Reviewed, UniProtKB/Swiss-Prot Q91V92 (ACLY_MOUSE)

Names and origin

Protein names

Recommended name:
    ATP-citrate synthase
    EC=2.3.3.8
Alternative name(s):
    ATP-citrate (pro-S-)-lyase
    Citrate cleavage enzyme

Gene names

Name:

Acly

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1091 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	ATP citrate-lyase 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.
Catalytic activity	ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family. In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	acetyl-CoA biosynthetic process Traceable author statement. Source: MGI cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activity Traceable author statement. Source: MGI magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct succinate-CoA ligase (ADP-forming) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Mef2c	Q8CFN5-4	2	EBI-644049,EBI-643822

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1091	1091	ATP-citrate synthase		PRO_0000102782
Regions
	Nucleotide binding	691 – 711	21	ATP By similarity
	Nucleotide binding	742 – 768	27	ATP By similarity
	Region	769 – 779	11	CoA-binding Potential
Sites
	Active site	750	1	Tele-phosphohistidine intermediate By similarity
	Metal binding	708	1	Magnesium By similarity
Amino acid modifications
	Modified residue	86	1	N6-acetyllysine By similarity
	Modified residue	131	1	Phosphotyrosine By similarity
	Modified residue	455	1	Phosphoserine; by PKA Ref.4 Ref.6 Ref.7
	Modified residue	536	1	N6-acetyllysine By similarity
	Modified residue	544	1	N6-acetyllysine By similarity
	Modified residue	672	1	Phosphotyrosine Ref.3 Ref.5
	Modified residue	938	1	N6-acetyllysine By similarity
	Modified residue	952	1	N6-acetyllysine By similarity
	Modified residue	958	1	N6-acetyllysine By similarity
	Modified residue	968	1	N6-acetyllysine By similarity
	Modified residue	1067	1	N6-acetyllysine By similarity
	Modified residue	1090	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q91V92-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 660293D027D797DD	FASTA	1,091	119,728
	10 20 30 40 50 60 MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL LSQSLVVKPD 70 80 90 100 110 120 QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG FLKNFLIEPF VPHSQAEEFY 130 140 150 160 170 180 VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NTEDIKRHLL VHAPEDKKEV 190 200 210 220 230 240 LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP 250 260 270 280 290 300 PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 310 320 330 340 350 360 LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPEGKILII GGSIANFTNV AATFKGIVRA 370 380 390 400 410 420 IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG 430 440 450 460 470 480 HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR ADEVAPAKKA KPAMPQGKSA 490 500 510 520 530 540 TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI 550 560 570 580 590 600 PVFKNMADAM KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI 610 620 630 640 650 660 KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV SRSGGMSNEL 670 680 690 700 710 720 NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG GTEEYKICRG 730 740 750 760 770 780 IKEGRLTKPV VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF 790 800 810 820 830 840 DELGEIIQSV YEDLVAKGAI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ 850 860 870 880 890 900 ELIYAGMPIT EVFKEEMGIG GVLGLLWFQR RLPKYSCQFI EMCLMVTADH GPAVSGAHNT 910 920 930 940 950 960 IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV NKMKKEGKLI 970 980 990 1000 1010 1020 MGIGHRVKSI NNPDMRVQIL KDFVKQHFPA TPLLDYALEV EKITTSKKPN LILNVDGFIG 1030 1040 1050 1060 1070 1080 VAFVDMLRNC GSFTREEADE YVDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD 1090 ISYVLPEHMS M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed: 11471062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ILS and ISS.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[3]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, MASS SPECTROMETRY. Tissue: Mast cell.
[4]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF332052 mRNA. Translation: AAK56081.1. AF332051 mRNA. Translation: AAK56080.1. BC056378 mRNA. Translation: AAH56378.1.
IPI	IPI00762047.
RefSeq	NP_598798.1.
UniGene	Mm.282039
3D structure databases
HSSP	HSSP built from PDB template 1SCU based on UniProtKB P07459.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q91V92. 2 interactions.
STRING	Q91V92.
PTM databases
PhosphoSite	Q91V92.
Proteomic databases
PRIDE	Q91V92.
Genome annotation databases
Ensembl	ENSMUST00000007131; ENSMUSP00000007131; ENSMUSG00000020917; Mus musculus. [Genome view] ENSMUST00000107389; ENSMUSP00000103012; ENSMUSG00000020917; Mus musculus. [Genome view]
GeneID	104112.
KEGG	mmu:104112.
NMPDR	fig|10090.3.peg.25294.
UCSC	uc007lll.1. mouse.
Organism-specific databases
CTD	104112.
MGI	MGI:103251. Acly.
Phylogenomic databases
HOVERGEN	Q91V92.
Enzyme and pathway databases
BRENDA	2.3.3.8. 244.
Gene expression databases
ArrayExpress	Q91V92.
Bgee	Q91V92.
CleanEx	MM_ACLY.
Genevestigator	Q91V92.
GermOnline	ENSMUSG00000020917. Mus musculus.
Family and domain databases
InterPro	IPR014608. ATP-citrate_synthase. IPR013816. ATP_grasp_subdomain_2. IPR017440. Cit_synth/succinyl-CoA_lig_AS. IPR016143. Citrate_synth-like_sm_a-sub. IPR003781. CoA_bd. IPR005810. CoA_lig_alpha. IPR005811. CoA_ligase. IPR016040. NAD(P)-bd_dom. IPR017866. Succ-CoA_synthase_bsu_CS. IPR016102. Succinyl-CoA_synth-like. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:1.10.230.10. Citrate_synthase_sm_a-sub. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit.
Pfam	PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view]
PIRSF	PIRSF036511. ATP_citrt_syn. 1 hit.
PROSITE	PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. 1 hit. PS01217. SUCCINYL_COA_LIG_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	356548.
SOURCE	Search...

Entry information

Entry name

ACLY_MOUSE

Accession

Primary (citable) accession number: Q91V92

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)