ACOT6_MOUSE
ID ACOT6_MOUSE Reviewed; 419 AA.
AC Q32Q92; Q3TQG7; Q8BXE0; Q8BYI3; Q99LZ0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Acyl-coenzyme A thioesterase 6 {ECO:0000305|PubMed:17613526};
DE Short=Acyl-CoA thioesterase 6 {ECO:0000305|PubMed:17613526};
DE EC=3.1.2.- {ECO:0000269|PubMed:17613526};
GN Name=Acot6 {ECO:0000312|MGI:MGI:1921287};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=17613526; DOI=10.1074/jbc.m703718200;
RA Westin M.A.K., Hunt M.C., Alexson S.E.H.;
RT "Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase
RT acting as a novel auxiliary enzyme in alpha- and beta-oxidation of methyl-
RT branched fatty acids in mouse.";
RL J. Biol. Chem. 282:26707-26716(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 63-419 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Cerebellum, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels. Catalyzes the hydrolysis of phytanoyl-CoA and pristanoyl-CoA,
CC two methyl-branched fatty acids derived from phytol, that enter the
CC body via the diet. {ECO:0000269|PubMed:17613526}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pristanoyl-CoA = 2,6,10,14-tetramethylpentadecanoate +
CC CoA + H(+); Xref=Rhea:RHEA:40415, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:77250,
CC ChEBI:CHEBI:77268; Evidence={ECO:0000269|PubMed:17613526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40416;
CC Evidence={ECO:0000305|PubMed:17613526};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phytanoyl-CoA = 3,7,11,15-tetramethylhexadecanoate + CoA
CC + H(+); Xref=Rhea:RHEA:40419, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37257, ChEBI:CHEBI:57287, ChEBI:CHEBI:57391;
CC Evidence={ECO:0000269|PubMed:17613526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40420;
CC Evidence={ECO:0000305|PubMed:17613526};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for pristanoyl-CoA {ECO:0000269|PubMed:17613526};
CC Vmax=3.2 umol/min/mg enzyme with pristanoyl-CoA as substrate
CC {ECO:0000269|PubMed:17613526};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:17613526}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17613526}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q32Q92-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32Q92-2; Sequence=VSP_028234, VSP_028235;
CC -!- TISSUE SPECIFICITY: Highly expressed in white adipose tissue. Detected
CC at lower levels in kidney, liver, brown adipose tissue and brain.
CC {ECO:0000269|PubMed:17613526}.
CC -!- INDUCTION: Up-regulated in liver upon treatment with peroxisome
CC proliferator. {ECO:0000269|PubMed:17613526}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30372.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC33071.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE37416.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Small insertion of unknown origin.; Evidence={ECO:0000305};
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DR EMBL; AY999300; AAY45894.1; -; mRNA.
DR EMBL; AK039518; BAC30372.1; ALT_INIT; mRNA.
DR EMBL; AK047479; BAC33071.1; ALT_FRAME; mRNA.
DR EMBL; AK135361; BAE22505.1; -; mRNA.
DR EMBL; AK163605; BAE37416.1; ALT_SEQ; mRNA.
DR EMBL; BC002159; AAH02159.1; -; mRNA.
DR CCDS; CCDS26038.1; -. [Q32Q92-1]
DR RefSeq; NP_766168.1; NM_172580.1. [Q32Q92-1]
DR AlphaFoldDB; Q32Q92; -.
DR SMR; Q32Q92; -.
DR STRING; 10090.ENSMUSP00000056131; -.
DR SwissLipids; SLP:000000558; -.
DR ESTHER; mouse-ACOT6; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A61; -.
DR iPTMnet; Q32Q92; -.
DR PhosphoSitePlus; Q32Q92; -.
DR jPOST; Q32Q92; -.
DR MaxQB; Q32Q92; -.
DR PaxDb; Q32Q92; -.
DR PRIDE; Q32Q92; -.
DR ProteomicsDB; 285652; -. [Q32Q92-1]
DR ProteomicsDB; 285653; -. [Q32Q92-2]
DR Antibodypedia; 63322; 49 antibodies from 17 providers.
DR Ensembl; ENSMUST00000056822; ENSMUSP00000056131; ENSMUSG00000043487. [Q32Q92-1]
DR Ensembl; ENSMUST00000222921; ENSMUSP00000152129; ENSMUSG00000043487. [Q32Q92-2]
DR GeneID; 217700; -.
DR KEGG; mmu:217700; -.
DR UCSC; uc007oei.1; mouse. [Q32Q92-1]
DR UCSC; uc007oej.2; mouse. [Q32Q92-2]
DR CTD; 641372; -.
DR MGI; MGI:1921287; Acot6.
DR VEuPathDB; HostDB:ENSMUSG00000043487; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q32Q92; -.
DR OMA; AWQRIQT; -.
DR PhylomeDB; Q32Q92; -.
DR TreeFam; TF314911; -.
DR Reactome; R-MMU-390247; Beta-oxidation of very long chain fatty acids.
DR SABIO-RK; Q32Q92; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 217700; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q32Q92; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q32Q92; protein.
DR Bgee; ENSMUSG00000043487; Expressed in cranial cartilage and 208 other tissues.
DR ExpressionAtlas; Q32Q92; baseline and differential.
DR Genevisible; Q32Q92; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; TAS:HGNC-UCL.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Peroxisome; Reference proteome; Serine esterase.
FT CHAIN 1..419
FT /note="Acyl-coenzyme A thioesterase 6"
FT /id="PRO_0000305099"
FT MOTIF 417..419
FT /note="Peroxisome targeting signal"
FT /evidence="ECO:0000305|PubMed:17613526"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT VAR_SEQ 154..176
FT /note="KGQFPGIIDLYGSIGGLCEHRAS -> EQLSTHLPTRFLSSQPSLFFGPE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028234"
FT VAR_SEQ 177..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028235"
SQ SEQUENCE 419 AA; 46769 MW; 33C12E7F3B2B94C7 CRC64;
MAATLSVEPA GRSCWDEPLS IAVRGLAPEQ PVTLRSVLRD EKGMLFRAHA RYRADSHGEL
DLARTPALGG SFSGLEPMGL LWAMEPDRPF WRLIKRDVQI PFVVELEVLD GHEPDGGQRL
ARAVHERHFM APGVRRVPVR EGRVRATLFL PPGKGQFPGI IDLYGSIGGL CEHRASLLAG
HGFAVLALAY FQFEDLPENL SDVRLEYFEE ALALMLRHPQ VKGPNIGLIG VSKGADLCLS
MAAFLKDNIT ATVLINACVA NTLVPLYYKD LFVPELGCDQ TKNKSGLMDL RDMWNNPLEE
PNHQSLIPLE KAQGPFLFLV GMDDHNWKSD VYARIACERL QAHGKDRPQI IYYPETGHCI
EPPYFPPPIA TVHFVLGEAV FNGGKPRAQS RAQLDAWQRI QTFFQKYLNG EKPARHSKL
