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Protein

Cytosolic acyl coenzyme A thioester hydrolase

Gene

Acot7

Organism
Mus musculus (Mouse)
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. Has a maximal activity toward palmitoyl-CoA.1 Publication

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Kineticsi

  1. KM=16 µM for palmitoyl-CoA (isoform A at 30 degrees Celsius)1 Publication
  2. KM=12 µM for palmitoyl-CoA (isoform D at 30 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei67 – 6711 Publication
    Active sitei256 – 25611 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BRENDAi3.1.2.2. 3474.
    SABIO-RKQ91V12.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:Acot7
    Synonyms:Bach
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 4

    Organism-specific databases

    MGIiMGI:1917275. Acot7.

    Subcellular locationi

    GO - Cellular componenti

    • cell body Source: MGI
    • cytoplasm Source: MGI
    • cytosol Source: MGI
    • extracellular exosome Source: MGI
    • neuron projection Source: MGI
    • nucleoplasm Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671N → A: Dramatic reduction in catalytic activity. 1 Publication
    Mutagenesisi256 – 2561D → A: Dramatic reduction in catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 381381Cytosolic acyl coenzyme A thioester hydrolasePRO_0000053807Add
    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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ91V12.
    PaxDbiQ91V12.
    PRIDEiQ91V12.

    2D gel databases

    REPRODUCTION-2DPAGEQ91V12.

    PTM databases

    PhosphoSiteiQ91V12.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Developmental stagei

    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.1 Publication

    Inductioni

    Up-Regulated in activated macrophages.1 Publication

    Gene expression databases

    BgeeiQ91V12.
    CleanExiMM_ACOT7.
    ExpressionAtlasiQ91V12. baseline and differential.
    GenevisibleiQ91V12. MM.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    BioGridi213825. 1 interaction.
    DIPiDIP-54691N.
    IntActiQ91V12. 3 interactions.
    MINTiMINT-4089008.
    STRINGi10090.ENSMUSP00000129121.

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi63 – 653Combined sources
    Beta strandi70 – 723Combined sources
    Helixi74 – 9320Combined sources
    Turni94 – 963Combined sources
    Beta strandi101 – 1088Combined sources
    Beta strandi122 – 13211Combined sources
    Beta strandi137 – 14610Combined sources
    Turni148 – 1503Combined sources
    Beta strandi153 – 17018Combined sources
    Helixi185 – 20117Combined sources
    Helixi224 – 2274Combined sources
    Beta strandi229 – 2346Combined sources
    Helixi248 – 26720Combined sources
    Beta strandi272 – 28110Combined sources
    Beta strandi289 – 30113Combined sources
    Beta strandi304 – 31613Combined sources
    Beta strandi324 – 33411Combined sources
    Helixi353 – 36715Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q2BX-ray2.50A/B203-381[»]
    2V1OX-ray1.78A/B/C/D/E/F59-206[»]
    4ZV3X-ray3.10A/B/C55-369[»]
    ProteinModelPortaliQ91V12.
    SMRiQ91V12. Positions 55-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ91V12.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 15296Acyl coenzyme A hydrolase 1Add
    BLAST
    Domaini243 – 32078Acyl coenzyme A hydrolase 2Add
    BLAST

    Domaini

    Both hydrolase domains are required for efficient activity.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1607.
    GeneTreeiENSGT00760000119297.
    HOGENOMiHOG000007663.
    HOVERGENiHBG036928.
    InParanoidiQ91V12.
    KOiK17360.
    OMAiMFIGEVA.
    OrthoDBiEOG7QZGB2.
    PhylomeDBiQ91V12.
    TreeFamiTF329579.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    InterProiIPR029069. HotDog_dom.
    IPR006683. Thioestr_supf.
    [Graphical view]
    PfamiPF03061. 4HBT. 2 hits.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 2 hits.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform B (identifier: Q91V12-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MKLLVGTLRL WEVGRQVAFS SLTPGQECSG LRKTFWAAMR AVRTRADHQK
    60 70 80 90 100
    LGHCVTMGRI MRPDDANVAG NVHGGTILKM IEEAGAIIST RHCNSQNGER
    110 120 130 140 150
    CVAALARVER TDFLSPMCIG EVAHVSAEIT YTSKHSVEVQ VHVMSENILT
    160 170 180 190 200
    GTKKLTNKAT LWYVPLSLKN VDKVLEVPPI VYLRQEQEEE GRKRYEAQKL
    210 220 230 240 250
    ERMETKWRNG DIVQPVLNPE PNTVSYSQSS LIHLVGPSDC TLHGFVHGGV
    260 270 280 290 300
    TMKLMDEVAG IVAARHCKTN IVTASVDAIN FHDKIRKGCV ITISGRMTFT
    310 320 330 340 350
    SNKSMEIEVL VDADPVVDNS QKRYRAASAF FTYVSLNQEG KPMPVPQLVP
    360 370 380
    ETEDEKKRFE EGKGRYLQMK AKRQGHTEPQ P
    Length:381
    Mass (Da):42,537
    Last modified:February 12, 2003 - v2
    Checksum:i813852DBEB6834C4
    GO
    Isoform A (identifier: Q91V12-2) [UniParc]FASTAAdd to basket

