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Q91V12 (BACH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionHydrolase
Serine esterase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid catabolic process

Inferred from direct assay Ref.2. Source: MGI

   Cellular_componentcell 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_functionpalmitoyl-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Cytosolic acyl coenzyme A thioester hydrolase
PRO_0000053807

Regions

Domain57 – 15296Acyl coenzyme A hydrolase 1
Domain243 – 32078Acyl coenzyme A hydrolase 2

Sites

Active site671 Ref.9
Active site2561 Ref.9

Amino acid modifications

Modified residue1691N6-acetyllysine By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue2841N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 5959MKLLV…VTMGR → MLTLHRALALRVLRKEVTEA YLREKVKQ in isoform C.
VSP_000157
Alternative sequence1 – 5858MKLLV…CVTMG → MSGPTTDTPAAIQIC in isoform A.
VSP_000158
Alternative sequence1 – 5858MKLLV…CVTMG → MAPPLPSSSMAPPRLIHSGT GLLDTCSQIPPPPPSSAVAA KMSGPTTDTPAAIQIC in isoform D.
VSP_016955

Experimental info

Mutagenesis671N → A: Dramatic reduction in catalytic activity. Ref.9
Mutagenesis2561D → A: Dramatic reduction in catalytic activity. Ref.9
Sequence conflict1861E → D in BAE31092. Ref.4

Secondary structure

.................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform B (mBACHb) [UniParc].

Last modified February 12, 2003. Version 2.
Checksum: 813852DBEB6834C4

FASTA38142,537
        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 

« Hide

Isoform A (mBach) (mBACHa) (43-kDa BACH) [UniParc].

Checksum: E1DB2E445494D477
Show »

FASTA33837,555
Isoform C (mBACHc) [UniParc].

Checksum: 306F06A966F6F40E
Show »

FASTA35039,259
Isoform D (50-kDa BACH) [UniParc].

Checksum: 832431B7D412E6FC
Show »

FASTA37941,616

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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.
RefSeqNP_001139529.1. NM_001146057.1.
NP_001139530.1. NM_001146058.1.
NP_579926.2. NM_133348.2.
UniGeneMm.296191.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q2BX-ray2.50A/B203-381[»]
2V1OX-ray1.78A/B/C/D/E/F59-206[»]
ProteinModelPortalQ91V12.
SMRQ91V12. Positions 55-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213825. 1 interaction.
IntActQ91V12. 3 interactions.
MINTMINT-4089008.

PTM databases

PhosphoSiteQ91V12.

2D gel databases

REPRODUCTION-2DPAGEQ91V12.

Proteomic databases

PaxDbQ91V12.
PRIDEQ91V12.

Protocols and materials databases

DNASU70025.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030779; ENSMUSP00000030779; ENSMUSG00000028937. [Q91V12-1]
ENSMUST00000075363; ENSMUSP00000074827; ENSMUSG00000028937. [Q91V12-4]
ENSMUST00000105652; ENSMUSP00000101277; ENSMUSG00000028937. [Q91V12-3]
GeneID70025.
KEGGmmu:70025.
UCSCuc008vzx.2. mouse. [Q91V12-4]
uc008vzz.2. mouse. [Q91V12-3]
uc008waa.2. mouse. [Q91V12-2]

Organism-specific databases

CTD11332.
MGIMGI:1917275. Acot7.

Phylogenomic databases

eggNOGCOG1607.
GeneTreeENSGT00750000117752.
HOGENOMHOG000007663.
HOVERGENHBG036928.
InParanoidQ91V12.
KOK17360.
OMAANKAALW.
OrthoDBEOG7QZGB2.
PhylomeDBQ91V12.
TreeFamTF329579.

Enzyme and pathway databases

BRENDA3.1.2.2. 3474.
SABIO-RKQ91V12.

Gene expression databases

ArrayExpressQ91V12.
BgeeQ91V12.
CleanExMM_ACOT7.
GenevestigatorQ91V12.

Family and domain databases

InterProIPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ91V12.
NextBio330849.
PROQ91V12.
SOURCESearch...

Entry information

Entry nameBACH_MOUSE
AccessionPrimary (citable) accession number: Q91V12
Secondary accession number(s): A2A8K9 expand/collapse secondary AC list , A2A8L0, A2A8L2, Q3U8C6, Q59HQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot