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Q5XI22

- THIC_RAT

UniProt

Q5XI22 - THIC_RAT

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Protein
Acetyl-CoA acetyltransferase, cytosolic
Gene
Acat2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediate By similarity
Active sitei353 – 3531Proton acceptor By similarity
Active sitei383 – 3831Proton acceptor By similarity

GO - Molecular functioni

  1. acetyl-CoA C-acetyltransferase activity Source: RGD

GO - Biological processi

  1. brain development Source: RGD
  2. cellular response to fatty acid Source: RGD
  3. cellular response to nutrient Source: RGD
  4. ketone body catabolic process Source: RGD
  5. 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: Unplaced

Organism-specific databases

RGDi1359366. Acat2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Acetyl-CoA acetyltransferase, cytosolic
PRO_0000271366Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ5XI22.
PRIDEiQ5XI22.

PTM databases

PhosphoSiteiQ5XI22.

Expressioni

Gene expression databases

GenevestigatoriQ5XI22.

Interactioni

Subunit structurei

Homotetramer By similarity.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018934.

Structurei

3D structure databases

ProteinModelPortaliQ5XI22.
SMRiQ5XI22. Positions 4-396.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.

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

MNAGSDPVVI ISAARTAIGS FNGALSTVPV HNLGTTVIKE VLQRAKVAPE    50
EVSEVIFGHV LTAGCGQNPT RQASVGAGIP YSVPAWSCQM ICGSGLKAVC 100
LAAQSIAMGD STIVVAGGME NMSKAPHLAH LRSGVKMGEV PLADSILCDG 150
LTDAFHNYHM GITAENVAKK WQVSREAQDK VAVVSQNRAE HAQKAGHFDK 200
EIVPVHVSSR KGLTEVKIDE FPRHGSNLEA MSKLKPYFLT DGTGTVTPAN 250
ASGMNDGAAA VVLMKKTEAE SRMLKPLAQV VSWSQAGVEP SVMGVGPIPA 300
IKQAVAKAGW SLEDVDVFEI NEAFAAVSAA IAKELGLSPE KVNIDGGAIA 350
LGHPLGASGC RILVTLLHTL ERVGGTRGVA ALCIGGGMGI AMCVQRG 397
Length:397
Mass (Da):41,108
Last modified:November 23, 2004 - v1
Checksum:i850589DD5AF4D84F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BC083872 mRNA. Translation: AAH83872.1 .
RefSeqi NP_001006996.1. NM_001006995.1.
UniGenei Rn.203063.

3D structure databases

ProteinModelPortali Q5XI22.
SMRi Q5XI22. Positions 4-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000018934.

PTM databases

PhosphoSitei Q5XI22.

Proteomic databases

PaxDbi Q5XI22.
PRIDEi Q5XI22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 308100.
KEGGi rno:308100.

Organism-specific databases

CTDi 39.
RGDi 1359366. Acat2.

Phylogenomic databases

eggNOGi COG0183.
HOGENOMi HOG000012238.
HOVERGENi HBG003112.
InParanoidi Q5XI22.
KOi K00626.

Enzyme and pathway databases

SABIO-RK Q5XI22.

Miscellaneous databases

NextBioi 658342.
PROi Q5XI22.

Gene expression databases

Genevestigatori Q5XI22.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 11, 2014
This is version 80 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

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