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Protein

Citrate synthase 4, mitochondrial

Gene

CSY4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei308 – 3081PROSITE-ProRule annotation
Active sitei354 – 3541PROSITE-ProRule annotation
Active sitei409 – 4091PROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: TAIR
  2. citrate (Si)-synthase activity Source: TAIR
  3. zinc ion binding Source: TAIR

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. response to cadmium ion Source: TAIR
  3. tricarboxylic acid cycle Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciARA:AT2G44350-MONOMER.
ARA:GQT-2323-MONOMER.
ReactomeiREACT_289406. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase 4, mitochondrial (EC:2.3.3.16)
Gene namesi
Name:CSY4
Ordered Locus Names:At2g44350
ORF Names:F4I1.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G44350.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. cell wall Source: TAIR
  2. chloroplast Source: TAIR
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616MitochondrionSequence AnalysisAdd
BLAST
Chaini17 – 474458Citrate synthase 4, mitochondrialPRO_0000005484Add
BLAST

Proteomic databases

PaxDbiP20115.
PRIDEiP20115.

Expressioni

Gene expression databases

GenevestigatoriP20115.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4378. 3 interactions.
IntActiP20115. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP20115.
SMRiP20115. Positions 40-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiP20115.
KOiK01647.
OMAiWLQMQSP.
PhylomeDBiP20115.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P20115-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MVFFRSVSAF TRLRSRVQGQ QSSLSNSVRW IQMQSSTDLD LKSQLQELIP
60 70 80 90 100
EQQDRLKKLK SEHGKVQLGN ITVDMVIGGM RGMTGLLWET SLLDPEEGIR
110 120 130 140 150
FRGLSIPECQ KVLPTAQSGA EPLPEGLLWL LLTGKVPSKE QVEALSKDLA
160 170 180 190 200
NRAAVPDYVY NAIDALPSTA HPMTQFASGV MALQVQSEFQ KAYENGIHKS
210 220 230 240 250
KFWEPTYEDC LNLIARVPVV AAYVYRRMYK NGDSIPSDKS LDYGANFSHM
260 270 280 290 300
LGFDDEKVKE LMRLYITIHS DHEGGNVSAH TGHLVGSALS DPYLSFAAAL
310 320 330 340 350
NGLAGPLHGL ANQEVLLWIK SVVEECGEDI SKEQLKEYVW KTLNSGKVIP
360 370 380 390 400
GYGHGVLRNT DPRYVCQREF ALKHLPDDPL FQLVSKLYEV VPPVLTELGK
410 420 430 440 450
VKNPWPNVDA HSGVLLNHYG LTEARYYTVL FGVSRSLGIC SQLIWDRALG
460 470
LALERPKSVT MDWLEAHCKK ASSA
Length:474
Mass (Da):52,782
Last modified:January 16, 2004 - v3
Checksum:iD306BD540868FCA9
GO
Isoform 2 (identifier: P20115-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     18-18: Missing.

Show »
Length:473
Mass (Da):52,654
Checksum:iDF747D3DA8943FFB
GO

Sequence cautioni

The sequence CAA35570.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251S → N in AAM62868 (Ref. 5) Curated
Sequence conflicti52 – 532QQ → HK in CAA35570 (PubMed:2491664).Curated
Sequence conflicti112 – 1121V → AL in CAA35570 (PubMed:2491664).Curated
Sequence conflicti156 – 1561P → S in CAA35570 (PubMed:2491664).Curated
Sequence conflicti257 – 2582KV → RL in CAA35570 (PubMed:2491664).Curated
Sequence conflicti375 – 3751L → H in CAA35570 (PubMed:2491664).Curated
Sequence conflicti383 – 3853LVS → CC in CAA35570 (PubMed:2491664).Curated
Sequence conflicti448 – 4503ALG → ELL in CAA35570 (PubMed:2491664).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei18 – 181Missing in isoform 2. 2 PublicationsVSP_009185

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17528 mRNA. Translation: CAA35570.1. Frameshift.
AC004521 Genomic DNA. Translation: AAC16084.2.
CP002685 Genomic DNA. Translation: AEC10410.1.
CP002685 Genomic DNA. Translation: AEC10411.1.
AF387018 mRNA. Translation: AAK62463.1.
BT006613 mRNA. Translation: AAP31957.1.
AY085647 mRNA. Translation: AAM62868.1.
PIRiJA0149. YKMUM.
T02390.
RefSeqiNP_566016.1. NM_129998.3. [P20115-2]
NP_850415.1. NM_180084.2. [P20115-1]
UniGeneiAt.34501.
At.71156.

Genome annotation databases

EnsemblPlantsiAT2G44350.2; AT2G44350.2; AT2G44350. [P20115-1]
GeneIDi819042.
KEGGiath:AT2G44350.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17528 mRNA. Translation: CAA35570.1. Frameshift.
AC004521 Genomic DNA. Translation: AAC16084.2.
CP002685 Genomic DNA. Translation: AEC10410.1.
CP002685 Genomic DNA. Translation: AEC10411.1.
AF387018 mRNA. Translation: AAK62463.1.
BT006613 mRNA. Translation: AAP31957.1.
AY085647 mRNA. Translation: AAM62868.1.
PIRiJA0149. YKMUM.
T02390.
RefSeqiNP_566016.1. NM_129998.3. [P20115-2]
NP_850415.1. NM_180084.2. [P20115-1]
UniGeneiAt.34501.
At.71156.

3D structure databases

ProteinModelPortaliP20115.
SMRiP20115. Positions 40-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4378. 3 interactions.
IntActiP20115. 2 interactions.

Proteomic databases

PaxDbiP20115.
PRIDEiP20115.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G44350.2; AT2G44350.2; AT2G44350. [P20115-1]
GeneIDi819042.
KEGGiath:AT2G44350.

Organism-specific databases

GeneFarmi4309.
TAIRiAT2G44350.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiP20115.
KOiK01647.
OMAiWLQMQSP.
PhylomeDBiP20115.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciARA:AT2G44350-MONOMER.
ARA:GQT-2323-MONOMER.
ReactomeiREACT_289406. Citric acid cycle (TCA cycle).

Gene expression databases

GenevestigatoriP20115.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a cDNA encoding mitochondrial citrate synthase from Arabidopsis thaliana."
    Unger E.A., Hand J.M., Cashmore A.R., Vasconcelos A.C.
    Plant Mol. Biol. 13:411-418(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "Proteomic analysis of the Arabidopsis cell wall reveals unexpected proteins with new cellular locations."
    Slabas A.R., Ndimba B., Simon W.J., Chivasa S.
    Biochem. Soc. Trans. 32:524-528(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, POSSIBLE SUBCELLULAR LOCATION.
  7. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiCISY4_ARATH
AccessioniPrimary (citable) accession number: P20115
Secondary accession number(s): O64869, Q8LE36, Q94EY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 16, 2004
Last modified: April 1, 2015
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.