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Q8VHF5 (CISY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Citrate synthase, mitochondrial
EC=2.3.3.1
Gene names
Name:Cs
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Tissue specificity

Expressed in the head region and flagellum of epididymal sperm. Ref.3

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 466439Citrate synthase, mitochondrial
PRO_0000253899

Sites

Active site3011 By similarity
Active site3471 By similarity
Active site4021 By similarity

Amino acid modifications

Modified residue761N6-acetyllysine; alternate By similarity
Modified residue761N6-succinyllysine; alternate By similarity
Modified residue3271N6-acetyllysine By similarity
Modified residue3751N6-acetyllysine By similarity
Modified residue3821N6-acetyllysine By similarity
Modified residue3931N6-acetyllysine By similarity
Modified residue3951N6,N6,N6-trimethyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VHF5 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: AF8D38379CD38124

FASTA46651,867
        10         20         30         40         50         60 
MALLTAAARL LGAKNSSCLV LAARHASASS TNLKDILSNL IPKEQARVKT FRQQHGKTVV 

        70         80         90        100        110        120 
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKLLPKAKG GEEPLPEGLF 

       130        140        150        160        170        180 
WLLVTGQMPT EEQVSWLSQE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AITALNSESN 

       190        200        210        220        230        240 
FARAYAEGIN RTKYWELIYE DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSKLDWSHNF 

       250        260        270        280        290        300 
TNMLCYTEPQ FTELMRLYLT IHSDHDGGNV SAHTSHLVGS ALSDTYLSFA AAMNGLAGPL 

       310        320        330        340        350        360 
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYSCQ 

       370        380        390        400        410        420 
REFALKHLPK DPMFKLVAQL YKIVPNILLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY 

       430        440        450        460 
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLMKF VDSKSG

« Hide

References

[1]"Rattus norvegicus citrate synthase cDNA."
Rossignol F., Jouaville L., Mounier R., Clottes E.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]Lubec G., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 77-92; 184-191; 209-215; 223-233; 330-340; 383-393 AND 429-440, 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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF461496 mRNA. Translation: AAL66372.1.
IPIIPI00206977.
RefSeqNP_570111.1. NM_130755.1.
UniGeneRn.231876.

3D structure databases

ProteinModelPortalQ8VHF5.
SMRQ8VHF5. Positions 28-464.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8VHF5. 2 interactions.
MINTMINT-4609680.

PTM databases

PhosphoSiteQ8VHF5.

2D gel databases

World-2DPAGE0004:Q8VHF5.

Proteomic databases

PaxDbQ8VHF5.
PRIDEQ8VHF5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID170587.
KEGGrno:170587.
UCSCRGD:620330. rat.

Organism-specific databases

CTD1431.
RGD620330. Cs.

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000130831.
HOVERGENHBG005336.
InParanoidQ8VHF5.
KOK01647.
OrthoDBEOG4FBHSR.

Enzyme and pathway databases

UniPathwayUPA00223; UER00717.

Gene expression databases

GenevestigatorQ8VHF5.
GermOnlineENSRNOG00000023520. Rattus norvegicus.

Family and domain databases

Gene3D1.10.580.10. 1 hit.
InterProIPR016142. 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]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. Citrate_synthase_core. 1 hit.
TIGRFAMsTIGR01793. cit_synth_euk. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621088.

Entry information

Entry nameCISY_RAT
AccessionPrimary (citable) accession number: Q8VHF5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 1, 2002
Last modified: May 29, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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