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P49753 (ACOT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
CTE-Ia
Long-chain acyl-CoA thioesterase 2
ZAP128
Gene names
Name:ACOT2
Synonyms:PTE2, PTE2A
OrganismHomo sapiens (Human) [Reference 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 Ref.2

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.

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 By similarity
Modified residue4701N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 2020Missing in isoform 2.
VSP_012225
Alternative sequence53 – 214162Missing in isoform 2.
VSP_012226
Natural variant161R → S.
Corresponds to variant rs11545741 [ dbSNP | Ensembl ].
VAR_057271
Natural variant4751H → R. Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs7494 [ dbSNP | Ensembl ].
VAR_016136

Experimental info

Sequence conflict1671E → V in AAZ31237. Ref.2
Sequence conflict1671E → V in BAA91989. Ref.3
Sequence conflict3281H → R in AAZ31237. Ref.2
Sequence conflict3281H → R in BAA91989. Ref.3
Sequence conflict3281H → R in BAD97355. Ref.4
Sequence conflict3281H → R in AAH04436. Ref.5
Sequence conflict3281H → R in AAH06335. Ref.5
Sequence conflict3281H → R in AAH06500. Ref.5
Sequence conflict3281H → R in AAF97985. Ref.6
Sequence conflict4541A → V in AAH06335. Ref.5

Secondary structure

................................................................. 483
Helix Strand Turn

Details...

Sequences

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

Last modified November 24, 2009. Version 6.
Checksum: FAEDD42BBBD935E4

FASTA48353,218
        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 ANVGGTLHYK 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 [UniParc].

Checksum: D157DF13EAF26EC6
Show »

FASTA30132,959

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-483 (ISOFORM 1), FUNCTION, VARIANT ARG-475.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9816.1. [P49753-1]
PIRJC7367.
RefSeqNP_006812.3. NM_006821.5. [P49753-1]
UniGeneHs.446685.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HLKX-ray2.10A/B46-483[»]
ProteinModelPortalP49753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116164. 3 interactions.
MINTMINT-5004303.
STRING9606.ENSP00000238651.

Chemistry

ChEMBLCHEMBL2189135.

Protein family/group databases

MEROPSS09.028.

PTM databases

PhosphoSiteP49753.

Polymorphism databases

DMDM269849771.

Proteomic databases

MaxQBP49753.
PRIDEP49753.

Protocols and materials databases

DNASU10965.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238651; ENSP00000238651; ENSG00000119673. [P49753-1]
GeneID10965.
KEGGhsa:10965.
UCSCuc001xon.5. human. [P49753-1]

Organism-specific databases

CTD10965.
GeneCardsGC14P074036.
H-InvDBHIX0011795.
HIX0172385.
HGNCHGNC:18431. ACOT2.
HPAHPA043705.
MIM609972. gene.
neXtProtNX_P49753.
PharmGKBPA142672653.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000116219.
HOVERGENHBG000331.
InParanoidP49753.
KOK01068.
OMAQWSLKSS.
PhylomeDBP49753.
TreeFamTF314911.

Enzyme and pathway databases

BioCycMetaCyc:HS04318-MONOMER.
BRENDA3.1.2.2. 2681.
SABIO-RKP49753.

Gene expression databases

ArrayExpressP49753.
BgeeP49753.
CleanExHS_ACOT2.
GenevestigatorP49753.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR016662. 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.
SUPFAMSSF53474. SSF53474. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP49753.
GeneWikiACOT2.
GenomeRNAi10965.
NextBio41670.
PROP49753.
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 24, 2009
Last modified: July 9, 2014
This is version 139 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

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