0368 Eukaryota
COG0439 LUCA
COG0511 LUCA
COG4799 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155049

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000214115

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005371

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
E9Q4Z2

KEGG Orthology (KO)

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KOi
K01946

Identification of Orthologs from Complete Genome Data

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OMAi
YLQVEHH

Database of Orthologous Groups

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OrthoDBi
156081at2759

TreeFam database of animal gene trees

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TreeFami
TF300061

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.1490.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif

Pfam protein domain database

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Pfami
View protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00878 Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

E9Q4Z2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLLLFLTCL VFSCLTFSWL KIWGKMTDSK PLTNSKVEAN LLSSEESLSA
60 70 80 90 100
SELSGEQLQE HGDHSCLSYR GPRDASQQRN SLPSSCQRPP RNPLSSNDTW
110 120 130 140 150
PSPELQTNWT AAPGPEVPDA NGLSFPARPP SQRTVSPSRE DRKQAHIKRQ
160 170 180 190 200
LMTSFILGSL DDNSSDEDPS AGSFQNSSRK SSRASLGTLS QEAALNTSDP
210 220 230 240 250
ESHAPTMRPS MSGLHLVKRG REHKKLDLHR DFTVASPAEF VTRFGGNRVI
260 270 280 290 300
EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT PEDLKANAEY
310 320 330 340 350
IKMADQYVPV PGGPNNNNYA NVELIIDIAK RIPVQAVWAG WGHASENPKL
360 370 380 390 400
PELLCKHEIA FLGPPSEAMW ALGDKIASTI VAQTLQIPTL PWSGSGLTVE
410 420 430 440 450
WTEDSRHQGK CISVPEDVYE QGCVKDVDEG LQAAEKIGFP LMIKASEGGG
460 470 480 490 500
GKGIRKAESA EDFPMLFRQV QSEIPGSPIF LMKLAQNARH LEVQVLADQY
510 520 530 540 550
GNAVSLFGRD CSIQRRHQKI IEEAPATIAA PAVFEFMEQC AVLLAKMVGY
560 570 580 590 600
VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL PAAQLQIAMG
610 620 630 640 650
VPLHRLKDIR LLYGESPWGV TPIPFETPLS PPIARGHVIA ARITSENPDE
660 670 680 690 700
GFKPSSGTVQ ELNFRSNKNV WGYFSVAAAG GLHEFADSQF GHCFSWGENR
710 720 730 740 750
EEAISNMVVA LKELSIRGDF RTTVEYLVNL LETESFQNND IDTGWLDHLI
760 770 780 790 800
AQRVQAEKPD IMLGVVCGAL NVADAMFRTC MTEFLHSLER GQVLPADSLL
810 820 830 840 850
NIVDVELIYG GIKYALKVAR QSLTMFVLIM NGCHIEIDAH RLNDGGLLLS
860 870 880 890 900
YNGSSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP SAGKLMQYTV
910 920 930 940 950
EDGDHVEAGS SYAEMEVMKM IMTLNVQESG RVKYIKRPGV ILEAGCVVAR
960 970 980 990 1000
LELDDPSKVH AAQPFTGELP AQQTLPILGE KLHQVFHGVL ENLTNVMSGY
1010 1020 1030 1040 1050
CLPEPFFSMK LKDWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKA
1060 1070 1080 1090 1100
VRRVMAQYAS NITSVLCQFP SQQIATILDC HAATLQRKAD REVFFMNTQS
1110 1120 1130 1140 1150
IVQLVQRYRS GTRGYMKAVV LDLLRKYLNV EHHFQQAHYD KCVINLREQF
1160 1170 1180 1190 1200
KPDMTQVLDC IFSHSQVAKK NQLVTMLIDE LCGPDPTLSD ELTSILCELT
1210 1220 1230 1240 1250
QLSRSEHCKV ALRARQVLIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
1260 1270 1280 1290 1300
ENLKKLILSE TTIFDVLPTF FYHENKVVCM ASLEVYVRRG YIAYELNSLQ
1310 1320 1330 1340 1350
HRELPDGTCV VEFQFMLPSS HPNRMAVPIS VSNPDLLRHS TELFMDSGFS
1360 1370 1380 1390 1400
PLCQRMGAMV AFRRFEEFTR NFDEVISCFA NVQTDTLLFS KACTSLYSEE
1410 1420 1430 1440 1450
DSKSLREEPI HILNVAIQCA DHMEDEALVP VFRAFVQSKK HILVDYGLRR
1460 1470 1480 1490 1500
ITFLVAQERE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL ELSRMRNFDL
1510 1520 1530 1540 1550
TAVPCANHKM HLYLGAAKVK EGLEVTDHRF FIRAIIRHSD LITKEASFEY
1560 1570 1580 1590 1600
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPLKIEES
1610 1620 1630 1640 1650
VRDMVMRYGS RLWKLRVLQA EVKINIRQTT SDSAIPIRLF ITNESGYYLD
1660 1670 1680 1690 1700
ISLYREVTDS RSGNIMFHSF GNKQGSLHGM LINTPYVTKD LLQAKRFQAQ
1710 1720 1730 1740 1750
SLGTTYVYDF PEMFRQALFK LWGSPEKYPK DILTYTELVL DSQGQLVEMN
1760 1770 1780 1790 1800
RLPGCNEVGM VAFKMRFKTP EYPEGRDAVV IGNDITFQIG SFGIGEDFLY
1810 1820 1830 1840 1850
LRASEMARTE GIPQIYLAAN SGARMGLAEE IKQIFQVAWV DPEDPHKGFR
1860 1870 1880 1890 1900
YLYLTPQDYT QISSQNSVHC KHIEDEGESR YVIVDVIGKD ANLGVENLRG
1910 1920 1930 1940 1950
SGMIAGEASL AYEKTVTISM VTCRALGIGA YLVRLGQRVI QVENSHIILT
1960 1970 1980 1990 2000
GAGALNKVLG REVYTSNNQL GGVQIMHTNG VSHVTVPDDF EGVCTILEWL
2010 2020 2030 2040 2050
SFIPKDNRSP VPITTPSDPI DREIEFTPTK APYDPRWMLA GRPHPTLKGT
2060 2070 2080 2090 2100
WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE TRTVEVAVPA
2110 2120 2130 2140 2150
DPANLDSEAK IIQQAGQVWF PDSAYKTAQV IRDFNKERLP LMIFANWRGF
2160 2170 2180 2190 2200
SGGMKDMYEQ MLKFGAYIVD GLRLYEQPIL IYIPPCAELR GGSWVVLDST
2210 2220 2230 2240 2250
INPLCIEMYA DKESRGGVLE PEGTVEIKFR KKDLVKTIRR IDPVCKKLVG
2260 2270 2280 2290 2300
QLGKAQLPDK DRKELEGQLK AREELLLPIY HQVAVQFADL HDTPGHMLEK
2310 2320 2330 2340 2350
GIISDVLEWK TARTFFYWRL RRLLLEAQVK QEILRASPEL NHEHTQSMLR
2360 2370 2380 2390 2400
RWFVETEGAV KAYLWDSNQV VVQWLEQHWS AKDGLRSTIR ENINYLKRDS
2410 2420 2430 2440
VLKTIQSLVQ EHPEVIMDCV AYLSQHLTPA ERIQVAQLLS TTESPASS
Length:2,448
Mass (Da):275,750
Last modified:April 5, 2011 - 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:i6CD686C7AF012A5E
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3Z0B3D3Z0B3_MOUSE
Acetyl-CoA carboxylase 2
Acacb
146Annotation 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 conflicti124S → P in AAS13686 (Ref. 1) Curated1
Sequence conflicti534F → S in AAS13686 (Ref. 1) Curated1
Sequence conflicti562Q → R in AAS13686 (Ref. 1) Curated1
Sequence conflicti1315F → S in AAS13686 (Ref. 1) Curated1
Sequence conflicti1402S → N in AAS13686 (Ref. 1) Curated1
Sequence conflicti2341N → S in AAS13686 (Ref. 1) 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

More...
DDBJi
Links Updated
AY451394 mRNA Translation: AAS13686.1
AC122282 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

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CCDSi
CCDS19561.1

NCBI Reference Sequences

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RefSeqi
NP_598665.2, NM_133904.2
XP_006530176.1, XM_006530113.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.81793

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000031583; ENSMUSP00000031583; ENSMUSG00000042010
ENSMUST00000102582; ENSMUSP00000099642; ENSMUSG00000042010

Database of genes from NCBI RefSeq genomes

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GeneIDi
100705

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:100705

UCSC genome browser

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UCSCi
uc008yzi.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
AY451394 mRNA Translation: AAS13686.1
AC122282 Genomic DNA No translation available.
CCDSiCCDS19561.1
RefSeqiNP_598665.2, NM_133904.2
XP_006530176.1, XM_006530113.3
UniGeneiMm.81793

3D structure databases

ProteinModelPortaliE9Q4Z2
SMRiE9Q4Z2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221514, 1 interactor
IntActiE9Q4Z2, 1 interactor
STRINGi10090.ENSMUSP00000031583

Chemistry databases

BindingDBiE9Q4Z2
ChEMBLiCHEMBL3108631

PTM databases

iPTMnetiE9Q4Z2
PhosphoSitePlusiE9Q4Z2
SwissPalmiE9Q4Z2

Proteomic databases

jPOSTiE9Q4Z2
MaxQBiE9Q4Z2
PaxDbiE9Q4Z2
PeptideAtlasiE9Q4Z2
PRIDEiE9Q4Z2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031583; ENSMUSP00000031583; ENSMUSG00000042010
ENSMUST00000102582; ENSMUSP00000099642; ENSMUSG00000042010
GeneIDi100705
KEGGimmu:100705
UCSCiuc008yzi.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
32
MGIiMGI:2140940 Acacb

Phylogenomic databases

eggNOGiKOG0368 Eukaryota
COG0439 LUCA
COG0511 LUCA
COG4799 LUCA
GeneTreeiENSGT00940000155049
HOGENOMiHOG000214115
HOVERGENiHBG005371
InParanoidiE9Q4Z2
KOiK01946
OMAiYLQVEHH
OrthoDBi156081at2759
TreeFamiTF300061

Enzyme and pathway databases

UniPathwayi
UPA00655;UER00711

BRENDAi6.4.1.2 3474
ReactomeiR-MMU-163765 ChREBP activates metabolic gene expression
R-MMU-196780 Biotin transport and metabolism
R-MMU-200425 Import of palmitoyl-CoA into the mitochondrial matrix

Miscellaneous databases

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

More...
ChiTaRSi
Acacb mouse

Protein Ontology

More...
PROi
PR:E9Q4Z2

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000042010 Expressed in 128 organ(s), highest expression level in brown adipose tissue
ExpressionAtlasiE9Q4Z2 baseline and differential
GenevisibleiE9Q4Z2 MM

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiACACB_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: E9Q4Z2
Secondary accession number(s): Q6JIZ0
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: April 5, 2011
Last modified: January 16, 2019
This is version 71 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

Complete proteome, 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
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