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    Acly ATP citrate lyase [ Rattus norvegicus (Norway rat) ]

    Gene ID: 24159, updated on 27-Nov-2024

    Summary

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    Official Symbol
    Aclyprovided by RGD
    Official Full Name
    ATP citrate lyaseprovided by RGD
    Primary source
    RGD:2018
    See related
    EnsemblRapid:ENSRNOG00000016924 AllianceGenome:RGD:2018
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Rattus norvegicus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
    Also known as
    ACL; Clatp
    Summary
    Enables ATP citrate synthase activity. Involved in acetyl-CoA metabolic process; citrate metabolic process; and fatty acid biosynthetic process. Predicted to be located in nucleoplasm. Predicted to be active in cytosol. Orthologous to human ACLY (ATP citrate lyase). [provided by Alliance of Genome Resources, Nov 2024]
    Expression
    Biased expression in Adrenal (RPKM 1293.6), Liver (RPKM 1056.3) and 9 other tissues See more
    Orthologs
    human mouse all
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    Genomic context

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    See Acly in Genome Data Viewer
    Location:
    10q31
    Exon count:
    30
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCr8 (GCF_036323735.1) 10 NC_086028.1 (85912402..85964605, complement)
    RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 10 NC_051345.1 (85412045..85464253, complement)
    106 previous assembly Rnor_6.0 (GCF_000001895.5) 10 NC_005109.4 (88392248..88442845, complement)

    Chromosome 10 - NC_086028.1Genomic Context describing neighboring genes Neighboring gene kelch-like family member 10 Neighboring gene kelch-like family member 11 Neighboring gene transfer RNA serine (anticodon AGA) 28 Neighboring gene outer dynein arm docking complex subunit 4

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
    • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
    • BioProject: PRJNA238328
    • Publication: PMID 24510058
    • Analysis date: Mon Jun 6 17:44:12 2016

    Bibliography

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    Related articles in PubMed

    1. Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age. Elshourbagy NA, et al. J Biol Chem, 1990 Jan 25. PMID 2295639
    2. Cloning and identification of exon-intron organization of the rat ATP-citrate lyase gene. Moon YA, et al. Biochim Biophys Acta, 1996 Jul 17. PMID 8688462
    3. Characterization of cis-acting elements in the rat ATP citrate-lyase gene promoter. Moon YA, et al. Exp Mol Med, 2002 Mar 31. PMID 11989980
    4. Critical role for cataplerosis via citrate in glucose-regulated insulin release. Flamez D, et al. Diabetes, 2002 Jul. PMID 12086928
    5. Normal flux through ATP-citrate lyase or fatty acid synthase is not required for glucose-stimulated insulin secretion. Joseph JW, et al. J Biol Chem, 2007 Oct 26. PMID 17823126

    See all (36) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. ATP citrate lyase is important for the pyruvate citrate shuttle and lipid synthesis in insulin secretion.
      Title: High level of ATP citrate lyase expression in human and rat pancreatic islets.
    2. Differences between human and rodent pancreatic islets: low pyruvate carboxylase, atp citrate lyase, and pyruvate carboxylation and high glucose-stimulated acetoacetate in human pancreatic islets.
      Title: Differences between human and rodent pancreatic islets: low pyruvate carboxylase, atp citrate lyase, and pyruvate carboxylation and high glucose-stimulated acetoacetate in human pancreatic islets.
    3. mRNAs of SCOT and ATP citrate lyase were decreased 55% and 58% and enzyme activities were decreased >70% in pancreatic islets of the GK rat, a model of type 2 diabetes.
      Title: Lower succinyl-CoA:3-ketoacid-CoA transferase (SCOT) and ATP citrate lyase in pancreatic islets of a rat model of type 2 diabetes: knockdown of SCOT inhibits insulin release in rat insulinoma cells.
    4. Normal flux through ATP-citrate lyase is not required for glucose-stimulated insulin secretion.
      Title: Normal flux through ATP-citrate lyase or fatty acid synthase is not required for glucose-stimulated insulin secretion.
    5. Results suggest that Sp1 acts on the ATP citrate lyase promoter to produce basal and induced transcription by low fat/high carbohydrate diets.
      Title: Characterization of cis-acting elements in the rat ATP citrate-lyase gene promoter.
    6. ATP-citrate lyase is a protein kinase B substrate in adipocytes
      Title: The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes.
    7. expression in insulin-producing beta cells is linked to glucose-regulated insulin secretion
      Title: Critical role for cataplerosis via citrate in glucose-regulated insulin release.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Clone Names

    • MGC124629

    Gene Ontology Provided by RGD

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP citrate synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP citrate synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP citrate synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP citrate synthase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in acetyl-CoA biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in acetyl-CoA biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in acetyl-CoA biosynthetic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in acetyl-CoA biosynthetic process NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in acetyl-CoA metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in citrate metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in citrate metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in citrate metabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in fatty acid biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in fatty acid biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in fatty acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in fatty acid biosynthetic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in lipid biosynthetic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in lipid biosynthetic process ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in lipid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in oxaloacetate metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in oxaloacetate metabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in cytosol ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    located_in nucleoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleoplasm ISO
    Inferred from Sequence Orthology
    more info
    		  

    General protein information

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    Preferred Names
    ATP-citrate synthase
    Names
    ATP-citrate (pro-S-)-lyase
    citrate cleavage enzyme
    NP_001104565.1
    NP_058683.2
    XP_038941092.1

    NCBI Reference Sequences (RefSeq)

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    NEW Try the new Transcript table

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001111095.1 → NP_001104565.1  ATP-citrate synthase isoform 2

      See identical proteins and their annotated locations for NP_001104565.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (2) lacks an alternate exon in the coding region compared to variant 1. The resulting protein (isoform 2) is shorter but has the same N- and C-termini compared to isoform 1.
      Source sequence(s)
      BC100618, CB800173, CR471829, DY473160, J05210
      UniProtKB/Swiss-Prot
      P16638, Q497C7, Q8VIQ1
      UniProtKB/TrEMBL
      A6HJ38, G3V9G4
      Related
      ENSRNOP00000046597.3, ENSRNOT00000043172.6
      Conserved Domains (6) summary
      cd06100
      Location:846 → 1083
      CCL_ACL-C; Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ...
      PLN02235
      Location:1 → 419
      PLN02235; ATP citrate (pro-S)-lyase
      PLN02522
      Location:479 → 1084
      PLN02522; ATP citrate (pro-S)-lyase
      pfam16114
      Location:247 → 421
      Citrate_bind; ATP citrate lyase citrate-binding
      cl21454
      Location:487 → 590
      NADB_Rossmann; Rossmann-fold NAD(P)(+)-binding proteins
      cl22543
      Location:650 → 775
      Ligase_CoA; CoA-ligase

    2. NM_016987.2 → NP_058683.2  ATP-citrate synthase isoform 1

      See identical proteins and their annotated locations for NP_058683.2

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) represents the longer transcript and encodes the longer protein (isoform 1).
      Source sequence(s)
      BC100618, CB800173, CR471829, DY473160, J05210
      UniProtKB/Swiss-Prot
      P16638, Q497C7, Q8VIQ1
      UniProtKB/TrEMBL
      A6HJ39, G3V888
      Related
      ENSRNOP00000023447.3, ENSRNOT00000023447.8
      Conserved Domains (2) summary
      PLN02522
      Location:489 → 1094
      PLN02522; ATP citrate (pro-S)-lyase
      cl29684
      Location:1 → 419
      Citrate_bind; ATP citrate lyase citrate-binding

    RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCr8

    Genomic

    1. NC_086028.1 Reference GRCr8

      Range
      85912402..85964605 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_039085164.2 → XP_038941092.1  ATP-citrate synthase isoform X1

      UniProtKB/Swiss-Prot
      P16638, Q497C7, Q8VIQ1
      UniProtKB/TrEMBL
      A6HJ39, G3V888
      Conserved Domains (2) summary
      PLN02522
      Location:489 → 1094
      PLN02522; ATP citrate (pro-S)-lyase
      cl29684
      Location:1 → 419
      Citrate_bind; ATP citrate lyase citrate-binding
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P16638.1 GenPept UniProtKB/Swiss-Prot:P16638

    Gene LinkOut

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