Q64559 (BACH_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Acot7
Synonyms:	Bach

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subunit structure	Homohexamer By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	Isoform 1 is expressed constitutively in brain and testis. Isoform 2 is induced in liver by treatment with the peroxisome proliferator.
Domain	Both hydrolase domains are required for efficient activity By similarity.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Contains 2 acyl coenzyme A hydrolase domains.
Caution	These proteins have been named according to their molecular weight (see Ref.8): 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.
Biophysicochemical properties	Kinetic parameters: KM=5.9 µM for palmitoyl-CoA Vmax=553 µmol/min/mg enzyme with palmitoyl-CoA as substrate

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Hydrolase Serine esterase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytosol Inferred from direct assay Ref.4. Source: RGD
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW palmitoyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q64559-2)

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.

Isoform 1 (identifier: Q64559-1)

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

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 381	381	Cytosolic acyl coenzyme A thioester hydrolase		PRO_0000053808
Regions
	Domain	57 – 152	96	Acyl coenzyme A hydrolase 1
	Domain	243 – 320	78	Acyl coenzyme A hydrolase 2
Sites
	Active site	67	1	By similarity
	Active site	256	1	By similarity
Amino acid modifications
	Modified residue	79	1	N6-acetyllysine By similarity
	Modified residue	169	1	N6-acetyllysine By similarity
	Modified residue	199	1	N6-acetyllysine By similarity
	Modified residue	284	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1 – 58	58	MKLLA…CIAMG → MSGPTTDTPAAIQIC in isoform 1.		VSP_016956
Experimental info
	Sequence conflict	86	1	V → A in AAC53202. Ref.1
	Sequence conflict	89	1	S → R in AAC53202. Ref.1
	Sequence conflict	144	1	L → M in AAC53202. Ref.1
	Sequence conflict	171	1	V → A in BAA19627. Ref.2
	Sequence conflict	216	1	I → V in AAC53202. Ref.1
	Sequence conflict	279	1	I → V in BAA19627. Ref.2
	Sequence conflict	343	1	L → M in AAC53202. Ref.1
	Sequence conflict	372	1	K → N in AAC53202. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (LACH1) (MTE-II) [UniParc]. Last modified January 10, 2006. Version 4. Checksum: F19CB7B34A4BE5D7	FASTA	381	42,735
	10 20 30 40 50 60 MKLLARTLYL WEVGRQVASW SLTSGQECLV LRETWWASMR AVRTRAVHHK PGHCIAMGRI 70 80 90 100 110 120 MRPDDANVAG NVHGGTILKM IEEAGVIIST RHCNSQNGER CVAALARVER TDFLSPMCIG 130 140 150 160 170 180 EVAHVSAEIT YTSKHSVEVQ VHVLSENILT GTKKLTNKAT LWYVPLSLKN VDKVLEVPPI 190 200 210 220 230 240 VYLRQEQEEE GRKRYEAQKL ERMETKWRNG DIVQPILNPE PNTVSYSQSS LIHLVGPSDC 250 260 270 280 290 300 TLHGFVHGGV TMKLMDEVAG IVAARHCKTN IVTASVDAIN FHDKIRKGCV ITISGRMTFT 310 320 330 340 350 360 SNKSMEIEVL VDADPVVDNS QKRYRAASAF FTYVSLNQEG KPLPVPQLVP ETEDEKKRFE 370 380 EGKGRYLQMK AKRQGHTEPQ P
	Isoform 1 (BACH) (CTE-IIa) (CTE-II) [UniParc]. Checksum: 0AF14A2D55DB12A2	FASTA	338	37,561
	10 20 30 40 50 60 MSGPTTDTPA AIQICRIMRP DDANVAGNVH GGTILKMIEE AGVIISTRHC NSQNGERCVA 70 80 90 100 110 120 ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVHV LSENILTGTK KLTNKATLWY 130 140 150 160 170 180 VPLSLKNVDK VLEVPPIVYL RQEQEEEGRK RYEAQKLERM ETKWRNGDIV QPILNPEPNT 190 200 210 220 230 240 VSYSQSSLIH LVGPSDCTLH GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD 250 260 270 280 290 300 KIRKGCVITI SGRMTFTSNK SMEIEVLVDA DPVVDNSQKR YRAASAFFTY VSLNQEGKPL 310 320 330 PVPQLVPETE DEKKRFEEGK GRYLQMKAKR QGHTEPQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8631842] [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: 9125130] [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: 9163348] [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: 15489334] [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), 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: 7906114] [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: 11755680] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00213571. IPI00326904.
PIR	JC5415. JC5416.
RefSeq	NP_001139533.1. NM_001146061.1. NP_037346.2. NM_013214.4.
UniGene	Rn.6024.
3D structure databases
ProteinModelPortal	Q64559.
SMR	Q64559. Positions 59-204, 219-376.
ModBase	Search...
Protein-protein interaction databases
STRING	Q64559.
PTM databases
PhosphoSite	Q64559.
Proteomic databases
PRIDE	Q64559.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014213; ENSRNOP00000014213; ENSRNOG00000010580.
GeneID	26759.
KEGG	rno:26759.
UCSC	D88891. rat.
Organism-specific databases
CTD	11332.
RGD	628856. Acot7.
Phylogenomic databases
eggNOG	roNOG15499.
GeneTree	ENSGT00390000000934.
HOVERGEN	HBG036928.
InParanoid	Q64559.
Enzyme and pathway databases
BRENDA	3.1.2.2. 5301.
Gene expression databases
ArrayExpress	Q64559.
Genevestigator	Q64559.
GermOnline	ENSRNOG00000010580. Rattus norvegicus.
Family and domain databases
InterPro	IPR006683. Thioestr_supf. [Graphical view]
KO	K01068.
Pfam	PF03061. 4HBT. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	608014.

Entry information

Entry name

BACH_RAT

Accession

Primary (citable) accession number: Q64559
Secondary accession number(s): O08652, O09041

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 10, 2006
Last modified:	January 25, 2012
This is version 94 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program