Reviewed, UniProtKB/Swiss-Prot Q8N9L9 (ACOT4_HUMAN)

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

Gene names

Name:	ACOT4
Synonyms:	PTE2B, PTEIB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subcellular location	Peroxisome Potential.
Sequence similarities	Belongs to the C/M/P thioester hydrolase family.

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Serine esterase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from direct assay. Source: HGNC dicarboxylic acid metabolic process Inferred from direct assay. Source: HGNC long-chain fatty acid metabolic process Inferred from direct assay. Source: HGNC saturated monocarboxylic acid metabolic process Inferred from direct assay. Source: HGNC short-chain fatty acid metabolic process Inferred from direct assay. Source: HGNC succinyl-CoA metabolic process Inferred from direct assay. Source: HGNC unsaturated monocarboxylic acid metabolic process Inferred from direct assay. Source: HGNC very-long-chain fatty acid metabolic process Inferred from direct assay. Source: HGNC
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA peroxisome Inferred from direct assay. Source: HGNC
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW palmitoyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC
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: dbSNP rs3742819. Ref.3		VAR_052300
	Natural variant	187	1	A → D: dbSNP rs35724886.		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

Sequences

	Sequence		Length	Mass (Da)
	Q8N9L9-1 [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

[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: 14702039] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-57. Tissue: Colon and Urinary bladder.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.49433
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q8N9L9.
Proteomic databases
PRIDE	Q8N9L9.
Genome annotation databases
Ensembl	ENSG00000177465. Homo sapiens. [Contig view]
GeneID	122970.
KEGG	hsa:122970.
UCSC	uc001xoo.1. human.
Organism-specific databases
GeneCards	GC14P073129.
HGNC	HGNC:19748. ACOT4.
HPA	HPA000779.
PharmGKB	PA142672654.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8N9L9.
HOVERGEN	Q8N9L9.
OMA	Q8N9L9. PSMIPIE.
Enzyme and pathway databases
BRENDA	3.1.2.2. 247.
Gene expression databases
ArrayExpress	Q8N9L9.
Bgee	Q8N9L9.
CleanEx	HS_ACOT4.
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 Resources
NextBio	81045.

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:	July 7, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)