ATP-citrate synthase - Mus musculus (Mouse)

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Q91V92 (ACLY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1091 AA.
Sequence status	Complete.
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.
Post-translational modification	ISGylated. Ref.3
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 biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process Traceable author statement PubMed 1371749. Source: MGI cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lipid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activity Traceable author statement PubMed 1371749. Source: MGI cofactor binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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	3	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

ATP By similarity

Nucleotide binding

742 – 768

ATP By similarity

Region

769 – 779

CoA-binding Potential

Sites

Active site

750

Tele-phosphohistidine intermediate By similarity

Metal binding

708

Magnesium By similarity

Binding site

346

Citrate; via amide nitrogen By similarity

Binding site

348

Citrate By similarity

Binding site

379

Citrate By similarity

Amino acid modifications

Modified residue

131

Phosphotyrosine By similarity

Modified residue

447

Phosphothreonine By similarity

Modified residue

451

Phosphoserine By similarity

Modified residue

455

Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2 Ref.5 Ref.7 Ref.8

Modified residue

536

N6-acetyllysine By similarity

Modified residue

544

N6-acetyllysine By similarity

Modified residue

629

Phosphothreonine By similarity

Modified residue

653

Phosphoserine By similarity

Modified residue

672

Phosphotyrosine Ref.4 Ref.6

Modified residue

829

Phosphoserine By similarity

Modified residue

938

N6-acetyllysine By similarity

Modified residue

958

N6-acetyllysine By similarity

Modified residue

1067

N6-acetyllysine By similarity

Modified residue

1090

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q91V92 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 660293D027D797DD
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[3]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
[4]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, MASS SPECTROMETRY. Tissue: Mast cell.
[5]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY. Tissue: Liver.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, MASS SPECTROMETRY. Tissue: Brain.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY. Tissue: Liver.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF332052 mRNA. Translation: AAK56081.1. AF332051 mRNA. Translation: AAK56080.1. BC056378 mRNA. Translation: AAH56378.1.
IPI	IPI00762047.
RefSeq	NP_598798.1. NM_134037.3.
UniGene	Mm.282039.
3D structure databases
ProteinModelPortal	Q91V92.
SMR	Q91V92. Positions 2-810, 901-1065.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q91V92. 2 interactions.
PTM databases
PhosphoSite	Q91V92.
Proteomic databases
PaxDb	Q91V92.
PRIDE	Q91V92.
Protocols and materials databases
DNASU	104112.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000007131; ENSMUSP00000007131; ENSMUSG00000020917. ENSMUST00000165111; ENSMUSP00000127632; ENSMUSG00000020917.
GeneID	104112.
KEGG	mmu:104112.
Organism-specific databases
CTD	47.
MGI	MGI:103251. Acly.
Phylogenomic databases
eggNOG	COG0372.
GeneTree	ENSGT00530000063275.
HOGENOM	HOG000151479.
HOVERGEN	HBG003318.
KO	K01648.
OrthoDB	EOG40ZQWS.
Gene expression databases
ArrayExpress	Q91V92.
Bgee	Q91V92.
CleanEx	MM_ACLY.
Genevestigator	Q91V92.
GermOnline	ENSMUSG00000020917. Mus musculus.
Family and domain databases
Gene3D	1.10.230.10. 1 hit. 3.30.470.20. 1 hit. 3.40.50.261. 2 hits. 3.40.50.720. 1 hit.
InterPro	IPR014608. ATP-citrate_synthase. IPR013650. ATP-grasp_succ-CoA_synth-type. IPR013816. ATP_grasp_subdomain_2. IPR017440. Cit_synth/succinyl-CoA_lig_AS. IPR016143. Citrate_synth-like_sm_a-sub. IPR002020. Citrate_synthase-like. IPR016141. Citrate_synthase-like_core. 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]
Pfam	PF08442. ATP-grasp_2. 1 hit. PF00285. Citrate_synt. 1 hit. PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view]
PIRSF	PIRSF036511. ATP_citrt_syn. 1 hit.
SUPFAM	SSF48256. Citrate_synthase_core. 1 hit. SSF52210. CoA_ligase. 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
ChEMBL	CHEMBL3264.
ChiTaRS	ACLY. mouse.
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:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents