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Q5XI22 (THIC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA acetyltransferase, cytosolic

EC=2.3.1.9
Alternative name(s):
Cytosolic acetoacetyl-CoA thiolase
Gene names
Name:Acat2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the thiolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Acetyl-CoA acetyltransferase, cytosolic
PRO_0000271366

Sites

Active site921Acyl-thioester intermediate By similarity
Active site3531Proton acceptor By similarity
Active site3831Proton acceptor By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2001N6-acetyllysine By similarity
Modified residue2331N6-acetyllysine By similarity
Modified residue2351N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XI22 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 850589DD5AF4D84F

FASTA39741,108
        10         20         30         40         50         60 
MNAGSDPVVI ISAARTAIGS FNGALSTVPV HNLGTTVIKE VLQRAKVAPE EVSEVIFGHV 

        70         80         90        100        110        120 
LTAGCGQNPT RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAAQSIAMGD STIVVAGGME 

       130        140        150        160        170        180 
NMSKAPHLAH LRSGVKMGEV PLADSILCDG LTDAFHNYHM GITAENVAKK WQVSREAQDK 

       190        200        210        220        230        240 
VAVVSQNRAE HAQKAGHFDK EIVPVHVSSR KGLTEVKIDE FPRHGSNLEA MSKLKPYFLT 

       250        260        270        280        290        300 
DGTGTVTPAN ASGMNDGAAA VVLMKKTEAE SRMLKPLAQV VSWSQAGVEP SVMGVGPIPA 

       310        320        330        340        350        360 
IKQAVAKAGW SLEDVDVFEI NEAFAAVSAA IAKELGLSPE KVNIDGGAIA LGHPLGASGC 

       370        380        390 
RILVTLLHTL ERVGGTRGVA ALCIGGGMGI AMCVQRG 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 16-39; 195-210; 218-223 AND 342-372, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC083872 mRNA. Translation: AAH83872.1.
RefSeqNP_001006996.1. NM_001006995.1.
UniGeneRn.203063.

3D structure databases

ProteinModelPortalQ5XI22.
SMRQ5XI22. Positions 4-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000018934.

PTM databases

PhosphoSiteQ5XI22.

Proteomic databases

PaxDbQ5XI22.
PRIDEQ5XI22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID308100.
KEGGrno:308100.

Organism-specific databases

CTD39.
RGD1359366. Acat2.

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHOG000012238.
HOVERGENHBG003112.
InParanoidQ5XI22.
KOK00626.

Enzyme and pathway databases

SABIO-RKQ5XI22.

Gene expression databases

GenevestigatorQ5XI22.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio658342.
PROQ5XI22.

Entry information

Entry nameTHIC_RAT
AccessionPrimary (citable) accession number: Q5XI22
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 23, 2004
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families