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Protein

Acetyl-CoA acetyltransferase, cytosolic

Gene

Acat2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediateBy similarity
Active sitei353 – 3531Proton acceptorPROSITE-ProRule annotation
Active sitei383 – 3831Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  • acetyl-CoA C-acetyltransferase activity Source: RGD

GO - Biological processi

  • brain development Source: RGD
  • cellular response to fatty acid Source: RGD
  • cellular response to nutrient Source: RGD
  • ketone body catabolic process Source: RGD
  • liver development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

SABIO-RKQ5XI22.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase, cytosolic (EC:2.3.1.9)
Alternative name(s):
Cytosolic acetoacetyl-CoA thiolase
Gene namesi
Name:Acat2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1359366. Acat2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Acetyl-CoA acetyltransferase, cytosolicPRO_0000271366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei200 – 2001N6-acetyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei235 – 2351N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ5XI22.
PRIDEiQ5XI22.

PTM databases

PhosphoSiteiQ5XI22.

Expressioni

Gene expression databases

GenevisibleiQ5XI22. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059561.

Structurei

3D structure databases

ProteinModelPortaliQ5XI22.
SMRiQ5XI22. Positions 4-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Phylogenomic databases

eggNOGiCOG0183.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ5XI22.
KOiK00626.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5XI22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAGSDPVVI ISAARTAIGS FNGALSTVPV HNLGTTVIKE VLQRAKVAPE
60 70 80 90 100
EVSEVIFGHV LTAGCGQNPT RQASVGAGIP YSVPAWSCQM ICGSGLKAVC
110 120 130 140 150
LAAQSIAMGD STIVVAGGME NMSKAPHLAH LRSGVKMGEV PLADSILCDG
160 170 180 190 200
LTDAFHNYHM GITAENVAKK WQVSREAQDK VAVVSQNRAE HAQKAGHFDK
210 220 230 240 250
EIVPVHVSSR KGLTEVKIDE FPRHGSNLEA MSKLKPYFLT DGTGTVTPAN
260 270 280 290 300
ASGMNDGAAA VVLMKKTEAE SRMLKPLAQV VSWSQAGVEP SVMGVGPIPA
310 320 330 340 350
IKQAVAKAGW SLEDVDVFEI NEAFAAVSAA IAKELGLSPE KVNIDGGAIA
360 370 380 390
LGHPLGASGC RILVTLLHTL ERVGGTRGVA ALCIGGGMGI AMCVQRG
Length:397
Mass (Da):41,108
Last modified:November 23, 2004 - v1
Checksum:i850589DD5AF4D84F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083872 mRNA. Translation: AAH83872.1.
RefSeqiNP_001006996.1. NM_001006995.1.
UniGeneiRn.203063.

Genome annotation databases

GeneIDi308100.
KEGGirno:308100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083872 mRNA. Translation: AAH83872.1.
RefSeqiNP_001006996.1. NM_001006995.1.
UniGeneiRn.203063.

3D structure databases

ProteinModelPortaliQ5XI22.
SMRiQ5XI22. Positions 4-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059561.

PTM databases

PhosphoSiteiQ5XI22.

Proteomic databases

PaxDbiQ5XI22.
PRIDEiQ5XI22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi308100.
KEGGirno:308100.

Organism-specific databases

CTDi39.
RGDi1359366. Acat2.

Phylogenomic databases

eggNOGiCOG0183.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ5XI22.
KOiK00626.

Enzyme and pathway databases

SABIO-RKQ5XI22.

Miscellaneous databases

NextBioi658342.
PROiQ5XI22.

Gene expression databases

GenevisibleiQ5XI22. RN.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTHIC_RAT
AccessioniPrimary (citable) accession number: Q5XI22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 23, 2004
Last modified: June 24, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.