Q91V12 (BACH_MOUSE) 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):
Acyl-CoA thioesterase 7
Brain acyl-CoA hydrolase
Short name=BACH
CTE-IIa
Short name=CTE-II
Long chain acyl-CoA thioester hydrolase

Gene names

Name:	Acot7
Synonyms:	Bach

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Has a maximal activity toward palmitoyl-CoA. Ref.2
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subunit structure	Homohexamer. Ref.9
Subcellular location	Isoform A: Cytoplasm Ref.3. Isoform D: Cytoplasm Ref.3.
Tissue specificity	Widely expressed with highest levels in brain. High levels also found in thymus, large intestine and testis. Negligible in muscle and adipose tissue. In the central and peripheral nervous systems, displays a predominantly neuronal localization with highest expression in cell bodies and neurites. Ref.2
Developmental stage	Detected in the brain as early as embryonic day (E) 11.5. The level was low until E12.5, but promptly elevated to a peak 7 days after birth. Thereafter, it declined somewhat and reached a steady-state level in adulthood. These changes in BACH expression were approximately reflected in the palmitoyl-CoA hydrolyzing activity in the developing mouse brain, and the time course was quite similar to that of microtubule-associated protein 2 (MAP2) expression. Induced during embryogenesis in association with neuronal differentiation, and persists after terminal differentiation into neurons in postnatal stages, resulting in the constitutive high expression of BACH in the adult brain in a neuron-specific manner. Ref.8
Induction	Up-Regulated in activated macrophages. Ref.9
Domain	Both hydrolase domains are required for efficient activity.
Sequence similarities	Contains 2 acyl coenzyme A hydrolase domains.
Biophysicochemical properties	Kinetic parameters: KM=16 µM for palmitoyl-CoA (isoform A at 30 degrees Celsius) Ref.3 KM=12 µM for palmitoyl-CoA (isoform D at 30 degrees Celsius)

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Hydrolase Serine esterase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid catabolic process Inferred from direct assay Ref.2. Source: MGI
Cellular_component	cell body Inferred from direct assay Ref.2. Source: MGI cytosol Inferred from direct assay Ref.2. Source: MGI neuron projection Inferred from direct assay Ref.2. Source: MGI
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW palmitoyl-CoA hydrolase activity Inferred from direct assay Ref.2. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform B (identifier: Q91V12-1)

Also known as: mBACHb;

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 A (identifier: Q91V12-2)

Also known as: mBach; mBACHa; 43-kDa BACH;

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

Note: Major isoform.

Isoform C (identifier: Q91V12-3)

Also known as: mBACHc;

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MKLLVGTLRL...KLGHCVTMGR → MLTLHRALALRVLRKEVTEAYLREKVKQ

Isoform D (identifier: Q91V12-4)

Also known as: 50-kDa BACH;

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: MKLLVGTLRL...QKLGHCVTMG → MAPPLPSSSM...TDTPAAIQIC

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_0000053807

Regions

Domain

57 – 152

96

Acyl coenzyme A hydrolase 1

Domain

243 – 320

78

Acyl coenzyme A hydrolase 2

Sites

Active site

67

1

Ref.9

Active site

256

1

Ref.9

Amino acid modifications

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 – 59

59

MKLLV…VTMGR → MLTLHRALALRVLRKEVTEA YLREKVKQ in isoform C.

VSP_000157

Alternative sequence

1 – 58

58

MKLLV…CVTMG → MSGPTTDTPAAIQIC in isoform A.

VSP_000158

Alternative sequence

1 – 58

58

MKLLV…CVTMG → MAPPLPSSSMAPPRLIHSGT GLLDTCSQIPPPPPSSAVAA KMSGPTTDTPAAIQIC in isoform D.

VSP_016955

Experimental info

Mutagenesis

67

1

N → A: Dramatic reduction in catalytic activity. Ref.9

Mutagenesis

256

1

D → A: Dramatic reduction in catalytic activity. Ref.9

Sequence conflict

186

1

E → D in BAE31092. Ref.4

Secondary structure

1

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381

Helix Strand Turn

Details...

Helix

63 – 65

3

Beta strand

70 – 72

3

Helix

74 – 93

20

Turn

94 – 96

3

Beta strand

101 – 108

8

Beta strand

122 – 132

11

Beta strand

137 – 146

10

Turn

148 – 150

3

Beta strand

153 – 170

18

Helix

185 – 201

17

Helix

224 – 227

4

Beta strand

229 – 234

6

Helix

248 – 267

20

Beta strand

272 – 281

10

Beta strand

289 – 301

13

Beta strand

304 – 316

13

Beta strand

324 – 334

11

Helix

353 – 367

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform B (mBACHb) [UniParc]. Last modified February 12, 2003. Version 2. Checksum: 813852DBEB6834C4	FASTA	381	42,537
	10 20 30 40 50 60 MKLLVGTLRL WEVGRQVAFS SLTPGQECSG LRKTFWAAMR AVRTRADHQK LGHCVTMGRI 70 80 90 100 110 120 MRPDDANVAG NVHGGTILKM IEEAGAIIST RHCNSQNGER CVAALARVER TDFLSPMCIG 130 140 150 160 170 180 EVAHVSAEIT YTSKHSVEVQ VHVMSENILT GTKKLTNKAT LWYVPLSLKN VDKVLEVPPI 190 200 210 220 230 240 VYLRQEQEEE GRKRYEAQKL ERMETKWRNG DIVQPVLNPE PNTVSYSQSS LIHLVGPSDC 250 260 270 280 290 300 TLHGFVHGGV TMKLMDEVAG IVAARHCKTN IVTASVDAIN FHDKIRKGCV ITISGRMTFT 310 320 330 340 350 360 SNKSMEIEVL VDADPVVDNS QKRYRAASAF FTYVSLNQEG KPMPVPQLVP ETEDEKKRFE 370 380 EGKGRYLQMK AKRQGHTEPQ P
	Isoform A (mBach) (mBACHa) (43-kDa BACH) [UniParc]. Checksum: E1DB2E445494D477	FASTA	338	37,555
	10 20 30 40 50 60 MSGPTTDTPA AIQICRIMRP DDANVAGNVH GGTILKMIEE AGAIISTRHC NSQNGERCVA 70 80 90 100 110 120 ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVHV MSENILTGTK KLTNKATLWY 130 140 150 160 170 180 VPLSLKNVDK VLEVPPIVYL RQEQEEEGRK RYEAQKLERM ETKWRNGDIV QPVLNPEPNT 190 200 210 220 230 240 VSYSQSSLIH LVGPSDCTLH GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD 250 260 270 280 290 300 KIRKGCVITI SGRMTFTSNK SMEIEVLVDA DPVVDNSQKR YRAASAFFTY VSLNQEGKPM 310 320 330 PVPQLVPETE DEKKRFEEGK GRYLQMKAKR QGHTEPQP
	Isoform C (mBACHc) [UniParc]. Checksum: 306F06A966F6F40E	FASTA	350	39,259
	10 20 30 40 50 60 MLTLHRALAL RVLRKEVTEA YLREKVKQIM RPDDANVAGN VHGGTILKMI EEAGAIISTR 70 80 90 100 110 120 HCNSQNGERC VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV HVMSENILTG 130 140 150 160 170 180 TKKLTNKATL WYVPLSLKNV DKVLEVPPIV YLRQEQEEEG RKRYEAQKLE RMETKWRNGD 190 200 210 220 230 240 IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI VAARHCKTNI 250 260 270 280 290 300 VTASVDAINF HDKIRKGCVI TISGRMTFTS NKSMEIEVLV DADPVVDNSQ KRYRAASAFF 310 320 330 340 350 TYVSLNQEGK PMPVPQLVPE TEDEKKRFEE GKGRYLQMKA KRQGHTEPQP
	Isoform D (50-kDa BACH) [UniParc]. Checksum: 832431B7D412E6FC	FASTA	379	41,616
	10 20 30 40 50 60 MAPPLPSSSM APPRLIHSGT GLLDTCSQIP PPPPSSAVAA KMSGPTTDTP AAIQICRIMR 70 80 90 100 110 120 PDDANVAGNV HGGTILKMIE EAGAIISTRH CNSQNGERCV AALARVERTD FLSPMCIGEV 130 140 150 160 170 180 AHVSAEITYT SKHSVEVQVH VMSENILTGT KKLTNKATLW YVPLSLKNVD KVLEVPPIVY 190 200 210 220 230 240 LRQEQEEEGR KRYEAQKLER METKWRNGDI VQPVLNPEPN TVSYSQSSLI HLVGPSDCTL 250 260 270 280 290 300 HGFVHGGVTM KLMDEVAGIV AARHCKTNIV TASVDAINFH DKIRKGCVIT ISGRMTFTSN 310 320 330 340 350 360 KSMEIEVLVD ADPVVDNSQK RYRAASAFFT YVSLNQEGKP MPVPQLVPET EDEKKRFEEG 370 KGRYLQMKAK RQGHTEPQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human brain acyl-CoA hydrolase isoforms encoded by a single gene." Yamada J., Kuramochi Y., Takagi M., Watanabe T., Suga T. Biochem. Biophys. Res. Commun. 299:49-56(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C). Strain: ICR. Tissue: Brain.
[2]	"Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular cloning and neuronal localization." Kuramochi Y., Takagi-Sakuma M., Kitahara M., Emori R., Asaba Y., Sakaguchi R., Watanabe T., Kuroda J., Hiratsuka K., Nagae Y., Suga T., Yamada J. Brain Res. Mol. Brain Res. 98:81-92(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING. Strain: ICR. Tissue: Brain.
[3]	"A 50-kDa isoform of mouse brain acyl-CoA hydrolase: expression and molecular properties." Takagi M., Kawabe K., Suga T., Yamada J. Arch. Biochem. Biophys. 429:100-105(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. Strain: ICR. Tissue: Brain.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Strain: C57BL/6J. Tissue: Bone marrow.
[5]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[6]	"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 A). Tissue: Colon.
[7]	Lubec G., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 174-184 AND 269-284, MASS SPECTROMETRY. Tissue: Brain and Hippocampus.
[8]	"Expression of acyl-CoA hydrolase in the developing mouse brain." Yamada J., Kuramochi Y., Takagi M., Suga T. Neurosci. Lett. 355:89-92(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[9]	"Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation." Forwood J.K., Thakur A.S., Guncar G., Marfori M., Mouradov D., Meng W., Robinson J., Huber T., Kellie S., Martin J.L., Hume D.A., Kobe B. Proc. Natl. Acad. Sci. U.S.A. 104:10382-10387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 203-381, X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 59-206 (ISOFORM A), SUBUNIT, INDUCTION, MUTAGENESIS OF ASN-67 AND ASP-256, ACTIVE SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB088411 mRNA. Translation: BAC20217.1.
AB088412 mRNA. Translation: BAC20218.1.
AB049821 mRNA. Translation: BAB61731.1.
AB207243 mRNA. Translation: BAD91166.1.
AK152277 mRNA. Translation: BAE31092.1.
AL772240, AL611985, AL671869 Genomic DNA. Translation: CAM19695.1.
AL772240, AL611985, AL671869 Genomic DNA. Translation: CAM19696.1.
AL772240, AL611985, AL671869 Genomic DNA. Translation: CAM19698.1.
AL611985, AL671869, AL772240 Genomic DNA. Translation: CAM23900.1.
AL611985, AL671869, AL772240 Genomic DNA. Translation: CAM23901.1.
AL611985, AL671869, AL772240 Genomic DNA. Translation: CAM23903.1.
AL671869, AL611985, AL772240 Genomic DNA. Translation: CAM26444.1.
AL671869, AL611985, AL772240 Genomic DNA. Translation: CAM26445.1.
AL671869, AL611985, AL772240 Genomic DNA. Translation: CAM26446.1.
BC013507 mRNA. Translation: AAH13507.1.

IPI

IPI00125939.
IPI00230588.
IPI00284094.
IPI00672508.

RefSeq

NP_001139529.1. NM_001146057.1.
NP_001139530.1. NM_001146058.1.
NP_579926.2. NM_133348.2.

UniGene

Mm.296191.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Q2B	X-ray	2.50	A/B	203-381	[»]
2V1O	X-ray	1.78	A/B/C/D/E/F	59-206	[»]

ProteinModelPortal

Q91V12.

SMR

Q91V12. Positions 55-376.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q91V12. 1 interaction.

PTM databases

PhosphoSite

Q91V12.

2D gel databases

REPRODUCTION-2DPAGE

Q91V12.

Proteomic databases

PaxDb

Q91V12.

PRIDE

Q91V12.

Protocols and materials databases

DNASU

70025.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000030779; ENSMUSP00000030779; ENSMUSG00000028937.
ENSMUST00000075363; ENSMUSP00000074827; ENSMUSG00000028937.
ENSMUST00000105652; ENSMUSP00000101277; ENSMUSG00000028937.

GeneID

70025.

KEGG

mmu:70025.

UCSC

uc008vzx.2. mouse.
uc008vzy.2. mouse.
uc008vzz.2. mouse.
uc008waa.2. mouse.

Organism-specific databases

CTD

11332.

MGI

MGI:1917275. Acot7.

Phylogenomic databases

eggNOG

COG1607.

GeneTree

ENSGT00620000087911.

HOGENOM

HOG000007663.

HOVERGEN

HBG036928.

InParanoid

Q91V12.

KO

K01068.

OMA

PDDANIA.

OrthoDB

EOG4JWVF5.

Enzyme and pathway databases

BRENDA

3.1.2.2. 3474.

Gene expression databases

ArrayExpress

Q91V12.

Bgee

Q91V12.

CleanEx

MM_ACOT7.

Genevestigator

Q91V12.

GermOnline

ENSMUSG00000028937. Mus musculus.

Family and domain databases

InterPro

IPR006683. Thioestr_supf.
[Graphical view]

Pfam

PF03061. 4HBT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q91V12.

NextBio

330849.

SOURCE

Search...

Entry information

Entry name

BACH_MOUSE

Accession

Primary (citable) accession number: Q91V12
Secondary accession number(s): A2A8K9 , A2A8L0, A2A8L2, Q3U8C6, Q59HQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	February 12, 2003
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program