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

Gene ID: 24159, updated on 11-Apr-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
Ensembl: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 and plasma membrane. Predicted to be active in cytosol. Orthologous to human ACLY (ATP citrate lyase). [provided by Alliance of Genome Resources, Apr 2022]
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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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. Critical role for cataplerosis via citrate in glucose-regulated insulin release. Flamez D, et al. Diabetes, 2002 Jul. PMID 12086928
  2. 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
  3. 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
  4. 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
  5. Enhanced lipid accumulation in the yeast Yarrowia lipolytica by over-expression of ATP:citrate lyase from Mus musculus. Zhang H, et al. J Biotechnol, 2014 Dec 20. PMID 25450640

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
  
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 oxaloacetate metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in oxaloacetate metabolic process ISO
Inferred from Sequence Orthology
more info
  
involved_in tricarboxylic acid cycle IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
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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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, ENSRNOT00000043172.5
    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, ENSRNOT00000023447.7
    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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