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Q9NPJ3 (ACO13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 13

Short name=Acyl-CoA thioesterase 13
EC=3.1.2.-
Alternative name(s):
Thioesterase superfamily member 2
Gene names
Name:ACOT13
Synonyms:THEM2
ORF Names:HT012, PNAS-27
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length140 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. 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. Ref.10 Ref.11

Subunit structure

Homotetramer. Ref.10 Ref.11

Subcellular location

Cytoplasmcytosol By similarity. Mitochondrion By similarity. Nucleus By similarity. Cytoplasmcytoskeletonspindle By similarity. Note: During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin By similarity.

Sequence similarities

Belongs to the thioesterase PaaI family.

Biophysicochemical properties

Kinetic parameters:

KM=4.9 µM for n-decanoyl-CoA Ref.11

KM=26 µM for n-octanoyl-CoA

KM=5 µM for myristoyl-CoA

KM=9 µM for palmitoyl-CoA

KM=9 µM for oleoyl-CoA

KM=10 µM for 3,4-dihydroxyphenylacetyl-CoA

KM=40 µM for 3-hydroxyphenylacetyl-CoA

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from direct assay Ref.10Ref.11. Source: GOC

protein homotetramerization

Inferred from physical interaction Ref.10Ref.11. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacyl-CoA hydrolase activity

Inferred from direct assay Ref.10Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NPJ3-1)

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: Q9NPJ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MTSMTQSLREVIKAMTKARNFERVLG → MVR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Acyl-coenzyme A thioesterase 13
PRO_0000156697
Initiator methionine11Removed; alternate Ref.6
Chain2 – 140139Acyl-coenzyme A thioesterase 13, N-terminally processed
PRO_0000424501

Sites

Binding site501Substrate

Amino acid modifications

Modified residue11N-acetylmethionine; in Acyl-coenzyme A thioesterase 13; alternate Ref.8 Ref.9
Modified residue21N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed Ref.6 Ref.8 Ref.9
Modified residue271N6-acetyllysine By similarity
Modified residue371N6-acetyllysine By similarity
Modified residue431N6-acetyllysine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue1271N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 2626MTSMT…ERVLG → MVR in isoform 2.
VSP_046101

Experimental info

Mutagenesis501N → A: Reduced activity. Ref.11
Mutagenesis561H → A: Decreases affinity for substrate. Ref.11
Mutagenesis651D → A: Loss of activity. Ref.10 Ref.11
Mutagenesis651D → E or N: Reduced activity. Ref.10 Ref.11
Mutagenesis831S → A: Reduced activity. Ref.11

Secondary structure

........................... 140
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: 084E36EFEE715A18

FASTA14014,960
        10         20         30         40         50         60 
MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT 

        70         80         90        100        110        120 
ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL 

       130        140 
TNKATGKLIA QGRHTKHLGN 

« Hide

Isoform 2 [UniParc].

Checksum: A6F50AA63A00583A
Show »

FASTA11712,366

References

« Hide 'large scale' references
[1]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
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. expand/collapse author list , 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.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland and Hypothalamus.
[2]"Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
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.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Promyelocytic leukemia.
[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] (ISOFORMS 1 AND 2).
Tissue: Teratocarcinoma.
[4]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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).
Tissue: Cervix.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Crystal structure of human thioesterase superfamily member 2."
Cheng Z., Song F., Shan X., Wei Z., Wang Y., Dunaway-Mariano D., Gong W.
Biochem. Biophys. Res. Commun. 349:172-177(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT.
[11]"The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, SUBUNIT.
[12]"The crystal structure of human thioesterase superfamily member 2."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF155649 mRNA. Translation: AAF67006.1.
AF220186 mRNA. Translation: AAF67651.1.
AF274952 mRNA. Translation: AAK07529.1.
AK000508 mRNA. Translation: BAA91215.1.
AK309738 mRNA. No translation available.
AL031775 Genomic DNA. Translation: CAD92509.1.
BC000894 mRNA. Translation: AAH00894.1.
CCDSCCDS4558.1. [Q9NPJ3-1]
CCDS54972.1. [Q9NPJ3-2]
RefSeqNP_001153566.1. NM_001160094.1. [Q9NPJ3-2]
NP_060943.1. NM_018473.3. [Q9NPJ3-1]
UniGeneHs.731605.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F0XX-ray2.30A/B/C/D/E/F/G/H1-140[»]
2H4UX-ray2.20A/B/C/D19-140[»]
3F5OX-ray1.70A/B/C/D/E/F/G/H1-140[»]
ProteinModelPortalQ9NPJ3.
SMRQ9NPJ3. Positions 2-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120958. 14 interactions.
IntActQ9NPJ3. 3 interactions.
STRING9606.ENSP00000230048.

PTM databases

PhosphoSiteQ9NPJ3.

Proteomic databases

MaxQBQ9NPJ3.
PaxDbQ9NPJ3.
PeptideAtlasQ9NPJ3.
PRIDEQ9NPJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1]
ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]
GeneID55856.
KEGGhsa:55856.
UCSCuc003nek.3. human. [Q9NPJ3-1]

Organism-specific databases

CTD55856.
GeneCardsGC06P024667.
H-InvDBHIX0005627.
HGNCHGNC:20999. ACOT13.
HPAHPA019881.
MIM615652. gene.
neXtProtNX_Q9NPJ3.
PharmGKBPA165617655.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2050.
HOGENOMHOG000170540.
InParanoidQ9NPJ3.
KOK17362.
OMAMNITYMS.
OrthoDBEOG7Q8CQ4.
PhylomeDBQ9NPJ3.
TreeFamTF315062.

Enzyme and pathway databases

SABIO-RKQ9NPJ3.

Gene expression databases

BgeeQ9NPJ3.
CleanExHS_THEM2.
GenevestigatorQ9NPJ3.

Family and domain databases

Gene3D3.10.129.10. 1 hit.
InterProIPR029069. HotDog_dom.
IPR003736. PAAI_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 1 hit.
[Graphical view]
SUPFAMSSF54637. SSF54637. 1 hit.
TIGRFAMsTIGR00369. unchar_dom_1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSACOT13. human.
EvolutionaryTraceQ9NPJ3.
GenomeRNAi55856.
NextBio61135.
PROQ9NPJ3.
SOURCESearch...

Entry information

Entry nameACO13_HUMAN
AccessionPrimary (citable) accession number: Q9NPJ3
Secondary accession number(s): F5H2L4, O95549
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 112 of the entry and version 1 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 chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM