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Acyl-coenzyme A thioesterase THEM4 (Acyl-CoA thioesterase THEM4) (EC 3.1.2.2) (Carboxyl-terminal modulator protein) (Thioesterase superfamily member 4)

 THEM4_HUMAN             Reviewed;         240 AA.
Q5T1C6; B2RBX2; Q96KR2;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
22-NOV-2017, entry version 118.
RecName: Full=Acyl-coenzyme A thioesterase THEM4;
Short=Acyl-CoA thioesterase THEM4;
EC=3.1.2.2;
AltName: Full=Carboxyl-terminal modulator protein;
AltName: Full=Thioesterase superfamily member 4;
Flags: Precursor;
Name=THEM4; Synonyms=CTMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH AKT1, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND VARIANT
ARG-17.
PubMed=11598301; DOI=10.1126/science.1062030;
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M.,
Hemmings B.A.;
"Carboxyl-terminal modulator protein (CTMP), a negative regulator of
PKB/Akt and v-Akt at the plasma membrane.";
Science 294:374-380(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-17.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-17.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-17.
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]
TISSUE SPECIFICITY.
PubMed=15026474; DOI=10.1093/jnci/djh064;
Knobbe C.B., Reifenberger J., Blaschke B., Reifenberger G.;
"Hypermethylation and transcriptional downregulation of the carboxyl-
terminal modulator protein gene in glioblastomas.";
J. Natl. Cancer Inst. 96:483-486(2004).
[7]
FUNCTION.
PubMed=17615157; DOI=10.1152/ajpcell.00570.2006;
Ono H., Sakoda H., Fujishiro M., Anai M., Kushiyama A., Fukushima Y.,
Katagiri H., Ogihara T., Oka Y., Kamata H., Horike N., Uchijima Y.,
Kurihara H., Asano T.;
"Carboxy-terminal modulator protein induces Akt phosphorylation and
activation, thereby enhancing antiapoptotic, glycogen synthetic, and
glucose uptake pathways.";
Am. J. Physiol. 293:C1576-C1585(2007).
[8]
PHOSPHORYLATION AT SER-37 AND SER-38, IDENTIFICATION BY MASS
SPECTROMETRY, MUTAGENESIS OF 37-SER-SER-38, AND SUBCELLULAR LOCATION.
PubMed=19604401; DOI=10.1186/1471-2121-10-53;
Piao L., Li Y., Yang K.J., Park K.A., Byun H.S., Won M., Hong J.,
Kim J.L., Kweon G.R., Hur G.M., Seok J.H., Cho J.Y., Chun T., Hess D.,
Sack R., Maira S.M., Brazil D.P., Hemmings B.A., Park J.;
"Heat shock protein 70-mediated sensitization of cells to apoptosis by
carboxyl-terminal modulator protein.";
BMC Cell Biol. 10:53-53(2009).
[9]
CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19453107; DOI=10.1021/bi900710w;
Zhao H., Martin B.M., Bisoffi M., Dunaway-Mariano D.;
"The Akt C-terminal modulator protein is an acyl-CoA thioesterase of
the Hotdog-Fold family.";
Biochemistry 48:5507-5509(2009).
[10]
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF SER-37.
PubMed=19168129; DOI=10.1016/j.cellsig.2009.01.016;
Parcellier A., Tintignac L.A., Zhuravleva E., Cron P., Schenk S.,
Bozulic L., Hemmings B.A.;
"Carboxy-terminal modulator protein (CTMP) is a mitochondrial protein
that sensitizes cells to apoptosis.";
Cell. Signal. 21:639-650(2009).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19421406; DOI=10.1371/journal.pone.0005471;
Parcellier A., Tintignac L.A., Zhuravleva E., Dummler B., Brazil D.P.,
Hynx D., Cron P., Schenk S., Olivieri V., Hemmings B.A.;
"The carboxy-terminal modulator protein (CTMP) regulates mitochondrial
dynamics.";
PLoS ONE 4:E5471-E5471(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-240 IN COMPLEX WITH
UNDECAN-2-ONE-COA, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, FUNCTION, ACTIVE SITE, INTERACTION WITH AKT1, AND MUTAGENESIS
OF HIS-152; ASP-161; THR-177; ASN-183; ARG-206 AND LYS-207.
PubMed=22871024; DOI=10.1021/bi300968n;
Zhao H., Lim K., Choudry A., Latham J.A., Pathak M.C., Dominguez D.,
Luo L., Herzberg O., Dunaway-Mariano D.;
"Correlation of structure and function in the human hotdog-fold enzyme
hTHEM4.";
Biochemistry 51:6490-6492(2012).
[13]
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 37-240, AND SUBUNIT.
PubMed=22586271; DOI=10.1128/MCB.00312-12;
Zhuravleva E., Gut H., Hynx D., Marcellin D., Bleck C.K., Genoud C.,
Cron P., Keusch J.J., Dummler B., Esposti M.D., Hemmings B.A.;
"Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin
remodeling and fatty liver development.";
Mol. Cell. Biol. 32:2685-2697(2012).
[14]
VARIANTS ARG-17 AND CYS-38.
PubMed=17013611; DOI=10.1007/s00401-006-0128-y;
Schick V., Majores M., Engels G., Spitoni S., Koch A., Elger C.E.,
Simon M., Knobbe C., Bluemcke I., Becker A.J.;
"Activation of Akt independent of PTEN and CTMP tumor-suppressor gene
mutations in epilepsy-associated Taylor-type focal cortical
dysplasias.";
Acta Neuropathol. 112:715-725(2006).
-!- FUNCTION: Has acyl-CoA thioesterase activity towards medium and
long-chain (C14 to C18) fatty acyl-CoA substrates, and probably
plays an role in mitochondrial fatty acid metabolism. Plays a role
in the apoptotic process, possibly via its regulation of AKT1
activity. According to PubMed:11598301, inhibits AKT1
phosphorylation and activity. According to PubMed:17615157,
enhances AKT1 activity by favoring its phosphorylation and
translocation to plasma membrane. {ECO:0000269|PubMed:11598301,
ECO:0000269|PubMed:17615157, ECO:0000269|PubMed:19168129,
ECO:0000269|PubMed:19421406, ECO:0000269|PubMed:19453107,
ECO:0000269|PubMed:22871024}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
{ECO:0000269|PubMed:19453107, ECO:0000269|PubMed:22871024}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.4 uM for myristoyl-CoA {ECO:0000269|PubMed:19453107,
ECO:0000269|PubMed:22871024};
KM=2.6 uM for palmitoyl-CoA {ECO:0000269|PubMed:19453107,
ECO:0000269|PubMed:22871024};
KM=5.2 uM for oleoyl-CoA {ECO:0000269|PubMed:19453107,
ECO:0000269|PubMed:22871024};
-!- SUBUNIT: Homodimer and homotetramer. Interacts with AKT1 in the
cytosol. {ECO:0000269|PubMed:11598301,
ECO:0000269|PubMed:22586271, ECO:0000269|PubMed:22871024}.
-!- INTERACTION:
P31749:AKT1; NbExp=4; IntAct=EBI-7684443, EBI-296087;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11598301}.
Cell projection, ruffle membrane {ECO:0000269|PubMed:11598301}.
Cytoplasm {ECO:0000269|PubMed:19604401}. Mitochondrion
{ECO:0000269|PubMed:19168129, ECO:0000269|PubMed:19421406,
ECO:0000269|PubMed:19604401}. Mitochondrion inner membrane;
Peripheral membrane protein {ECO:0000269|PubMed:19168129}.
Mitochondrion intermembrane space {ECO:0000269|PubMed:19168129,
ECO:0000269|PubMed:19604401}. Note=Released from the mitochondria
into the cytosol in response to apoptotic stimuli.
{ECO:0000269|PubMed:19168129}.
-!- TISSUE SPECIFICITY: Expressed predominantly in skeletal muscle,
testis, uterus, brain and kidney. Down-regulated in glioblastoma
or glioma compared to non-neoplastic brain due to promoter
hypermethylation. {ECO:0000269|PubMed:11598301,
ECO:0000269|PubMed:15026474}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:11598301,
ECO:0000269|PubMed:19604401}.
-!- SIMILARITY: Belongs to the THEM4/THEM5 thioesterase family.
{ECO:0000305}.
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EMBL; AJ313515; CAC86384.1; -; mRNA.
EMBL; AK314852; BAG37369.1; -; mRNA.
EMBL; AL450992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53400.1; -; Genomic_DNA.
EMBL; BC065277; AAH65277.1; -; mRNA.
CCDS; CCDS1006.1; -.
RefSeq; NP_444283.2; NM_053055.4.
UniGene; Hs.164070; -.
PDB; 4AE8; X-ray; 1.59 A; A/B/C/D=37-240.
PDB; 4GAH; X-ray; 2.30 A; A/B=40-240.
PDBsum; 4AE8; -.
PDBsum; 4GAH; -.
ProteinModelPortal; Q5T1C6; -.
SMR; Q5T1C6; -.
BioGrid; 125557; 18.
DIP; DIP-60764N; -.
IntAct; Q5T1C6; 1.
MINT; MINT-8306269; -.
STRING; 9606.ENSP00000357804; -.
SwissLipids; SLP:000000657; -.
iPTMnet; Q5T1C6; -.
PhosphoSitePlus; Q5T1C6; -.
BioMuta; THEM4; -.
DMDM; 74744451; -.
EPD; Q5T1C6; -.
MaxQB; Q5T1C6; -.
PaxDb; Q5T1C6; -.
PeptideAtlas; Q5T1C6; -.
PRIDE; Q5T1C6; -.
Ensembl; ENST00000368814; ENSP00000357804; ENSG00000159445.
GeneID; 117145; -.
KEGG; hsa:117145; -.
UCSC; uc001ezj.3; human.
CTD; 117145; -.
DisGeNET; 117145; -.
EuPathDB; HostDB:ENSG00000159445.12; -.
GeneCards; THEM4; -.
HGNC; HGNC:17947; THEM4.
HPA; HPA028161; -.
MIM; 606388; gene.
neXtProt; NX_Q5T1C6; -.
OpenTargets; ENSG00000159445; -.
PharmGKB; PA142670813; -.
eggNOG; KOG4781; Eukaryota.
eggNOG; ENOG4111ZF6; LUCA.
GeneTree; ENSGT00390000018826; -.
HOGENOM; HOG000220857; -.
HOVERGEN; HBG054340; -.
InParanoid; Q5T1C6; -.
KO; K16339; -.
OMA; RKFFVSC; -.
OrthoDB; EOG091G0G1S; -.
PhylomeDB; Q5T1C6; -.
TreeFam; TF332518; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-165158; Activation of AKT2.
Reactome; R-HSA-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
SIGNOR; Q5T1C6; -.
ChiTaRS; THEM4; human.
GenomeRNAi; 117145; -.
PRO; PR:Q5T1C6; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000159445; -.
CleanEx; HS_THEM4; -.
ExpressionAtlas; Q5T1C6; baseline and differential.
Genevisible; Q5T1C6; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0047617; F:acyl-CoA hydrolase activity; TAS:Reactome.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0006637; P:acyl-CoA metabolic process; TAS:Reactome.
GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IMP:UniProtKB.
InterPro; IPR029069; HotDog_dom_sf.
InterPro; IPR006683; Thioestr_dom.
Pfam; PF03061; 4HBT; 1.
SUPFAM; SSF54637; SSF54637; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Fatty acid metabolism; Hydrolase;
Lipid metabolism; Membrane; Mitochondrion;
Mitochondrion inner membrane; Phosphoprotein; Polymorphism;
Reference proteome; Transit peptide.
TRANSIT 1 36 Mitochondrion. {ECO:0000255}.
CHAIN 37 240 Acyl-coenzyme A thioesterase THEM4.
/FTId=PRO_0000314179.
REGION 206 207 Substrate binding.
ACT_SITE 161 161 Proton donor/acceptor.
{ECO:0000305|PubMed:22871024}.
BINDING 183 183 Substrate.
BINDING 185 185 Substrate.
MOD_RES 37 37 Phosphoserine.
{ECO:0000269|PubMed:19604401}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000269|PubMed:19604401}.
MOD_RES 55 55 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q3UUI3}.
MOD_RES 66 66 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q3UUI3}.
MOD_RES 74 74 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q3UUI3}.
MOD_RES 98 98 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q3UUI3}.
MOD_RES 207 207 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q3UUI3}.
VARIANT 17 17 L -> R (in dbSNP:rs3748805).
{ECO:0000269|PubMed:11598301,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17013611,
ECO:0000269|Ref.4}.
/FTId=VAR_037865.
VARIANT 38 38 S -> C (in dbSNP:rs144257719).
{ECO:0000269|PubMed:17013611}.
/FTId=VAR_037866.
MUTAGEN 37 38 SS->DD: Abolishes import into the
mitochondria.
{ECO:0000269|PubMed:19604401}.
MUTAGEN 37 37 S->A: Abolishes cleavage of mitochondrial
transit peptide.
{ECO:0000269|PubMed:19168129}.
MUTAGEN 152 152 H->A,F: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:22871024}.
MUTAGEN 161 161 D->E,N: Nearly abolishes enzyme activity.
Strongly reduced affinity for myristoyl-
CoA. {ECO:0000269|PubMed:22871024}.
MUTAGEN 177 177 T->A: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:22871024}.
MUTAGEN 183 183 N->A: No effect on enzyme activity.
{ECO:0000269|PubMed:22871024}.
MUTAGEN 206 206 R->A: Reduces enzyme activity.
{ECO:0000269|PubMed:22871024}.
MUTAGEN 207 207 K->A: Slightly reduced enzyme activity.
{ECO:0000269|PubMed:22871024}.
HELIX 55 67 {ECO:0000244|PDB:4AE8}.
TURN 68 70 {ECO:0000244|PDB:4AE8}.
STRAND 71 76 {ECO:0000244|PDB:4AE8}.
HELIX 84 93 {ECO:0000244|PDB:4GAH}.
HELIX 111 113 {ECO:0000244|PDB:4AE8}.
TURN 117 119 {ECO:0000244|PDB:4AE8}.
STRAND 120 128 {ECO:0000244|PDB:4AE8}.
TURN 129 132 {ECO:0000244|PDB:4AE8}.
STRAND 133 140 {ECO:0000244|PDB:4AE8}.
HELIX 142 144 {ECO:0000244|PDB:4AE8}.
STRAND 145 147 {ECO:0000244|PDB:4AE8}.
HELIX 153 172 {ECO:0000244|PDB:4AE8}.
STRAND 175 184 {ECO:0000244|PDB:4AE8}.
STRAND 193 204 {ECO:0000244|PDB:4AE8}.
STRAND 207 216 {ECO:0000244|PDB:4AE8}.
STRAND 222 232 {ECO:0000244|PDB:4AE8}.
TURN 235 237 {ECO:0000244|PDB:4GAH}.
SEQUENCE 240 AA; 27130 MW; A01071B07A1B5FB2 CRC64;
MLRSCAARLR TLGALCLPPV GRRLPGSEPR PELRSFSSEE VILKDCSVPN PSWNKDLRLL
FDQFMKKCED GSWKRLPSYK RTPTEWIQDF KTHFLDPKLM KEEQMSQAQL FTRSFDDGLG
FEYVMFYNDI EKRMVCLFQG GPYLEGPPGF IHGGAIATMI DATVGMCAMM AGGIVMTANL
NINYKRPIPL CSVVMINSQL DKVEGRKFFV SCNVQSVDEK TLYSEATSLF IKLNPAKSLT


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EIAAB42239 Carboxyl-terminal modulator protein,CTMP,Homo sapiens,Human,THEM4,Thioesterase superfamily member 4
THEM4 THEM4 Gene thioesterase superfamily member 4
EIAAB37321 Mch,Olah,Oleoyl-ACP hydrolase,Rat,Rattus norvegicus,S-acyl fatty acid synthase thioesterase, medium chain,Thedc1,Thioesterase domain-containing protein 1,Thioesterase II
EIAAB37319 Mouse,Mus musculus,Olah,Oleoyl-ACP hydrolase,S-acyl fatty acid synthase thioesterase, medium chain,Thedc1,Thioesterase domain-containing protein 1,Thioesterase II
201-20-5875 THEM4{thioesterase superfamily member 4}rabbit.pAb 0.2ml
CSB-EL023494RA Rat Thioesterase superfamily member 4(THEM4) ELISA kit 96T
H5683 Thioesterase superfamily member 4 (THEM4), Rat, ELISA Kit 96T
H5681 Thioesterase superfamily member 4 (THEM4), Human, ELISA Kit 96T
H5680 Thioesterase superfamily member 4 (THEM4), Bovine, ELISA Kit 96T
CSB-EL023494RA Rat Thioesterase superfamily member 4(THEM4) ELISA kit SpeciesRat 96T
H5682 Thioesterase superfamily member 4 (THEM4), Mouse, ELISA Kit 96T
CSB-EL023494BO Bovine Thioesterase superfamily member 4(THEM4) ELISA kit 96T
CSB-EL023494MO Mouse Thioesterase superfamily member 4(THEM4) ELISA kit 96T
EIAAB42240 Rat,Rattus norvegicus,Them4,Thioesterase superfamily member 4
EIAAB42241 Bos taurus,Bovine,THEM4,Thioesterase superfamily member 4
CSB-EL023494HU Human Thioesterase superfamily member 4(THEM4) ELISA kit 96T
THEM4_RAT ELISA Kit FOR Thioesterase superfamily member 4; organism: Rat; gene name: Them4 96T
CSB-EL023494HU Human Thioesterase superfamily member 4(THEM4) ELISA kit SpeciesHuman 96T
CSB-EL023494BO Bovine Thioesterase superfamily member 4(THEM4) ELISA kit SpeciesBovine 96T
CSB-EL023494MO Mouse Thioesterase superfamily member 4(THEM4) ELISA kit SpeciesMouse 96T
THEM4_MOUSE ELISA Kit FOR Thioesterase superfamily member 4; organism: Mouse; gene name: Them4 96T
CSB-EL023494RA Rat thioesterase superfamily member 4 (THEM4) ELISA kit, Species Rat, Sample Type serum, plasma 96T
LF-MA10003 anti-Acyl-CoA Thioesterase 9 (4E4), Mouse monoclonal to Acyl-CoA Thioesterase 9, Isotype IgG1, Host Mouse 100 ug
CSB-EL023494BO Bovine thioesterase superfamily member 4 (THEM4) ELISA kit, Species Bovine, Sample Type serum, plasma 96T


 

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