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Protein

ATP-citrate synthase

Gene

Acly

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionTransferase
Biological processLipid biosynthesis, Lipid metabolism
LigandATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:103251 Acly

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

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-acetyllysine; alternateBy similarity1
Cross-linki530Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei536N6-acetyllysine; alternateBy similarity1
Cross-linki536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei544N6-acetyllysine; alternateBy similarity1
Cross-linki544Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
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, Isopeptide bond, 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, 4 interactors
IntActiQ91V92, 6 interactors
MINTiQ91V92
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

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
3.40.50.261, 2 hits
InterProiView protein in InterPro
IPR014608 ATP-citrate_synthase
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
IPR036969 Citrate_synthase_sf
IPR033847 Citrt_syn/SCS-alpha_CS
IPR003781 CoA-bd
IPR005811 CoA_ligase
IPR036291 NAD(P)-bd_dom_sf
IPR017866 Succ-CoA_synthase_bsu_CS
IPR016102 Succinyl-CoA_synth-like
PfamiView protein in Pfam
PF16114 Citrate_bind, 1 hit
PF00285 Citrate_synt, 1 hit
PF02629 CoA_binding, 1 hit
PF00549 Ligase_CoA, 1 hit
PIRSFiPIRSF036511 ATP_citrt_syn, 1 hit
SMARTiView protein in SMART
SM00881 CoA_binding, 1 hit
SUPFAMiSSF48256 SSF48256, 2 hits
SSF51735 SSF51735, 1 hit
SSF52210 SSF52210, 1 hit
PROSITEiView protein in PROSITE
PS01216 SUCCINYL_COA_LIG_1, 1 hit
PS00399 SUCCINYL_COA_LIG_2, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiACLY_MOUSE
AccessioniPrimary (citable) accession number: Q91V92
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: May 23, 2018
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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