Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 170 (13 Nov 2019)
Sequence version 1 (01 Aug 1990)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

ATP-citrate synthase

Gene

Acly

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phosphorylation results in activation of its activity (By similarity). Glucose 6-phosphate, fructose 6-phosphate, fructose 2,6-bisphosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate also act as activators (By similarity).By similarity

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=155.0 µM for citrate1 Publication
  2. KM=103.0 µM for ATP1 Publication
  3. KM=15.0 µM for CoA1 Publication
  1. Vmax=1.9 µmol/h/µg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei58ATPBy similarity1
Binding sitei118ATPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi201MagnesiumBy similarity1
Metal bindingi203MagnesiumBy similarity1
Binding sitei346Citrate; via amide nitrogenBy similarity1
Binding sitei348CitrateBy similarity1
Binding sitei379CitrateBy similarity1
Metal bindingi717MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei759Tele-phosphohistidine intermediate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi66 – 67ATPBy similarity2
Nucleotide bindingi109 – 111ATPBy similarity3
Nucleotide bindingi700 – 720ATPBy similarityAdd BLAST21
Nucleotide bindingi751 – 777ATPBy similarityAdd BLAST27

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processLipid biosynthesis, Lipid metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-163765 ChREBP activates metabolic gene expression
R-RNO-6798695 Neutrophil degranulation
R-RNO-75105 Fatty acyl-CoA biosynthesis

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ATP-citrate synthase (EC:2.3.3.81 Publication)
Alternative name(s):
ATP-citrate (pro-S-)-lyase
Citrate cleavage enzyme
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Acly
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2018 Acly

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2745

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001027831 – 1100ATP-citrate synthaseAdd BLAST1100

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei131PhosphotyrosineBy similarity1
Modified residuei263PhosphoserineBy similarity1
Modified residuei446Phosphothreonine1 Publication1
Modified residuei450Phosphoserine1 Publication1
Modified residuei454Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2Combined sources1 Publication1
Modified residuei458PhosphoserineBy similarity1
Modified residuei480PhosphoserineCombined sources1
Modified residuei539N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki539Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei545N6-acetyllysine; alternateBy similarity1
Cross-linki545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei553N6-acetyllysine; alternateBy similarity1
Cross-linki553Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei638PhosphothreonineBy similarity1
Modified residuei662PhosphoserineCombined sources1
Modified residuei681PhosphotyrosineBy similarity1
Modified residuei838PhosphoserineBy similarity1
Modified residuei947N6-acetyllysineBy similarity1
Modified residuei967N6-acetyllysineBy similarity1
Modified residuei977N6-acetyllysineBy similarity1
Modified residuei1076N6-acetyllysineBy similarity1
Modified residuei1099PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by PKA and GSK3 in a sequential manner; phosphorylation results in activation of its activity (By similarity). Phosphorylation on Thr-446 and Ser-450 depends on the phosphorylation state of Ser-454 (PubMed:12107176, PubMed:2176822). Phosphorylation on Ser-454 is decreased by prior phosphorylation on the other 2 residues (PubMed:12107176, PubMed:2176822).By similarity2 Publications
The N-terminus is blocked.1 Publication
ISGylated.By similarity
Acetylated at Lys-539, Lys-545 and Lys-553 by KAT2B/PCAF (By similarity). Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites (By similarity). Acetylation promotes de novo lipid synthesis (By similarity). Deacetylated by SIRT2 (By similarity).By similarity
Ubiquitinated at Lys-539, Lys-545 and Lys-553 by UBR4, leading to its degradation (By similarity). Ubiquitination is probably inhibited by acetylation at same site (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P16638

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P16638

PeptideAtlas

More...
PeptideAtlasi
P16638

PRoteomics IDEntifications database

More...
PRIDEi
P16638

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16638

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P16638

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the brain, kidney, mammary gland, lung and liver.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246351, 4 interactors

Protein interaction database and analysis system

More...
IntActi
P16638, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000023447

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P16638

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P16638

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 265ATP-graspAdd BLAST262

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni778 – 788CoA-bindingSequence analysisAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1254 Eukaryota
COG0045 LUCA
COG0074 LUCA
COG0372 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000151479

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16638

KEGG Orthology (KO)

More...
KOi
K01648

Database of Orthologous Groups

More...
OrthoDBi
349367at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P16638

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.230.10, 1 hit
1.10.580.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.261, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014608 ATP-citrate_synthase
IPR013815 ATP_grasp_subdomain_1
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16114 Citrate_bind, 1 hit
PF00285 Citrate_synt, 1 hit
PF02629 CoA_binding, 1 hit
PF00549 Ligase_CoA, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036511 ATP_citrt_syn, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00881 CoA_binding, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48256 SSF48256, 1 hit
SSF51735 SSF51735, 1 hit
SSF52210 SSF52210, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01216 SUCCINYL_COA_LIG_1, 1 hit
PS00399 SUCCINYL_COA_LIG_2, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P16638-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 DVGDVDTKAQ
160 170 180 190 200
KLLVGVDEKL NAEDIKRHLL VHAPEDKKEI 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 KHPDGKILII GGSIANFTNV
360 370 380 390 400
AATFKGIVRA IRDYQGSLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI
410 420 430 440 450
PIHVFGTETH MTAIVGMAWA PAIPNQPPTA AHTANFLLNA SGSTSTPAPS
460 470 480 490 500
RTASFSESRA DEVAPAKKAK PAMPQDSVPS PRSLQGKSAT LFSRHTKAIV
510 520 530 540 550
WGMQTRAVQG MLDFDYVCSR DEPSVAAMVY PFTGDHKQKF YWGHKEILIP
560 570 580 590 600
VFKNMADAMK KHPEVDVLIN FASLRSAYDS TMETMNYAQI RTIAIIAEGI
610 620 630 640 650
PEALTRKLIK KADQKGVTII GPATVGGIKP GCFKIGNTGG MLDNILASKL
660 670 680 690 700
YRPGSVAYVS RSGGMSNELN NIISRTTDGV YEGVAIGGDR YPGSTFMDHV
710 720 730 740 750
LRYQDTPGVK MIVVLGEIGG TEEYKICRGI KEGRLTKPVV CWCIGTCATM
760 770 780 790 800
FSSEVQFGHA GACANQASET AVAKNQALKE AGVFVPRSFD ELGEIIQSVY
810 820 830 840 850
EDLVAKGAIV PAQEVPPPTV PMDYSWAREL GLIRKPASFM TSICDERGQE
860 870 880 890 900
LIYAGMPITE VFKEEMGIGG VLGLLWFQRR LPKYSCQFIE MCLMVTADHG
910 920 930 940 950
PAVSGAHNTI ICARAGKDLV SSLTSGLLTI GDRFGGALDA AAKMFSKAFD
960 970 980 990 1000
SGIIPMEFVN KMKKEGKLIM GIGHRVKSIN NPDMRVQILK DFVKQHFPAT
1010 1020 1030 1040 1050
PLLDYALEVE KITTSKKPNL ILNVDGFIGV AFVDMLRNCG SFTREEADEY
1060 1070 1080 1090 1100
VDIGALNGVF VLGRSMGFIG HYLDQKRLKQ GLYRHPWDDI SYVLPEHMSM
Length:1,100
Mass (Da):120,636
Last modified:August 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2C6BE4BC1F53BDD2
GO
Isoform 2 (identifier: P16638-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     419-422: WAPA → LGHRP
     475-484: Missing.

Show »
Length:1,091
Mass (Da):119,704
Checksum:iCC7A9B9F0C18E62E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V888G3V888_RAT
ATP-citrate synthase
Acly rCG_33241
1,101Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V9G4G3V9G4_RAT
ATP-citrate synthase
Acly rCG_33241
1,091Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2K5E7A0A0G2K5E7_RAT
ATP-citrate synthase
Acly
1,100Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti116A → V in AAI00619 (PubMed:15489334).Curated1
Sequence conflicti367S → P in AAI00619 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_026273419 – 422WAPA → LGHRP in isoform 2. 1 Publication4
Alternative sequenceiVSP_026274475 – 484Missing in isoform 2. 1 Publication10

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J05210 mRNA Translation: AAA74463.1
BC100618 mRNA Translation: AAI00619.1
AH011205 Genomic DNA Translation: AAL34316.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A35007

NCBI Reference Sequences

More...
RefSeqi
NP_001104565.1, NM_001111095.1
NP_058683.2, NM_016987.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24159

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24159

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05210 mRNA Translation: AAA74463.1
BC100618 mRNA Translation: AAI00619.1
AH011205 Genomic DNA Translation: AAL34316.1
PIRiA35007
RefSeqiNP_001104565.1, NM_001111095.1
NP_058683.2, NM_016987.2

3D structure databases

SMRiP16638
ModBaseiSearch...

Protein-protein interaction databases

BioGridi246351, 4 interactors
IntActiP16638, 2 interactors
STRINGi10116.ENSRNOP00000023447

Chemistry databases

BindingDBiP16638
ChEMBLiCHEMBL2745

PTM databases

iPTMnetiP16638
PhosphoSitePlusiP16638

Proteomic databases

jPOSTiP16638
PaxDbiP16638
PeptideAtlasiP16638
PRIDEiP16638

Genome annotation databases

GeneIDi24159
KEGGirno:24159

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
47
RGDi2018 Acly

Phylogenomic databases

eggNOGiKOG1254 Eukaryota
COG0045 LUCA
COG0074 LUCA
COG0372 LUCA
HOGENOMiHOG000151479
InParanoidiP16638
KOiK01648
OrthoDBi349367at2759
PhylomeDBiP16638

Enzyme and pathway databases

ReactomeiR-RNO-163765 ChREBP activates metabolic gene expression
R-RNO-6798695 Neutrophil degranulation
R-RNO-75105 Fatty acyl-CoA biosynthesis

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P16638

Family and domain databases

Gene3Di1.10.230.10, 1 hit
1.10.580.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.261, 2 hits
InterProiView protein in InterPro
IPR014608 ATP-citrate_synthase
IPR013815 ATP_grasp_subdomain_1
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, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACLY_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16638
Secondary accession number(s): Q497C7, Q8VIQ1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 13, 2019
This is version 170 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again