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Q9W401

- CISY_DROME

UniProt

Q9W401 - CISY_DROME

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Protein
Probable citrate synthase, mitochondrial
Gene
kdn, l(1)G0030, CG3861
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Plays a role in controlling neuronal activity and seizure susceptibility.1 Publication

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei302 – 3021 By similarity
Active sitei348 – 3481 By similarity
Active sitei403 – 4031 By similarity

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: UniProtKB

GO - Biological processi

  1. behavior Source: UniProtKB-KW
  2. carbohydrate metabolic process Source: UniProtKB
  3. cellular carbohydrate metabolic process Source: InterPro
  4. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Behavior, Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_218888. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable citrate synthase, mitochondrial (EC:2.3.3.16)
Alternative name(s):
Protein knockdown
Gene namesi
Name:kdn
Synonyms:l(1)G0030
ORF Names:CG3861
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0261955. kdn.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. microtubule associated complex Source: FlyBase
  2. mitochondrial matrix Source: UniProtKB
  3. mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 464Probable citrate synthase, mitochondrialPRO_0000291603
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Proteomic databases

PaxDbiQ9W401.
PRIDEiQ9W401.

Expressioni

Gene expression databases

BgeeiQ9W401.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi58066. 3 interactions.
MINTiMINT-936064.
STRINGi7227.FBpp0070871.

Structurei

3D structure databases

ProteinModelPortaliQ9W401.
SMRiQ9W401. Positions 29-462.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00390000006813.
InParanoidiQ9W401.
KOiK01647.
OMAiELIYEDC.
OrthoDBiEOG73BVCB.
PhylomeDBiQ9W401.

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. Align

Isoform A (identifier: Q9W401-1) [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

MSLYRISARK LSEAQKLPNV GAYVRMIAAD GKSLRDVLAA KVPQEQERVK    50
NFRKQHGATK MGETTIDMMY GGMRGIKALV TETSVLDADE GIRFRGLSIP 100
ECQKVLPAAD GGTEPLPEGL FWLLLTGEVP TKSQVQQLSR EWAERAALPQ 150
HVVTMLNNMP TTLHPMSQFA AAVTALNHDS KFAKAYSDGV HKSKYWEYVY 200
EDSMDLIAKL PVVAATIYCN TYRGGKGSRS IDSSLDWSAN FVKMLGYDNA 250
PFTELMRLYL TIHSDHEGGN VSAHTVHLVG SALSDPYLSF AAGLNGLAGP 300
LHGLANQEVL VWLRKLQKEA GNNPSEEQLK EYIWKTLKSG QVVPGYGHAV 350
LRKTDPRYTC QREFALKHLP EDETFQLVSK IYKVVPPILT ETGKVKNPWP 400
NVDAHSGVLL QYYGMKEMNY YTVLFGVSRA LGVLASLVWD RALGLPIERP 450
KSFSTDLLVK MVQK 464

Note: No experimental confirmation available.

Length:464
Mass (Da):51,574
Last modified:May 1, 2000 - v1
Checksum:i57D582652931B4F9
GO
Isoform B (identifier: Q9W401-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-13: SLYRISARKLSE → FVRRFGNGSL...ETLNMPDMQD

Note: No experimental confirmation available.

Show »
Length:522
Mass (Da):58,217
Checksum:i7CA9D79350F2764D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 1312SLYRI…RKLSE → FVRRFGNGSLGHHFAFQRRY LAKNSMWDSKSIGTPSSFRM RSKKDNVTGNLKEQQQSATP ETLNMPDMQD in isoform B.
VSP_027491Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014298 Genomic DNA. Translation: AAF46159.1.
AE014298 Genomic DNA. Translation: AAN09169.1.
AY089318 mRNA. Translation: AAL90056.1.
RefSeqiNP_572319.2. NM_132091.2. [Q9W401-1]
NP_727091.1. NM_167072.1. [Q9W401-2]
UniGeneiDm.8.

Genome annotation databases

EnsemblMetazoaiFBtr0070907; FBpp0070872; FBgn0261955. [Q9W401-1]
GeneIDi31579.
KEGGidme:Dmel_CG3861.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014298 Genomic DNA. Translation: AAF46159.1 .
AE014298 Genomic DNA. Translation: AAN09169.1 .
AY089318 mRNA. Translation: AAL90056.1 .
RefSeqi NP_572319.2. NM_132091.2. [Q9W401-1 ]
NP_727091.1. NM_167072.1. [Q9W401-2 ]
UniGenei Dm.8.

3D structure databases

ProteinModelPortali Q9W401.
SMRi Q9W401. Positions 29-462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58066. 3 interactions.
MINTi MINT-936064.
STRINGi 7227.FBpp0070871.

Proteomic databases

PaxDbi Q9W401.
PRIDEi Q9W401.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0070907 ; FBpp0070872 ; FBgn0261955 . [Q9W401-1 ]
GeneIDi 31579.
KEGGi dme:Dmel_CG3861.

Organism-specific databases

CTDi 31579.
FlyBasei FBgn0261955. kdn.

Phylogenomic databases

eggNOGi COG0372.
GeneTreei ENSGT00390000006813.
InParanoidi Q9W401.
KOi K01647.
OMAi ELIYEDC.
OrthoDBi EOG73BVCB.
PhylomeDBi Q9W401.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .
Reactomei REACT_218888. Citric acid cycle (TCA cycle).

Miscellaneous databases

GenomeRNAii 31579.
NextBioi 774282.
PROi Q9W401.

Gene expression databases

Bgeei Q9W401.

Family and domain databases

Gene3Di 1.10.580.10. 1 hit.
InterProi IPR016142. 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 ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
TIGRFAMsi TIGR01793. cit_synth_euk. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Testis.
  4. Cited for: IDENTIFICATION.
  5. "Metabolic disruption in Drosophila bang-sensitive seizure mutants."
    Fergestad T., Bostwick B., Ganetzky B.
    Genetics 173:1357-1364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCISY_DROME
AccessioniPrimary (citable) accession number: Q9W401
Secondary accession number(s): Q8T477
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Mutation of kdn causes a behavioral mutation ('bang sensitivity' = temporarily paralysis in response to a physical jolt). Flies lacking kdn exhibit alterations in neuronal firing patterns in the giant fiber (GF) pathway.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi