Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Citrate synthase, mitochondrial

Gene

Cs

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei301 – 3011PROSITE-ProRule annotation
Active sitei347 – 3471PROSITE-ProRule annotation
Active sitei402 – 4021PROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. acetyl-CoA metabolic process Source: RGD
  2. carbohydrate metabolic process Source: UniProtKB
  3. cellular carbohydrate metabolic process Source: InterPro
  4. citrate metabolic process Source: RGD
  5. oxaloacetate metabolic process Source: RGD
  6. tricarboxylic acid cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrial (EC:2.3.3.1)
Alternative name(s):
Citrate (Si)-synthase
Gene namesi
Name:Cs
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620330. Cs.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionBy similarityAdd
BLAST
Chaini28 – 466439Citrate synthase, mitochondrialPRO_0000253899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei76 – 761N6-acetyllysine; alternateBy similarity
Modified residuei76 – 761N6-succinyllysine; alternateBy similarity
Modified residuei103 – 1031N6-succinyllysineBy similarity
Modified residuei193 – 1931N6-succinyllysineBy similarity
Modified residuei321 – 3211N6-acetyllysine; alternateBy similarity
Modified residuei321 – 3211N6-succinyllysine; alternateBy similarity
Modified residuei327 – 3271N6-acetyllysine; alternateBy similarity
Modified residuei327 – 3271N6-succinyllysine; alternateBy similarity
Modified residuei375 – 3751N6-acetyllysine; alternateBy similarity
Modified residuei375 – 3751N6-succinyllysine; alternateBy similarity
Modified residuei382 – 3821N6-acetyllysineBy similarity
Modified residuei393 – 3931N6-acetyllysine; alternateBy similarity
Modified residuei393 – 3931N6-succinyllysine; alternateBy similarity
Modified residuei395 – 3951N6,N6,N6-trimethyllysineBy similarity
Modified residuei450 – 4501N6-succinyllysineBy similarity
Modified residuei459 – 4591N6-acetyllysine; alternateBy similarity
Modified residuei459 – 4591N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiQ8VHF5.
PRIDEiQ8VHF5.

2D gel databases

World-2DPAGE0004:Q8VHF5.

PTM databases

PhosphoSiteiQ8VHF5.

Expressioni

Tissue specificityi

Expressed in the head region and flagellum of epididymal sperm.1 Publication

Gene expression databases

GenevestigatoriQ8VHF5.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ8VHF5. 3 interactions.
MINTiMINT-4609680.

Structurei

3D structure databases

ProteinModelPortaliQ8VHF5.
SMRiQ8VHF5. Positions 28-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiQ8VHF5.
KOiK01647.
PhylomeDBiQ8VHF5.

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]

Sequencei

Sequence statusi: Complete.

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

Q8VHF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLTAAARL LGAKNSSCLV LAARHASASS TNLKDILSNL IPKEQARVKT
60 70 80 90 100
FRQQHGKTVV GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE
110 120 130 140 150
CQKLLPKAKG GEEPLPEGLF WLLVTGQMPT EEQVSWLSQE WAKRAALPSH
160 170 180 190 200
VVTMLDNFPT NLHPMSQLSA AITALNSESN FARAYAEGIN RTKYWELIYE
210 220 230 240 250
DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSKLDWSHNF TNMLCYTEPQ
260 270 280 290 300
FTELMRLYLT IHSDHDGGNV SAHTSHLVGS ALSDTYLSFA AAMNGLAGPL
310 320 330 340 350
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL
360 370 380 390 400
RKTDPRYSCQ REFALKHLPK DPMFKLVAQL YKIVPNILLE QGKAKNPWPN
410 420 430 440 450
VDAHSGVLLQ YYGMTEMNYY TVLFGVSRAL GVLAQLIWSR ALGFPLERPK
460
SMSTDGLMKF VDSKSG
Length:466
Mass (Da):51,867
Last modified:February 28, 2002 - v1
Checksum:iAF8D38379CD38124
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF461496 mRNA. Translation: AAL66372.1.
RefSeqiNP_570111.1. NM_130755.1.
UniGeneiRn.66581.

Genome annotation databases

GeneIDi170587.
KEGGirno:170587.
UCSCiRGD:620330. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF461496 mRNA. Translation: AAL66372.1.
RefSeqiNP_570111.1. NM_130755.1.
UniGeneiRn.66581.

3D structure databases

ProteinModelPortaliQ8VHF5.
SMRiQ8VHF5. Positions 28-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VHF5. 3 interactions.
MINTiMINT-4609680.

PTM databases

PhosphoSiteiQ8VHF5.

2D gel databases

World-2DPAGE0004:Q8VHF5.

Proteomic databases

PaxDbiQ8VHF5.
PRIDEiQ8VHF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi170587.
KEGGirno:170587.
UCSCiRGD:620330. rat.

Organism-specific databases

CTDi1431.
RGDi620330. Cs.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
HOVERGENiHBG005336.
InParanoidiQ8VHF5.
KOiK01647.
PhylomeDBiQ8VHF5.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Miscellaneous databases

NextBioi621088.
PROiQ8VHF5.

Gene expression databases

GenevestigatoriQ8VHF5.

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

  1. "Rattus norvegicus citrate synthase cDNA."
    Rossignol F., Jouaville L., Mounier R., Clottes E.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. Lubec G., Kang S.U.
    Submitted (JUN-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 77-92; 184-191; 209-215; 223-233; 330-340; 383-393 AND 429-440, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
    Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
    Reproduction 138:81-93(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCISY_RAT
AccessioniPrimary (citable) accession number: Q8VHF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2006
Last sequence update: February 28, 2002
Last modified: March 3, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.