Q8N9L9 (ACOT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A thioesterase 4
Short name=Acyl-CoA thioesterase 4
EC=3.1.2.2

Alternative name(s):
PTE-2b
Peroxisomal acyl coenzyme A thioester hydrolase Ib
Peroxisomal long-chain acyl-CoA thioesterase Ib
Short name=PTE-Ib

Gene names

Name:	ACOT4
Synonyms:	PTE2B, PTEIB

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	421 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 By similarity. Succinyl-CoA thioesterase that also hydrolyzes long chain saturated and unsaturated monocarboxylic acyl-CoAs.
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subcellular location	Peroxisome Ref.4.
Tissue specificity	Strongest expression in liver and kidney and weaker expression in placenta, heart, and muscle. Ref.4
Miscellaneous	Human ACOT4 may have acquired the combined activities of mouse ACOT3, ACOT4, and ACOT5.
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.
Biophysicochemical properties	Kinetic parameters: KM=14 µM for succinyl-CoA Ref.4 KM=147 µM for glutaryl-CoA KM=3.4 µM for C14-acyl-CoA Vmax=581 nmol/min/mg enzyme toward succinyl-CoA Vmax=132 nmol/min/mg enzyme toward glutaryl-CoA Vmax=137 nmol/min/mg enzyme toward C14-acyl-CoA

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Serine esterase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dicarboxylic acid catabolic process Inferred from direct assay PubMed 16141203. Source: UniProtKB long-chain fatty acid metabolic process Inferred from direct assay Ref.4. Source: HGNC saturated monocarboxylic acid metabolic process Inferred from direct assay Ref.4. Source: HGNC short-chain fatty acid metabolic process Inferred from direct assay Ref.4. Source: HGNC succinyl-CoA metabolic process Inferred from direct assay Ref.4. Source: HGNC unsaturated monocarboxylic acid metabolic process Inferred from direct assay Ref.4. Source: HGNC very long-chain fatty acid metabolic process Inferred from direct assay Ref.4. Source: HGNC
Cellular_component	peroxisome Inferred from direct assay PubMed 16141203. Source: UniProtKB
Molecular_function	acyl-CoA hydrolase activity Inferred from direct assay PubMed 16141203. Source: UniProtKB carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW palmitoyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC succinyl-CoA hydrolase activity Inferred from direct assay PubMed 16141203. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 421

421

Acyl-coenzyme A thioesterase 4

PRO_0000202149

Regions

Motif

419 – 421

3

Microbody targeting signal Potential

Sites

Active site

232

1

Charge relay system By similarity

Active site

326

1

Charge relay system By similarity

Active site

360

1

Charge relay system By similarity

Natural variations

Natural variant

57

1

R → C. Ref.3
Corresponds to variant rs3742819 [ dbSNP | Ensembl ].

VAR_052300

Natural variant

187

1

A → D.
Corresponds to variant rs35724886 [ dbSNP | Ensembl ].

VAR_052301

Experimental info

Sequence conflict

130

1

L → P in BAC04313. Ref.1

Sequence conflict

187 – 190

4

ALAY → DLQS in BAC04313. Ref.1

Secondary structure

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421

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

20 – 25

6

Beta strand

31 – 39

9

Beta strand

45 – 53

9

Turn

62 – 64

3

Beta strand

69 – 72

4

Helix

79 – 82

4

Beta strand

85 – 88

4

Beta strand

102 – 112

11

Beta strand

119 – 130

12

Beta strand

135 – 141

7

Beta strand

144 – 150

7

Beta strand

152 – 154

3

Beta strand

159 – 163

5

Helix

173 – 179

7

Turn

180 – 182

3

Beta strand

184 – 189

6

Beta strand

191 – 193

3

Helix

206 – 216

11

Beta strand

224 – 231

8

Helix

233 – 244

12

Beta strand

246 – 255

10

Beta strand

265 – 267

3

Beta strand

270 – 272

3

Helix

279 – 281

3

Helix

302 – 304

3

Helix

311 – 313

3

Beta strand

318 – 323

6

Beta strand

327 – 329

3

Helix

331 – 344

14

Beta strand

351 – 355

5

Beta strand

372 – 375

4

Turn

376 – 379

4

Beta strand

380 – 383

4

Helix

388 – 409

22

Sequences

	Sequence		Length	Mass (Da)
	Q8N9L9 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 41BBE5AA826A9F2C	FASTA	421	46,327
	10 20 30 40 50 60 MSATLILEPP GRCCWNEPVR IAVRGLAPEQ RVTLRASLRD EKGALFRAHA RYCADARGEL 70 80 90 100 110 120 DLERAPALGG SFAGLEPMGL LWALEPEKPF WRFLKRDVQI PFVVELEVLD GHDPEPGRLL 130 140 150 160 170 180 CQAQHERHFL PPGVRRQSVR AGRVRATLFL PPGPGPFPGI IDIFGIGGGL LEYRASLLAG 190 200 210 220 230 240 HGFATLALAY YNFEDLPNNM DNISLEYFEE AVCYMLQHPQ VKGPGIGLLG ISLGADICLS 250 260 270 280 290 300 MASFLKNVSA TVSINGSGIS GNTAINYKHS SIPPLGYDLR RIKVAFSGLV DIVDIRNALV 310 320 330 340 350 360 GGYKNPSMIP IEKAQGPILL IVGQDDHNWR SELYAQTVSE RLQAHGKEKP QIICYPGTGH 370 380 390 400 410 420 YIEPPYFPLC PASLHRLLNK HVIWGGEPRA HSKAQEDAWK QILAFFCKHL GGTQKTAVPK L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Cerebellum and Kidney.
[2]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Neuroblastoma and Placenta.
[3]	"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], VARIANT CYS-57. Tissue: Colon and Urinary bladder.
[4]	"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: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK094223 mRNA. Translation: BAC04313.1.
AK055797 mRNA. Translation: BAB71017.1.
BX248023 mRNA. Translation: CAD62346.1.
BX248047 mRNA. Translation: CAD62354.1.
BC031799 mRNA. Translation: AAH31799.2.
BC090945 mRNA. Translation: AAH90945.1.
BC117341 mRNA. Translation: AAI17342.1.
BC117343 mRNA. Translation: AAI17344.1.

IPI

IPI00171211.

RefSeq

NP_689544.3. NM_152331.3.

UniGene

Hs.49433.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3K2I	X-ray	2.40	A/B	1-421	[»]

ProteinModelPortal

Q8N9L9.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000323071.

Protein family/group databases

MEROPS

S09.029.

PTM databases

PhosphoSite

Q8N9L9.

Polymorphism databases

DMDM

50401071.

Proteomic databases

PaxDb

Q8N9L9.

PRIDE

Q8N9L9.

Protocols and materials databases

DNASU

122970.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000326303; ENSP00000323071; ENSG00000177465.

GeneID

122970.

KEGG

hsa:122970.

UCSC

uc001xoo.3. human.

Organism-specific databases

CTD

122970.

GeneCards

GC14P074058.

H-InvDB

HIX0202062.

HGNC

HGNC:19748. ACOT4.

HPA

HPA000779.

MIM

614314. gene.

neXtProt

NX_Q8N9L9.

PharmGKB

PA142672654.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1073.

HOGENOM

HOG000116219.

HOVERGEN

HBG000331.

InParanoid

Q8N9L9.

KO

K01068.

OMA

CPASLHR.

OrthoDB

EOG4QC15F.

PhylomeDB

Q8N9L9.

Enzyme and pathway databases

BioCyc

MetaCyc:HS16863-MONOMER.

SABIO-RK

Q8N9L9.

Gene expression databases

Bgee

Q8N9L9.

CleanEx

HS_ACOT4.

Genevestigator

Q8N9L9.

GermOnline

ENSG00000177465. Homo sapiens.

Family and domain databases

InterPro

IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]

Pfam

PF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]

PIRSF

PIRSF016521. Acyl-CoA_hydro. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8N9L9.

GenomeRNAi

122970.

NextBio

81045.

SOURCE

Search...

Entry information

Entry name

ACOT4_HUMAN

Accession

Primary (citable) accession number: Q8N9L9
Secondary accession number(s): Q17RF4 , Q5BKT6, Q86TX0, Q86TX1, Q96N88

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 92 of the entry and version 2 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.