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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

  1. carboxylic ester hydrolase activity Source: UniProtKB-KW
  2. fatty-acyl-CoA binding Source: MGI
  3. long-chain fatty acyl-CoA binding Source: MGI
  4. palmitoyl-CoA hydrolase activity Source: MGI
  5. protein homodimerization activity Source: MGI

GO - Biological processi

  1. coenzyme A biosynthetic process Source: MGI
  2. fatty acid catabolic process Source: MGI
  3. long-chain fatty-acyl-CoA catabolic process Source: MGI
  4. medium-chain fatty acid biosynthetic process Source: MGI
  5. medium-chain fatty-acyl-CoA catabolic process Source: MGI
  6. palmitic acid biosynthetic process Source: MGI
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

  1. cell body Source: MGI
  2. cytoplasm Source: MGI
  3. cytosol Source: MGI
  4. extracellular vesicular exosome Source: MGI
  5. neuron projection Source: MGI
  6. 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.
GenevestigatoriQ91V12.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

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

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[»]
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[»]
ProteinModelPortaliQ91V12.
SMRiQ91V12. Positions 55-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

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.
GenevestigatoriQ91V12.

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(2001) [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(2001) [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(2003) [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(2004) [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(2003) [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 (JUN-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(2003) [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(2006) [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: March 4, 2015
This is version 118 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.