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Protein

Cytosolic acyl coenzyme A thioester hydrolase

Gene

Acot7

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

Functioni

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18.

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Kineticsi

  1. KM=5.9 µM for palmitoyl-CoA
  1. Vmax=553 µmol/min/mg enzyme with palmitoyl-CoA as substrate

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671By similarity
Active sitei256 – 2561By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.2.2. 5301.
3.1.2.20. 5301.
ReactomeiR-RNO-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKQ64559.

Chemistry

SwissLipidsiSLP:000000586.
SLP:000000614. [Q64559-1]

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic acyl coenzyme A thioester hydrolase (EC:3.1.2.2)
Alternative name(s):
ACH1
ACT
Acyl-CoA thioesterase 7
Brain acyl-CoA hydrolase
Short name:
BACH
CTE-IIa
CTE-IIb
Short name:
CTE-II
LACH1
Long chain acyl-CoA thioester hydrolase
MTE-II
Gene namesi
Name:Acot7
Synonyms:Bach
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi628856. Acot7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • nucleoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Cytosolic acyl coenzyme A thioester hydrolasePRO_0000053808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei284 – 2841N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ64559.
PRIDEiQ64559.

PTM databases

iPTMnetiQ64559.
PhosphoSiteiQ64559.

Expressioni

Tissue specificityi

Isoform 1 is expressed constitutively in brain and testis. Isoform 2 is induced in liver by treatment with the peroxisome proliferator.

Gene expression databases

ExpressionAtlasiQ64559. baseline and differential.
GenevisibleiQ64559. RN.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014213.

Structurei

3D structure databases

ProteinModelPortaliQ64559.
SMRiQ64559. Positions 59-204, 219-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 169119HotDog ACOT-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini225 – 339115HotDog ACOT-type 2PROSITE-ProRule annotationAdd
BLAST

Domaini

Both HotDog ACOT-type hydrolase domains are required for efficient activity.By similarity

Sequence similaritiesi

Contains 2 HotDog ACOT-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2763. Eukaryota.
COG1607. LUCA.
GeneTreeiENSGT00760000119297.
HOGENOMiHOG000007663.
HOVERGENiHBG036928.
InParanoidiQ64559.
KOiK17360.
PhylomeDBiQ64559.
TreeFamiTF329579.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR033120. HOTDOG_ACOT.
IPR029069. HotDog_dom.
IPR006683. Thioestr_dom.
[Graphical view]
PfamiPF03061. 4HBT. 2 hits.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 2 hits.
PROSITEiPS51770. HOTDOG_ACOT. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q64559-2) [UniParc]FASTAAdd to basket

Also known as: LACH1, MTE-II

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKLLARTLYL WEVGRQVASW SLTSGQECLV LRETWWASMR AVRTRAVHHK
60 70 80 90 100
PGHCIAMGRI MRPDDANVAG NVHGGTILKM IEEAGVIIST RHCNSQNGER
110 120 130 140 150
CVAALARVER TDFLSPMCIG EVAHVSAEIT YTSKHSVEVQ VHVLSENILT
160 170 180 190 200
GTKKLTNKAT LWYVPLSLKN VDKVLEVPPI VYLRQEQEEE GRKRYEAQKL
210 220 230 240 250
ERMETKWRNG DIVQPILNPE PNTVSYSQSS LIHLVGPSDC TLHGFVHGGV
260 270 280 290 300
TMKLMDEVAG IVAARHCKTN IVTASVDAIN FHDKIRKGCV ITISGRMTFT
310 320 330 340 350
SNKSMEIEVL VDADPVVDNS QKRYRAASAF FTYVSLNQEG KPLPVPQLVP
360 370 380
ETEDEKKRFE EGKGRYLQMK AKRQGHTEPQ P
Length:381
Mass (Da):42,735
Last modified:January 10, 2006 - v4
Checksum:iF19CB7B34A4BE5D7
GO
Isoform 1 (identifier: Q64559-1) [UniParc]FASTAAdd to basket

Also known as: BACH, CTE-IIa, CTE-II

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: MKLLARTLYLWEVGRQVASWSLTSGQECLVLRETWWASMRAVRTRAVHHKPGHCIAMG → MSGPTTDTPAAIQIC

Show »
Length:338
Mass (Da):37,561
Checksum:i0AF14A2D55DB12A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861V → A in AAC53202 (PubMed:8631842).Curated
Sequence conflicti89 – 891S → R in AAC53202 (PubMed:8631842).Curated
Sequence conflicti144 – 1441L → M in AAC53202 (PubMed:8631842).Curated
Sequence conflicti171 – 1711V → A in BAA19627 (PubMed:9125130).Curated
Sequence conflicti216 – 2161I → V in AAC53202 (PubMed:8631842).Curated
Sequence conflicti279 – 2791I → V in BAA19627 (PubMed:9125130).Curated
Sequence conflicti343 – 3431L → M in AAC53202 (PubMed:8631842).Curated
Sequence conflicti372 – 3721K → N in AAC53202 (PubMed:8631842).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858MKLLA…CIAMG → MSGPTTDTPAAIQIC in isoform 1. 4 PublicationsVSP_016956Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49694 mRNA. Translation: AAC53202.1.
D88890 mRNA. Translation: BAA19626.1.
D88891 mRNA. Translation: BAA19627.2.
Y09332 mRNA. Translation: CAA70512.1.
BC087716 mRNA. Translation: AAH87716.1.
PIRiJC5415.
JC5416.
RefSeqiNP_001139533.1. NM_001146061.1. [Q64559-2]
NP_037346.2. NM_013214.4.
UniGeneiRn.6024.

Genome annotation databases

EnsembliENSRNOT00000014213; ENSRNOP00000014213; ENSRNOG00000010580. [Q64559-2]
GeneIDi26759.
KEGGirno:26759.
UCSCiRGD:628856. rat. [Q64559-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49694 mRNA. Translation: AAC53202.1.
D88890 mRNA. Translation: BAA19626.1.
D88891 mRNA. Translation: BAA19627.2.
Y09332 mRNA. Translation: CAA70512.1.
BC087716 mRNA. Translation: AAH87716.1.
PIRiJC5415.
JC5416.
RefSeqiNP_001139533.1. NM_001146061.1. [Q64559-2]
NP_037346.2. NM_013214.4.
UniGeneiRn.6024.

3D structure databases

ProteinModelPortaliQ64559.
SMRiQ64559. Positions 59-204, 219-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014213.

Chemistry

SwissLipidsiSLP:000000586.
SLP:000000614. [Q64559-1]

PTM databases

iPTMnetiQ64559.
PhosphoSiteiQ64559.

Proteomic databases

PaxDbiQ64559.
PRIDEiQ64559.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014213; ENSRNOP00000014213; ENSRNOG00000010580. [Q64559-2]
GeneIDi26759.
KEGGirno:26759.
UCSCiRGD:628856. rat. [Q64559-2]

Organism-specific databases

CTDi11332.
RGDi628856. Acot7.

Phylogenomic databases

eggNOGiKOG2763. Eukaryota.
COG1607. LUCA.
GeneTreeiENSGT00760000119297.
HOGENOMiHOG000007663.
HOVERGENiHBG036928.
InParanoidiQ64559.
KOiK17360.
PhylomeDBiQ64559.
TreeFamiTF329579.

Enzyme and pathway databases

BRENDAi3.1.2.2. 5301.
3.1.2.20. 5301.
ReactomeiR-RNO-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKQ64559.

Miscellaneous databases

NextBioi608014.
PROiQ64559.

Gene expression databases

ExpressionAtlasiQ64559. baseline and differential.
GenevisibleiQ64559. RN.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR033120. HOTDOG_ACOT.
IPR029069. HotDog_dom.
IPR006683. Thioestr_dom.
[Graphical view]
PfamiPF03061. 4HBT. 2 hits.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 2 hits.
PROSITEiPS51770. HOTDOG_ACOT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of cDNA encoding rat brain cytosolic acyl-coenzyme A thioester hydrolase."
    Broustas C.G., Larkins L.K., Uhler M.D., Hajra A.K.
    J. Biol. Chem. 271:10470-10476(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 306-343.
    Tissue: Brain.
  2. "Molecular cloning and expression of cDNAs encoding rat brain and liver cytosolic long-chain acyl-CoA hydrolases."
    Yamada J., Furihata T., Iida N., Watanabe T., Hosokawa M., Satoh T., Someya A., Nagaoka I., Suga T.
    Biochem. Biophys. Res. Commun. 232:198-203(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 60-72; 256-264; 315-343 AND 370-380.
    Strain: Sprague-Dawley.
    Tissue: Brain and Liver.
  3. Yamada J., Furihata T., Iida N., Watanabe T., Hosokawa M., Satoh T., Someya A., Nagaoka I., Suga T.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS (ISOFORM 2).
  4. "Peroxisome proliferator-induced acyl-CoA thioesterase from rat liver cytosol: molecular cloning and functional expression in Chinese hamster ovary cells."
    Engberg S.T., Aoyama T., Alexson S.E.H., Hashimoto T., Svensson L.T.
    Biochem. J. 323:525-531(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. "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] (ISOFORM 1).
    Tissue: Brain.
  6. Lubec G., Diao W., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 135-153 AND 173-184 (ISOFORMS 1/2), IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  7. "Purification and properties of long-chain acyl-CoA hydrolases from the liver cytosol of rats treated with peroxisome proliferator."
    Yamada J., Matsumoto I., Furihata T., Sakuma M., Suga T.
    Arch. Biochem. Biophys. 308:118-125(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism."
    Hunt M.C., Alexson S.E.H.
    Prog. Lipid Res. 41:99-130(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBACH_RAT
AccessioniPrimary (citable) accession number: Q64559
Secondary accession number(s): O08652, O09041
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 10, 2006
Last modified: May 11, 2016
This is version 124 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

These proteins have been named according to their molecular weight (see PubMed:11755680): BACH (also called CTE-IIa and CTE-II), LACH1 (also called MTE-II) and ACT (also called CTE-IIb). It is unknown whether ACT corresponds to another isoform.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.