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Protein

Acyl-coenzyme A thioesterase 12

Gene

Acot12

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

Functioni

Hydrolyzes acetyl-CoA to acetate and CoA.

Catalytic activityi

Acetyl-CoA + H2O = CoA + acetate.

Enzyme regulationi

Allosterically regulated by ATP (activator) and ADP (inhibitor).

Pathwayi: pyruvate metabolism

This protein is involved in the pathway pyruvate metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway pyruvate metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei145Coenzyme ABy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Hydrolase, Serine esterase
Biological processFatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.2.1 5301
SABIO-RKQ99NB7
UniPathwayiUPA00231

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 12 (EC:3.1.2.1)
Short name:
Acyl-CoA thioesterase 12
Alternative name(s):
Acyl-CoA thioester hydrolase 12
Cytoplasmic acetyl-CoA hydrolase 1
Short name:
CACH-1
Short name:
rACH
Short name:
rCACH-1
Gene namesi
Name:Acot12
Synonyms:Cach, Cach1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619752 Acot12

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000538111 – 556Acyl-coenzyme A thioesterase 12Add BLAST556

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34N6-succinyllysineBy similarity1
Modified residuei97N6-succinyllysineBy similarity1
Modified residuei160N6-succinyllysineBy similarity1
Modified residuei229N6-succinyllysineBy similarity1

Proteomic databases

PaxDbiQ99NB7
PRIDEiQ99NB7

Expressioni

Inductioni

By 2-(p-chlorophenoxy)isobutyric acid (CPIB).

Interactioni

Subunit structurei

Active homodimer or homotetramer at room temperature and inactive monomer at low temperature.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021675

Structurei

3D structure databases

ProteinModelPortaliQ99NB7
SMRiQ99NB7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 118HotDog ACOT-type 1PROSITE-ProRule annotationAdd BLAST113
Domaini180 – 295HotDog ACOT-type 2PROSITE-ProRule annotationAdd BLAST116
Domaini341 – 550STARTPROSITE-ProRule annotationAdd BLAST210

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 56Coenzyme A bindingBy similarity3
Regioni83 – 85Coenzyme A bindingBy similarity3
Regioni235 – 237Coenzyme A bindingBy similarity3

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2763 Eukaryota
COG1607 LUCA
HOGENOMiHOG000232032
HOVERGENiHBG023847
InParanoidiQ99NB7
KOiK01067
PhylomeDBiQ99NB7

Family and domain databases

Gene3Di3.30.530.20, 1 hit
InterProiView protein in InterPro
IPR033120 HOTDOG_ACOT
IPR029069 HotDog_dom_sf
IPR023393 START-like_dom_sf
IPR002913 START_lipid-bd_dom
IPR006683 Thioestr_dom
PfamiView protein in Pfam
PF03061 4HBT, 2 hits
PF01852 START, 1 hit
SMARTiView protein in SMART
SM00234 START, 1 hit
SUPFAMiSSF54637 SSF54637, 2 hits
PROSITEiView protein in PROSITE
PS51770 HOTDOG_ACOT, 2 hits
PS50848 START, 1 hit

Sequencei

Sequence statusi: Complete.

Q99NB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPTVAPGEV LMSQAIQPAH ADSRGELSAG QLLKWMDTTA CLAAEKHAGI
60 70 80 90 100
SCVTASMDDI LFEDTARIGQ IVTIRAKVTR AFSTSMEISI KVRVQDKFTG
110 120 130 140 150
IQKLLCVAFS TFVVKPLGKE KVHLKPVLLQ TEQEQVEHRL ASERRKVRLQ
160 170 180 190 200
HENTFSNIMK ESNWLRDPVC NEEEGTATTM ATSVQSIELV LPPHANHHGN
210 220 230 240 250
TFGGQIMAWM ETVATISASR LCHGHPFLKS VDMFKFRGPS TVGDRLVFNA
260 270 280 290 300
IVNNTFQNSV EVGVRVEAFD CREWAEGQGR HINSAFLIYN AVDDQEELIT
310 320 330 340 350
FPRIQPISKD DFRRYQGAIA RRRIRLGRKY VISHKKEVPL GTQWDISKKG
360 370 380 390 400
SISNTNVEAL KNLASKSGWE ITTTLEKIKI YTLEEQDAIS VKVEKQVGSP
410 420 430 440 450
ARVAYHLLSD FTKRPLWDPH YISCEVIDQV SEDDQIYYIT CSVVNGDKPK
460 470 480 490 500
DFVVLVSQRK PLKDDNTYIV ALMSVVLPSV PPSPQYIRSQ VICAGFLIQP
510 520 530 540 550
VDSSSCTVAY LNQMSDSILP YFAGNIGGWS KSIEEAAASC IKFIENATHD

GLKSVL
Length:556
Mass (Da):62,018
Last modified:June 1, 2001 - v1
Checksum:i81E592F066AB0C9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040609 mRNA Translation: BAB39852.1
RefSeqiNP_570103.1, NM_130747.1
UniGeneiRn.212205

Genome annotation databases

GeneIDi170570
KEGGirno:170570
UCSCiRGD:619752 rat

Similar proteinsi

Entry informationi

Entry nameiACO12_RAT
AccessioniPrimary (citable) accession number: Q99NB7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2001
Last modified: May 23, 2018
This is version 108 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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