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Protein

ATP-citrate synthase

Gene

Acly

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine (By similarity).By similarity

Catalytic activityi

ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.

Cofactori

Mg2+By similarity

Enzyme regulationi

Phosphorylation results in a 6-fold increase in V(max) and the conversion of citrate dependence from sigmoidal to hyperbolic. Fructose 6-phosphate (F6P) is also a potent activator.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei58ATPBy similarity1
Binding sitei118ATPBy similarity1
Metal bindingi201MagnesiumBy similarity1
Metal bindingi203MagnesiumBy similarity1
Binding sitei346Citrate; via amide nitrogenBy similarity1
Binding sitei348CitrateBy similarity1
Binding sitei379CitrateBy similarity1
Metal bindingi708MagnesiumBy similarity1
Active sitei750Tele-phosphohistidine intermediateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 67ATPBy similarity2
Nucleotide bindingi109 – 111ATPBy similarity3
Nucleotide bindingi691 – 711ATPBy similarityAdd BLAST21
Nucleotide bindingi742 – 768ATPBy similarityAdd BLAST27

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-163765. ChREBP activates metabolic gene expression.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Chemistry databases

SwissLipidsiSLP:000001386.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-citrate synthase (EC:2.3.3.8)
Alternative name(s):
ATP-citrate (pro-S-)-lyase
Citrate cleavage enzyme
Gene namesi
Name:Acly
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:103251. Acly.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3264.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001027821 – 1091ATP-citrate synthaseAdd BLAST1091

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei131PhosphotyrosineBy similarity1
Modified residuei263PhosphoserineCombined sources1
Modified residuei447PhosphothreonineBy similarity1
Modified residuei451PhosphoserineBy similarity1
Modified residuei455Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2Combined sources1
Modified residuei459PhosphoserineBy similarity1
Modified residuei530N6-acetyllysineBy similarity1
Modified residuei536N6-acetyllysineBy similarity1
Modified residuei544N6-acetyllysineBy similarity1
Modified residuei629PhosphothreonineBy similarity1
Modified residuei653PhosphoserineCombined sources1
Modified residuei672PhosphotyrosineCombined sources1
Modified residuei829PhosphoserineBy similarity1
Modified residuei938N6-acetyllysineBy similarity1
Modified residuei958N6-acetyllysineBy similarity1
Modified residuei968N6-acetyllysineCombined sources1
Modified residuei1067N6-acetyllysineBy similarity1
Modified residuei1090PhosphoserineCombined sources1

Post-translational modificationi

ISGylated.1 Publication
Acetylated at Lys-530, Lys-536 and Lys-544 by KAT2B/PCAF. Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites. Acetylation promotes de novo lipid synthesis. Deacetylated by SIRT2 (By similarity).By similarity
Ubiquitinated at Lys-530, Lys-536 and Lys-544 by UBR4, leading to its degradation. Ubiquitination is probably inhibited by acetylation at same site (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ91V92.
MaxQBiQ91V92.
PaxDbiQ91V92.
PeptideAtlasiQ91V92.
PRIDEiQ91V92.

PTM databases

iPTMnetiQ91V92.
PhosphoSitePlusiQ91V92.
SwissPalmiQ91V92.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020917.
CleanExiMM_ACLY.
ExpressionAtlasiQ91V92. baseline and differential.
GenevisibleiQ91V92. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Mef2cQ8CFN5-43EBI-644049,EBI-643822

Protein-protein interaction databases

BioGridi222369. 3 interactors.
IntActiQ91V92. 6 interactors.
MINTiMINT-1700320.
STRINGi10090.ENSMUSP00000103012.

Structurei

3D structure databases

ProteinModelPortaliQ91V92.
SMRiQ91V92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 265ATP-graspAdd BLAST262

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni769 – 779CoA-bindingSequence analysisAdd BLAST11

Sequence similaritiesi

In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.Curated
In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.Curated
Contains 1 ATP-grasp domain.Curated

Phylogenomic databases

eggNOGiKOG1254. Eukaryota.
COG0045. LUCA.
COG0074. LUCA.
COG0372. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000151479.
HOVERGENiHBG003318.
InParanoidiQ91V92.
KOiK01648.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR014608. ATP-citrate_synthase.
IPR013816. ATP_grasp_subdomain_2.
IPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR032263. Citrate-bd.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR033847. Citrt_syn/SCS-alpha_CS.
IPR003781. CoA-bd.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF16114. Citrate_bind. 1 hit.
PF00285. Citrate_synt. 1 hit.
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF036511. ATP_citrt_syn. 1 hit.
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF48256. SSF48256. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 1 hit.
PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91V92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL
60 70 80 90 100
LSQSLVVKPD QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG
110 120 130 140 150
FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ
160 170 180 190 200
KLLVGVDEKL NTEDIKRHLL VHAPEDKKEV LASFISGLFN FYEDLYFTYL
210 220 230 240 250
EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE
260 270 280 290 300
AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE
310 320 330 340 350
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPEGKILII GGSIANFTNV
360 370 380 390 400
AATFKGIVRA IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI
410 420 430 440 450
PIHVFGTETH MTAIVGMALG HRPIPNQPPT AAHTANFLLN ASGSTSTPAP
460 470 480 490 500
SRTASFSESR ADEVAPAKKA KPAMPQGKSA TLFSRHTKAI VWGMQTRAVQ
510 520 530 540 550
GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI PVFKNMADAM
560 570 580 590 600
KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI
610 620 630 640 650
KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV
660 670 680 690 700
SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV
710 720 730 740 750
KMIVVLGEIG GTEEYKICRG IKEGRLTKPV VCWCIGTCAT MFSSEVQFGH
760 770 780 790 800
AGACANQASE TAVAKNQALK EAGVFVPRSF DELGEIIQSV YEDLVAKGAI
810 820 830 840 850
VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ ELIYAGMPIT
860 870 880 890 900
EVFKEEMGIG GVLGLLWFQR RLPKYSCQFI EMCLMVTADH GPAVSGAHNT
910 920 930 940 950
IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV
960 970 980 990 1000
NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDFVKQHFPA TPLLDYALEV
1010 1020 1030 1040 1050
EKITTSKKPN LILNVDGFIG VAFVDMLRNC GSFTREEADE YVDIGALNGI
1060 1070 1080 1090
FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD ISYVLPEHMS M
Length:1,091
Mass (Da):119,728
Last modified:December 1, 2001 - v1
Checksum:i660293D027D797DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332052 mRNA. Translation: AAK56081.1.
AF332051 mRNA. Translation: AAK56080.1.
BC056378 mRNA. Translation: AAH56378.1.
CCDSiCCDS25425.1.
RefSeqiNP_598798.1. NM_134037.3.
UniGeneiMm.282039.

Genome annotation databases

EnsembliENSMUST00000007131; ENSMUSP00000007131; ENSMUSG00000020917.
ENSMUST00000165111; ENSMUSP00000127632; ENSMUSG00000020917.
GeneIDi104112.
KEGGimmu:104112.
UCSCiuc007lll.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332052 mRNA. Translation: AAK56081.1.
AF332051 mRNA. Translation: AAK56080.1.
BC056378 mRNA. Translation: AAH56378.1.
CCDSiCCDS25425.1.
RefSeqiNP_598798.1. NM_134037.3.
UniGeneiMm.282039.

3D structure databases

ProteinModelPortaliQ91V92.
SMRiQ91V92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222369. 3 interactors.
IntActiQ91V92. 6 interactors.
MINTiMINT-1700320.
STRINGi10090.ENSMUSP00000103012.

Chemistry databases

ChEMBLiCHEMBL3264.
SwissLipidsiSLP:000001386.

PTM databases

iPTMnetiQ91V92.
PhosphoSitePlusiQ91V92.
SwissPalmiQ91V92.

Proteomic databases

EPDiQ91V92.
MaxQBiQ91V92.
PaxDbiQ91V92.
PeptideAtlasiQ91V92.
PRIDEiQ91V92.

Protocols and materials databases

DNASUi104112.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007131; ENSMUSP00000007131; ENSMUSG00000020917.
ENSMUST00000165111; ENSMUSP00000127632; ENSMUSG00000020917.
GeneIDi104112.
KEGGimmu:104112.
UCSCiuc007lll.2. mouse.

Organism-specific databases

CTDi47.
MGIiMGI:103251. Acly.

Phylogenomic databases

eggNOGiKOG1254. Eukaryota.
COG0045. LUCA.
COG0074. LUCA.
COG0372. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000151479.
HOVERGENiHBG003318.
InParanoidiQ91V92.
KOiK01648.

Enzyme and pathway databases

ReactomeiR-MMU-163765. ChREBP activates metabolic gene expression.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

ChiTaRSiAcly. mouse.
PROiQ91V92.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020917.
CleanExiMM_ACLY.
ExpressionAtlasiQ91V92. baseline and differential.
GenevisibleiQ91V92. MM.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR014608. ATP-citrate_synthase.
IPR013816. ATP_grasp_subdomain_2.
IPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR032263. Citrate-bd.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR033847. Citrt_syn/SCS-alpha_CS.
IPR003781. CoA-bd.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF16114. Citrate_bind. 1 hit.
PF00285. Citrate_synt. 1 hit.
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF036511. ATP_citrt_syn. 1 hit.
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF48256. SSF48256. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 1 hit.
PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACLY_MOUSE
AccessioniPrimary (citable) accession number: Q91V92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.