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

Cleaved into the following chain:

1. Acyl-coenzyme A thioesterase 13, N-terminally processed

Gene names

Name:	ACOT13
Synonyms:	THEM2
ORF Names:	HT012, PNAS-27

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	140 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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-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	Cytoplasm › cytosol By similarity. Mitochondrion By similarity. Nucleus By similarity. Cytoplasm › cytoskeleton › spindle 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 component	Cytoplasm Cytoskeleton Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	metabolic process Inferred from direct assay Ref.10Ref.11. Source: GOC protein homotetramerization Inferred from physical interaction Ref.10Ref.11. Source: UniProtKB
Cellular_component	cytosol 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_function	acyl-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 140

140

Acyl-coenzyme A thioesterase 13

PRO_0000156697

Initiator methionine

1

1

Removed; alternate Ref.6

Chain

2 – 140

139

Acyl-coenzyme A thioesterase 13, N-terminally processed

PRO_0000424501

Sites

Binding site

50

1

Substrate

Amino acid modifications

Modified residue

1

1

N-acetylmethionine; in Acyl-coenzyme A thioesterase 13; alternate Ref.8 Ref.9

Modified residue

2

1

N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed Ref.6 Ref.8 Ref.9

Modified residue

27

1

N6-acetyllysine By similarity

Modified residue

37

1

N6-acetyllysine By similarity

Modified residue

43

1

N6-acetyllysine By similarity

Modified residue

108

1

N6-acetyllysine By similarity

Modified residue

127

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

1 – 26

26

MTSMT…ERVLG → MVR in isoform 2.

VSP_046101

Experimental info

Mutagenesis

50

1

N → A: Reduced activity. Ref.11

Mutagenesis

56

1

H → A: Decreases affinity for substrate. Ref.11

Mutagenesis

65

1

D → A: Loss of activity. Ref.10 Ref.11

Mutagenesis

65

1

D → E or N: Reduced activity. Ref.10 Ref.11

Mutagenesis

83

1

S → A: Reduced activity. Ref.11

Secondary structure

1

.

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140

Helix Strand Turn

Details...

Helix

3 – 15

13

Beta strand

18 – 20

3

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)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: A6F50AA63A00583A	FASTA	117	12,366
	10 20 30 40 50 60 MVRKITLVSA APGKVICEMK VEEEHTNAIG TLHGGLTATL VDNISTMALL CTERGAPGVS 70 80 90 100 110 VDMNITYMSP AKLGEDIVIT AHVLKQGKTL AFTSVDLTNK ATGKLIAQGR HTKHLGN

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] [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. , 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. , 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.

CCDS

CCDS4558.1. [Q9NPJ3-1]
CCDS54972.1. [Q9NPJ3-2]

RefSeq

NP_001153566.1. NM_001160094.1. [Q9NPJ3-2]
NP_060943.1. NM_018473.3. [Q9NPJ3-1]

UniGene

Hs.731605.

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...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

120958. 14 interactions.

IntAct

Q9NPJ3. 3 interactions.

STRING

9606.ENSP00000230048.

PTM databases

PhosphoSite

Q9NPJ3.

Proteomic databases

MaxQB

Q9NPJ3.

PaxDb

Q9NPJ3.

PeptideAtlas

Q9NPJ3.

PRIDE

Q9NPJ3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000230048; ENSP00000230048; ENSG00000112304. [Q9NPJ3-1]
ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]

GeneID

55856.

KEGG

hsa:55856.

UCSC

uc003nek.3. human. [Q9NPJ3-1]

Organism-specific databases

CTD

55856.

GeneCards

GC06P024667.

H-InvDB

HIX0005627.

HGNC

HGNC:20999. ACOT13.

HPA

HPA019881.

MIM

615652. gene.

neXtProt

NX_Q9NPJ3.

PharmGKB

PA165617655.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2050.

HOGENOM

HOG000170540.

InParanoid

Q9NPJ3.

KO

K17362.

OMA

MNITYMS.

OrthoDB

EOG7Q8CQ4.

PhylomeDB

Q9NPJ3.

TreeFam

TF315062.

Enzyme and pathway databases

SABIO-RK

Q9NPJ3.

Gene expression databases

Bgee

Q9NPJ3.

CleanEx

HS_THEM2.

Genevestigator

Q9NPJ3.

Family and domain databases

Gene3D

3.10.129.10. 1 hit.

InterPro

IPR029069. HotDog_dom.
IPR003736. PAAI_dom.
IPR006683. Thioestr_supf.
[Graphical view]

Pfam

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

SUPFAM

SSF54637. SSF54637. 1 hit.

TIGRFAMs

TIGR00369. unchar_dom_1. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

ACOT13. human.

EvolutionaryTrace

Q9NPJ3.

GenomeRNAi

55856.

NextBio

61135.

PRO

Q9NPJ3.

SOURCE

Search...

Entry information

Entry name

ACO13_HUMAN

Accession

Primary (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 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.