Q9NPJ3 (ACO13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	140 AA.
Sequence status	Complete.
Protein existence	Evidence 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-dihydrohyphenylacetyl-CoA (in vitro). Ref.7 Ref.8
Subunit structure	Homotetramer. Ref.7 Ref.8
Subcellular location	Cytoplasm By similarity. Mitochondrion By similarity.
Sequence similarities	Belongs to the thioesterase PaaI family.
Biophysicochemical properties	Kinetic parameters: KM=4.9 µM for n-decanoyl-CoA Ref.8 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-dihydrohyphenylacetyl-CoA KM=40 µM for 3-hydrohyphenylacetyl-CoA

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein homotetramerization Inferred from physical interaction Ref.7Ref.8. Source: UniProtKB
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyl-CoA hydrolase activity Inferred from direct assay Ref.7Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 140

140

Acyl-coenzyme A thioesterase 13

PRO_0000156697

Sites

Binding site

50

1

Substrate

Experimental info

Mutagenesis

50

1

N → A: Reduced activity. Ref.8

Mutagenesis

56

1

H → A: Decreases affinity for substrate. Ref.8

Mutagenesis

65

1

D → A: Loss of activity. Ref.7 Ref.8

Mutagenesis

65

1

D → E or N: Reduced activity. Ref.7 Ref.8

Mutagenesis

83

1

S → A: Reduced activity. Ref.8

Secondary structure

1

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140

Helix Strand Turn

Details...

Helix

4 – 17

14

Helix

21 – 25

5

Beta strand

29 – 34

6

Beta strand

37 – 43

7

Helix

46 – 48

3

Beta strand

53 – 55

3

Helix

57 – 73

17

Beta strand

75 – 77

3

Beta strand

82 – 90

9

Beta strand

99 – 109

11

Beta strand

111 – 122

12

Turn

123 – 125

3

Beta strand

128 – 137

10

Sequences

	Sequence		Length	Mass (Da)
	Q9NPJ3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 084E36EFEE715A18	FASTA	140	14,960
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]. 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. , 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].
[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. , 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: 14574404] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[6]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"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: 16934754] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT.
[8]	"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: 19170545] [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.
[9]	"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.
AL031775 Genomic DNA. Translation: CAD92509.1.
BC000894 mRNA. Translation: AAH00894.1.

IPI

IPI00020530.

RefSeq

NP_060943.1. NM_018473.3.

UniGene

Hs.727546.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F0X	X-ray	2.30	A/B/C/D/E/F/G/H	1-140	[»]
2H4U	X-ray	2.20	A/B/C/D	19-140	[»]
3F5O	X-ray	1.70	A/B/C/D/E/F/G/H	1-140	[»]

ProteinModelPortal

Q9NPJ3.

SMR

Q9NPJ3. Positions 2-139.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NPJ3. 2 interactions.

STRING

Q9NPJ3.

Polymorphism databases

DMDM

23396822.

Proteomic databases

PeptideAtlas

Q9NPJ3.

PRIDE

Q9NPJ3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000230048; ENSP00000230048; ENSG00000112304.

GeneID

55856.

KEGG

hsa:55856.

UCSC

uc003nek.1. human.

Organism-specific databases

CTD

55856.

GeneCards

GC06P024667.

H-InvDB

HIX0005626.

HGNC

HGNC:20999. ACOT13.

HPA

HPA019881.

neXtProt

NX_Q9NPJ3.

PharmGKB

PA128394691.
PA165617655.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20053.

GeneTree

ENSGT00390000013934.

InParanoid

Q9NPJ3.

OMA

MKVEEQH.

OrthoDB

EOG4SQWZ8.

PhylomeDB

Q9NPJ3.

Gene expression databases

ArrayExpress

Q9NPJ3.

Bgee

Q9NPJ3.

CleanEx

HS_THEM2.

Genevestigator

Q9NPJ3.

GermOnline

ENSG00000112304. Homo sapiens.

Family and domain databases

InterPro

IPR003736. PAAI.
IPR006683. Thioestr_supf.
[Graphical view]

Pfam

PF03061. 4HBT. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00369. Unchar_dom_1. 1 hit.

ProtoNet

Search...

Other

NextBio

61135.

Entry information

Entry name

ACO13_HUMAN

Accession

Primary (citable) accession number: Q9NPJ3
Secondary accession number(s): O95549

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.