    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.
    Show »
    Length:338
    Mass (Da):37,555
    Checksum:iE1DB2E445494D477
    GO
    Isoform C (identifier: Q91V12-3) [UniParc]FASTAAdd to basket

    Also known as: mBACHc

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

    Show »
    Length:350
    Mass (Da):39,259
    Checksum:i306F06A966F6F40E
    GO
    Isoform D (identifier: Q91V12-4) [UniParc]FASTAAdd to basket

    Also known as: 50-kDa BACH

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

    Show »
    Length:379
    Mass (Da):41,616
    Checksum:i832431B7D412E6FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861E → D in BAE31092 (PubMed:16141072).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5959MKLLV…VTMGR → MLTLHRALALRVLRKEVTEA YLREKVKQ in isoform C. 1 PublicationVSP_000157Add
    BLAST
    Alternative sequencei1 – 5858MKLLV…CVTMG → MSGPTTDTPAAIQIC in isoform A. 3 PublicationsVSP_000158Add
    BLAST
    Alternative sequencei1 – 5858MKLLV…CVTMG → MAPPLPSSSMAPPRLIHSGT GLLDTCSQIPPPPPSSAVAA KMSGPTTDTPAAIQIC in isoform D. 1 PublicationVSP_016955Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS51390.1. [Q91V12-4]
    CCDS51392.1. [Q91V12-3]
    RefSeqiNP_001139529.1. NM_001146057.1.
    NP_001139530.1. NM_001146058.1. [Q91V12-3]
    NP_579926.2. NM_133348.2. [Q91V12-4]
    UniGeneiMm.296191.

    Genome annotation databases

    EnsembliENSMUST00000030779; ENSMUSP00000030779; ENSMUSG00000028937. [Q91V12-1]
    ENSMUST00000075363; ENSMUSP00000074827; ENSMUSG00000028937. [Q91V12-4]
    ENSMUST00000105652; ENSMUSP00000101277; ENSMUSG00000028937. [Q91V12-3]
    GeneIDi70025.
    KEGGimmu:70025.
    UCSCiuc008vzx.2. mouse. [Q91V12-4]
    uc008vzz.2. mouse. [Q91V12-3]
    uc008waa.2. mouse. [Q91V12-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS51390.1. [Q91V12-4]
    CCDS51392.1. [Q91V12-3]
    RefSeqiNP_001139529.1. NM_001146057.1.
    NP_001139530.1. NM_001146058.1. [Q91V12-3]
    NP_579926.2. NM_133348.2. [Q91V12-4]
    UniGeneiMm.296191.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q2BX-ray2.50A/B203-381[»]
    2V1OX-ray1.78A/B/C/D/E/F59-206[»]
    4ZV3X-ray3.10A/B/C55-369[»]
    ProteinModelPortaliQ91V12.
    SMRiQ91V12. Positions 55-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi213825. 1 interaction.
    DIPiDIP-54691N.
    IntActiQ91V12. 3 interactions.
    MINTiMINT-4089008.
    STRINGi10090.ENSMUSP00000129121.

    PTM databases

    PhosphoSiteiQ91V12.

    2D gel databases

    REPRODUCTION-2DPAGEQ91V12.

    Proteomic databases

    MaxQBiQ91V12.
    PaxDbiQ91V12.
    PRIDEiQ91V12.

    Protocols and materials databases

    DNASUi70025.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000030779; ENSMUSP00000030779; ENSMUSG00000028937. [Q91V12-1]
    ENSMUST00000075363; ENSMUSP00000074827; ENSMUSG00000028937. [Q91V12-4]
    ENSMUST00000105652; ENSMUSP00000101277; ENSMUSG00000028937. [Q91V12-3]
    GeneIDi70025.
    KEGGimmu:70025.
    UCSCiuc008vzx.2. mouse. [Q91V12-4]
    uc008vzz.2. mouse. [Q91V12-3]
    uc008waa.2. mouse. [Q91V12-2]

    Organism-specific databases

    CTDi11332.
    MGIiMGI:1917275. Acot7.

    Phylogenomic databases

    eggNOGiCOG1607.
    GeneTreeiENSGT00760000119297.
    HOGENOMiHOG000007663.
    HOVERGENiHBG036928.
    InParanoidiQ91V12.
    KOiK17360.
    OMAiMFIGEVA.
    OrthoDBiEOG7QZGB2.
    PhylomeDBiQ91V12.
    TreeFamiTF329579.

    Enzyme and pathway databases

    BRENDAi3.1.2.2. 3474.
    SABIO-RKQ91V12.

    Miscellaneous databases

    EvolutionaryTraceiQ91V12.
    NextBioi330849.
    PROiQ91V12.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ91V12.
    CleanExiMM_ACOT7.
    ExpressionAtlasiQ91V12. baseline and differential.
    GenevisibleiQ91V12. MM.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    InterProiIPR029069. HotDog_dom.
    IPR006683. Thioestr_supf.
    [Graphical view]
    PfamiPF03061. 4HBT. 2 hits.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. 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.

    Entry informationi

    Entry nameiBACH_MOUSE
    AccessioniPrimary (citable) accession number: Q91V12
    Secondary accession number(s): A2A8K9
    , A2A8L0, A2A8L2, Q3U8C6, Q59HQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: February 12, 2003
    Last modified: July 22, 2015
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.