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Reviewed, UniProtKB/Swiss-Prot P49753 (ACOT2_HUMAN)

Last modified October 13, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acyl-coenzyme A thioesterase 2, mitochondrial
      Short name=Acyl-CoA thioesterase 2
    EC=3.1.2.2
Alternative name(s):
    Acyl-coenzyme A thioester hydrolase 2a
    Long-chain acyl-CoA thioesterase 2
    ZAP128
    CTE-Ia
Gene names
Name: ACOT2
Synonyms: PTE2, PTE2A
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

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. Displays high levels of activity on medium- and long chain acyl CoAs. Ref.6

Catalytic activity

Palmitoyl-CoA + H2O = CoA + palmitate.

Subcellular location

Mitochondrion. Ref.2

Tissue specificity

Strongest expression in heart, liver, muscle and kidney. Weak in placenta and pancreas. Ref.2

Sequence similarities

Belongs to the C/M/P thioester hydrolase family.

Caution

Was originally (Ref.6) thought to be peroxisomal but was later shown (Ref.2) to be mitochondrial.

Biophysicochemical properties

Kinetic parameters:

KM=40.3 µM for C10-acyl-CoA

KM=8.9 µM for C12-acyl-CoA

KM=1.6 µM for C14-acyl-CoA

KM=2.0 µM for C16-acyl-CoA

KM=2.8 µM for C18-acyl-CoA

KM=4.8 µM for C20-acyl-CoA

KM=4.5 µM for C16:1-acyl-CoA

KM=6.1 µM for C18:1-acyl-CoA

KM=4.3 µM for C18:1-trans-acyl-CoA

Vmax=212 nmol/min/mg enzyme toward C10-acyl-CoA

Vmax=681 nmol/min/mg enzyme toward C12-acyl-CoA

Vmax=766 nmol/min/mg enzyme toward C14-acyl-CoA

Vmax=656 nmol/min/mg enzyme toward C16-acyl-CoA

Vmax=488 nmol/min/mg enzyme toward C18-acyl-CoA

Vmax=408 nmol/min/mg enzyme toward C20-acyl-CoA

Vmax=661 nmol/min/mg enzyme toward C16:1-acyl-CoA

Vmax=304 nmol/min/mg enzyme toward C18:1-acyl-CoA

Vmax=418 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA

Sequence caution

The sequence AAC42007.1 differs from that shown. Reason: Frameshift at positions 215 and 226.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZNF277Q9NRM21EBI-1052865,EBI-949305

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49753-1)

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.
Isoform 2 (identifier: P49753-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.
     53-214: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 483Acyl-coenzyme A thioesterase 2, mitochondrialPRO_0000202147

Regions

Motif481 – 4833Microbody targeting signal Potential

Sites

Active site2941Charge relay system By similarity
Active site3881Charge relay system By similarity
Active site4221Charge relay system By similarity

Amino acid modifications

Modified residue1041N6-acetyllysine Ref.7

Natural variations

Alternative sequence1 – 2020Missing in isoform 2.
VSP_012225
Alternative sequence53 – 214162Missing in isoform 2.
VSP_012226
Natural variant161R → S: dbSNP rs11545741.
VAR_057271
Natural variant4751H → R: dbSNP rs7494. Ref.6 Ref.3 Ref.4 Ref.5
VAR_016136

Experimental info

Sequence conflict1671E → V in AAZ31237. Ref.2
Sequence conflict1671E → V in BAA91989. Ref.3
Sequence conflict3281R → H in AAC42007. Ref.1
Sequence conflict4541A → V in AAH06335. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 13, 2007. Version 5.
Checksum: FAF96B6F4533745E

FASTA48353,238
        10         20         30         40         50         60 
MSNKLLSPHP HSVVLRSEFK MASSPAVLRA SRLYQWSLKS SAQFLGSPQL RQVGQIIRVP 

        70         80         90        100        110        120 
ARMAATLILE PAGRCCWDEP VRIAVRGLAP EQPVTLRASL RDEKGALFQA HARYRADTLG 

       130        140        150        160        170        180 
ELDLERAPAL GGSFAGLEPM GLLWALEPEK PLVRLVKRDV RTPLAVELEV LDGHDPDPGR 

       190        200        210        220        230        240 
LLCQTRHERY FLPPGVRREP VRVGRVRGTL FLPPEPGPFP GIVDMFGTGG GLLEYRASLL 

       250        260        270        280        290        300 
AGKGFAVMAL AYYNYEDLPK TMETLHLEYF EEAMNYLLSH PEVKGPGVGL LGISKGGELC 

       310        320        330        340        350        360 
LSMASFLKGI TAAVVINGSV ANVGGTLRYK GETLPPVGVN RNRIKVTKDG YADIVDVLNS 

       370        380        390        400        410        420 
PLEGPDQKSF IPVERAESTF LFLVGQDDHN WKSEFYANEA CKRLQAHGRR KPQIICYPET 

       430        440        450        460        470        480 
GHYIEPPYFP LCRASLHALV GSPIIWGGEP RAHAMAQVDA WKQLQTFFHK HLGGHEGTIP 


SKV 

« Hide

Isoform 2.

Checksum: D143605714182F7C
Show »

FASTA30132,978

References

« Hide 'large scale' references
[1]"Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease."
Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L. expand/collapse author list , Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M., St George-Hyslop P.H.
Nature 375:754-760(1995) [PubMed: 7596406] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs."
Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.
FASEB J. 20:1855-1864(2006) [PubMed: 16940157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-475.
Tissue: Placenta.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-475.
Tissue: Spleen.
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-475.
Tissue: Lung and Uterus.
[6]"Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase."
Jones J.M., Gould S.J.
Biochem. Biophys. Res. Commun. 275:233-240(2000) [PubMed: 10944470] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-483 (ISOFORM 1), FUNCTION, VARIANT ARG-475.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

L40401 mRNA. Translation: AAC42007.1. Frameshift.
DQ082755 mRNA. Translation: AAZ31237.1.
AK001939 mRNA. Translation: BAA91989.1.
AK223635 mRNA. Translation: BAD97355.1.
BC004436 mRNA. Translation: AAH04436.2.
BC006335 mRNA. Translation: AAH06335.1.
BC006500 mRNA. Translation: AAH06500.4.
AY005822 mRNA. Translation: AAF97985.1.
IPIIPI00220906.
IPI00513928.
PIRJC7367.
RefSeqNP_006812.3.
UniGeneHs.446685
Hs.710625

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3HLKX-ray2.10A/B46-483[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP49753. 1 interaction.
STRINGP49753.

Proteomic databases

PRIDEP49753.

Genome annotation databases

EnsemblENST00000238651; ENSP00000238651; ENSG00000119673; Homo sapiens. [Genome view]
GeneID10965.
KEGGhsa:10965.
UCSCuc001xon.2. human.

Organism-specific databases

CTD10965.
GeneCardsGC14P073106.
H-InvDBHIX0037756.
HGNCHGNC:18431. ACOT2.
MIM609972. gene.
PharmGKBPA142672653.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP49753.
HOVERGENP49753.

Enzyme and pathway databases

BRENDA3.1.2.2. 247.

Gene expression databases

BgeeP49753.
CleanExHS_ACOT2.
GenevestigatorP49753.
GermOnlineENSG00000119673. Homo sapiens.

Family and domain databases

InterProIPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFPIRSF016521. Acyl-CoA_hydro. 1 hit.
ProtoNetSearch...

Other Resources

NextBio41670.
SOURCESearch...

Entry information

Entry nameACOT2_HUMAN
AccessionPrimary (citable) accession number: P49753
Secondary accession number(s): Q3I5F8, Q53EK4, Q9NUX4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: October 13, 2009
This is version 94 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 14: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents