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Acyl-coenzyme A thioesterase 13 (Acyl-CoA thioesterase 13) (EC 3.1.2.-) (Thioesterase superfamily member 2) [Cleaved into: Acyl-coenzyme A thioesterase 13, N-terminally processed]

 ACO13_HUMAN             Reviewed;         140 AA.
Q9NPJ3; F5H2L4; O95549;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 146.
RecName: Full=Acyl-coenzyme A thioesterase 13;
Short=Acyl-CoA thioesterase 13;
EC=3.1.2.-;
AltName: Full=Thioesterase superfamily member 2;
Contains:
RecName: Full=Acyl-coenzyme A thioesterase 13, N-terminally processed;
Name=ACOT13; Synonyms=THEM2; ORFNames=HT012, PNAS-27;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal gland, and Hypothalamus;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Promyelocytic leukemia;
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F.,
Yan W., Yang H., Zhao Z.-L.;
"Human acute promyelocytic leukemia cell line NB4's apoptosis related
genes.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY
MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, AND SUBUNIT.
PubMed=16934754; DOI=10.1016/j.bbrc.2006.08.025;
Cheng Z., Song F., Shan X., Wei Z., Wang Y., Dunaway-Mariano D.,
Gong W.;
"Crystal structure of human thioesterase superfamily member 2.";
Biochem. Biophys. Res. Commun. 349:172-177(2006).
[13]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
ASN-50; HIS-56; ASP-65 AND SER-83, AND SUBUNIT.
PubMed=19170545; DOI=10.1021/bi801879z;
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.;
"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate
recognition and catalysis illuminated by a structure and function
based analysis.";
Biochemistry 48:1293-1304(2009).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Structural genomics consortium (SGC);
"The crystal structure of human thioesterase superfamily member 2.";
Submitted (FEB-2009) to the PDB data bank.
-!- 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. Has
acyl-CoA thioesterase activity towards medium (C12) and long-chain
(C18) fatty acyl-CoA substrates. Can also hydrolyze 3-
hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in
vitro). May play a role in controlling adaptive thermogenesis (By
similarity). {ECO:0000250, ECO:0000269|PubMed:16934754,
ECO:0000269|PubMed:19170545}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4.9 uM for n-decanoyl-CoA {ECO:0000269|PubMed:19170545};
KM=26 uM for n-octanoyl-CoA {ECO:0000269|PubMed:19170545};
KM=5 uM for myristoyl-CoA {ECO:0000269|PubMed:19170545};
KM=9 uM for palmitoyl-CoA {ECO:0000269|PubMed:19170545};
KM=9 uM for oleoyl-CoA {ECO:0000269|PubMed:19170545};
KM=10 uM for 3,4-dihydroxyphenylacetyl-CoA
{ECO:0000269|PubMed:19170545};
KM=40 uM for 3-hydroxyphenylacetyl-CoA
{ECO:0000269|PubMed:19170545};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16934754,
ECO:0000269|PubMed:19170545}.
-!- INTERACTION:
Q969H8:MYDGF; NbExp=4; IntAct=EBI-1045357, EBI-718622;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q9CQR4}. Mitochondrion
{ECO:0000250|UniProtKB:Q9CQR4}. Nucleus
{ECO:0000250|UniProtKB:Q9CQR4}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:Q9CQR4}. Note=During interphase, found both
in the nucleus and in the cytoplasm. At mitosis, localizes to the
spindle. Colocalizes with tubulin. {ECO:0000250|UniProtKB:Q9CQR4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NPJ3-1; Sequence=Displayed;
Name=2;
IsoId=Q9NPJ3-2; Sequence=VSP_046101;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the thioesterase PaaI family.
{ECO:0000305}.
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EMBL; AF155649; AAF67006.1; -; mRNA.
EMBL; AF220186; AAF67651.1; -; mRNA.
EMBL; AF274952; AAK07529.1; -; mRNA.
EMBL; AK000508; BAA91215.1; -; mRNA.
EMBL; AK309738; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL031775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000894; AAH00894.1; -; mRNA.
CCDS; CCDS4558.1; -. [Q9NPJ3-1]
CCDS; CCDS54972.1; -. [Q9NPJ3-2]
RefSeq; NP_001153566.1; NM_001160094.1. [Q9NPJ3-2]
RefSeq; NP_060943.1; NM_018473.3. [Q9NPJ3-1]
UniGene; Hs.731605; -.
PDB; 2F0X; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-140.
PDB; 2H4U; X-ray; 2.20 A; A/B/C/D=19-140.
PDB; 3F5O; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-140.
PDBsum; 2F0X; -.
PDBsum; 2H4U; -.
PDBsum; 3F5O; -.
ProteinModelPortal; Q9NPJ3; -.
SMR; Q9NPJ3; -.
BioGrid; 120958; 24.
IntAct; Q9NPJ3; 6.
STRING; 9606.ENSP00000230048; -.
DrugBank; DB08688; undecan-2-one.
iPTMnet; Q9NPJ3; -.
PhosphoSitePlus; Q9NPJ3; -.
BioMuta; ACOT13; -.
EPD; Q9NPJ3; -.
MaxQB; Q9NPJ3; -.
PaxDb; Q9NPJ3; -.
PeptideAtlas; Q9NPJ3; -.
PRIDE; Q9NPJ3; -.
TopDownProteomics; Q9NPJ3-1; -. [Q9NPJ3-1]
Ensembl; ENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1]
Ensembl; ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]
GeneID; 55856; -.
KEGG; hsa:55856; -.
UCSC; uc003nek.4; human. [Q9NPJ3-1]
CTD; 55856; -.
DisGeNET; 55856; -.
EuPathDB; HostDB:ENSG00000112304.10; -.
GeneCards; ACOT13; -.
H-InvDB; HIX0005627; -.
HGNC; HGNC:20999; ACOT13.
HPA; HPA019881; -.
MIM; 615652; gene.
neXtProt; NX_Q9NPJ3; -.
OpenTargets; ENSG00000112304; -.
PharmGKB; PA165617655; -.
eggNOG; KOG3328; Eukaryota.
eggNOG; COG2050; LUCA.
GeneTree; ENSGT00390000013934; -.
HOGENOM; HOG000170540; -.
InParanoid; Q9NPJ3; -.
KO; K17362; -.
OMA; KMGTLHG; -.
OrthoDB; EOG091G125K; -.
PhylomeDB; Q9NPJ3; -.
TreeFam; TF315062; -.
BRENDA; 3.1.2.20; 2681.
Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
SABIO-RK; Q9NPJ3; -.
ChiTaRS; ACOT13; human.
EvolutionaryTrace; Q9NPJ3; -.
GenomeRNAi; 55856; -.
PRO; PR:Q9NPJ3; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112304; -.
CleanEx; HS_THEM2; -.
Genevisible; Q9NPJ3; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0006637; P:acyl-CoA metabolic process; TAS:Reactome.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
InterPro; IPR029069; HotDog_dom.
InterPro; IPR003736; PAAI_dom.
InterPro; IPR006683; Thioestr_dom.
Pfam; PF03061; 4HBT; 1.
SUPFAM; SSF54637; SSF54637; 1.
TIGRFAMs; TIGR00369; unchar_dom_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Cytoskeleton; Hydrolase; Mitochondrion; Nucleus;
Reference proteome.
CHAIN 1 140 Acyl-coenzyme A thioesterase 13.
/FTId=PRO_0000156697.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
CHAIN 2 140 Acyl-coenzyme A thioesterase 13, N-
terminally processed.
/FTId=PRO_0000424501.
BINDING 50 50 Substrate.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 2 2 N-acetylthreonine; in Acyl-coenzyme A
thioesterase 13, N-terminally processed.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 27 27 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQR4}.
MOD_RES 37 37 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQR4}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQR4}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQR4}.
MOD_RES 127 127 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CQR4}.
VAR_SEQ 1 26 MTSMTQSLREVIKAMTKARNFERVLG -> MVR (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046101.
MUTAGEN 50 50 N->A: Reduced activity.
{ECO:0000269|PubMed:19170545}.
MUTAGEN 56 56 H->A: Decreases affinity for substrate.
{ECO:0000269|PubMed:19170545}.
MUTAGEN 65 65 D->A: Loss of activity.
{ECO:0000269|PubMed:16934754,
ECO:0000269|PubMed:19170545}.
MUTAGEN 65 65 D->E,N: Reduced activity.
{ECO:0000269|PubMed:16934754,
ECO:0000269|PubMed:19170545}.
MUTAGEN 83 83 S->A: Reduced activity.
{ECO:0000269|PubMed:19170545}.
HELIX 3 15 {ECO:0000244|PDB:3F5O}.
STRAND 18 20 {ECO:0000244|PDB:3F5O}.
HELIX 21 25 {ECO:0000244|PDB:3F5O}.
STRAND 29 34 {ECO:0000244|PDB:3F5O}.
STRAND 37 43 {ECO:0000244|PDB:3F5O}.
HELIX 46 48 {ECO:0000244|PDB:3F5O}.
STRAND 53 55 {ECO:0000244|PDB:3F5O}.
HELIX 57 73 {ECO:0000244|PDB:3F5O}.
STRAND 75 77 {ECO:0000244|PDB:3F5O}.
STRAND 82 90 {ECO:0000244|PDB:3F5O}.
STRAND 99 109 {ECO:0000244|PDB:3F5O}.
STRAND 111 122 {ECO:0000244|PDB:3F5O}.
TURN 123 125 {ECO:0000244|PDB:3F5O}.
STRAND 128 137 {ECO:0000244|PDB:3F5O}.
SEQUENCE 140 AA; 14960 MW; 084E36EFEE715A18 CRC64;
MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT
ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL
TNKATGKLIA QGRHTKHLGN


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ant-424 Mouse Anti Human Acyl-Coenzyme A Thioesterase 11 20
E1060h Mouse ELISA Kit FOR Acyl-coenzyme A thioesterase 6 96T
E1427m Human ELISA Kit FOR Acyl-coenzyme A thioesterase 8 96T
ant-424 Mouse Anti Human Acyl-Coenzyme A Thioesterase 11 100
CSB-EL001170RA Rat Acyl-coenzyme A thioesterase 8(ACOT8) ELISA kit 96T
CSB-EL001165RA Rat Acyl-coenzyme A thioesterase 12(ACOT12) ELISA kit 96T
CSB-EL001163RA Rat Acyl-coenzyme A thioesterase 1(ACOT1) ELISA kit 96T
E10782h Mouse ELISA Kit FOR Acyl-coenzyme A thioesterase 4 96T
ant-424 Mouse Anti Human Acyl-Coenzyme A Thioesterase 11 ACOT11 100
ant-424 Mouse Anti Human Acyl-Coenzyme A Thioesterase 11 ACOT11 5
CSB-EL001170MO Mouse Acyl-coenzyme A thioesterase 8(ACOT8) ELISA kit 96T
E1426h Human ELISA Kit FOR Putative acyl-coenzyme A thioesterase 6 96T
CSB-EL001163MO Mouse Acyl-coenzyme A thioesterase 1(ACOT1) ELISA kit 96T
CSB-EL001164MO Mouse Acyl-coenzyme A thioesterase 11(ACOT11) ELISA kit 96T
E2003Rb Mouse ELISA Kit FOR Acyl-coenzyme A thioesterase 9, mitochondrial 96T
CSB-EL001165MO Mouse Acyl-coenzyme A thioesterase 12(ACOT12) ELISA kit 96T
CSB-EL001167MO Mouse Acyl-coenzyme A thioesterase 4(ACOT4) ELISA kit 96T


 

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