Q8WYK0 (ACO12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A thioesterase 12
Short name=Acyl-CoA thioesterase 12
EC=3.1.2.1

Alternative name(s):
Acyl-CoA thioester hydrolase 12
Cytoplasmic acetyl-CoA hydrolase 1
Short name=CACH-1
Short name=hCACH-1
START domain-containing protein 15
Short name=StARD15

Gene names

Name:	ACOT12
Synonyms:	CACH, CACH1, STARD15

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	555 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes acetyl-CoA to acetate and CoA. Ref.1
Catalytic activity	Acetyl-CoA + H2O = CoA + acetate.
Enzyme regulation	Inhibited by ADP. Active in the presence of ATP. Ref.1
Pathway	Carbohydrate metabolism; pyruvate metabolism.
Subunit structure	Homodimer or homotetramer By similarity.
Subcellular location	Cytoplasm Ref.1.
Sequence similarities	Contains 2 acyl coenzyme A hydrolase domains. Contains 1 START domain.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat
Molecular function	Hydrolase Serine esterase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: Compara acyl-CoA metabolic process Inferred from sequence or structural similarity. Source: HGNC fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyruvate metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: HGNC
Molecular_function	ATP binding Inferred from electronic annotation. Source: Compara acetyl-CoA hydrolase activity Inferred from sequence or structural similarity. Source: HGNC carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 555

555

Acyl-coenzyme A thioesterase 12

PRO_0000053809

Regions

Domain

1 – 127

127

Acyl coenzyme A hydrolase 1

Domain

165 – 301

137

Acyl coenzyme A hydrolase 2

Domain

340 – 549

210

START

Region

53 – 55

3

Coenzyme A binding

Region

82 – 84

3

Coenzyme A binding

Region

234 – 236

3

Coenzyme A binding

Sites

Binding site

144

1

Coenzyme A

Natural variations

Natural variant

190

1

L → H Found in a clear cell renal carcinoma case; somatic mutation. Ref.6

VAR_064691

Natural variant

230

1

V → I.
Corresponds to variant rs34607174 [ dbSNP | Ensembl ].

VAR_048192

Natural variant

403

1

A → T.
Corresponds to variant rs10371 [ dbSNP | Ensembl ].

VAR_048193

Secondary structure

1

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555

Helix Strand Turn

Details...

Beta strand

7 – 14

8

Helix

17 – 19

3

Beta strand

24 – 26

3

Helix

28 – 47

20

Beta strand

51 – 56

6

Beta strand

69 – 80

12

Beta strand

82 – 95

14

Turn

96 – 98

3

Beta strand

101 – 113

13

Helix

131 – 149

19

Beta strand

183 – 188

6

Helix

191 – 193

3

Helix

202 – 218

17

Beta strand

220 – 223

4

Beta strand

226 – 230

5

Beta strand

244 – 255

12

Beta strand

258 – 268

11

Helix

270 – 275

6

Beta strand

279 – 289

11

Helix

294 – 296

3

Sequences

	Sequence		Length	Mass (Da)
	Q8WYK0 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 707560D55504732C	FASTA	555	62,034
	10 20 30 40 50 60 MERPAPGEVV MSQAIQPAHA TARGELSAGQ LLKWIDTTAC LAAEKHAGVS CVTASVDDIQ 70 80 90 100 110 120 FEETARVGQV ITIKAKVTRA FSTSMEISIK VMVQDMLTGI EKLVSVAFST FVAKPVGKEK 130 140 150 160 170 180 IHLKPVTLLT EQDHVEHNLA AERRKVRLQH EDTFNNLMKE SSKFDDLIFD EEEGAVSTRG 190 200 210 220 230 240 TSVQSIELVL PPHANHHGNT FGGQIMAWME TVATISASRL CWAHPFLKSV DMFKFRGPST 250 260 270 280 290 300 VGDRLVFTAI VNNTFQTCVE VGVRVEAFDC QEWAEGRGRH INSAFLIYNA ADDKENLITF 310 320 330 340 350 360 PRIQPISKDD FRRYRGAIAR KRIRLGRKYV ISHKEEVPLC IHWDISKQAS LSDSNVEALK 370 380 390 400 410 420 KLAAKRGWEV TSTVEKIKIY TLEEHDVLSV WVEKHVGSPA HLAYRLLSDF TKRPLWDPHF 430 440 450 460 470 480 VSCEVIDWVS EDDQLYHITC PILNDDKPKD LVVLVSRRKP LKDGNTYTVA VKSVILPSVP 490 500 510 520 530 540 PSPQYIRSEI ICAGFLIHAI DSNSCIVSYF NHMSASILPY FAGNLGGWSK SIEETAASCI 550 QFLENPPDDG FVSTF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase." Suematsu N., Isohashi F. Acta Biochim. Pol. 53:553-561(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, ENZYME REGULATION, FUNCTION. Tissue: Liver.
[2]	"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: Liver.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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].
[5]	"Human acyl-coenzyme A thioesterase 12." Structural genomics consortium (SGC) Submitted (NOV-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-316 IN COMPLEX WITH COENZYME A.
[6]	"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A. Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-190.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB078619 mRNA. Translation: BAB84022.1.
AK122960 mRNA. Translation: BAG53821.1.
CH471084 Genomic DNA. Translation: EAW95875.1.
BC075010 mRNA. Translation: AAH75010.1.
BC075011 mRNA. Translation: AAH75011.1.

IPI

IPI00103729.

RefSeq

NP_570123.1. NM_130767.2.

UniGene

Hs.591756.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3B7K	X-ray	2.70	A/B/C	7-316	[»]

ProteinModelPortal

Q8WYK0.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000303246.

Protein family/group databases

TCDB

4.C.3.1.2. acyl-CoA thioesterase (AcoT) family.

PTM databases

PhosphoSite

Q8WYK0.

Polymorphism databases

DMDM

25008183.

Proteomic databases

PaxDb

Q8WYK0.

PeptideAtlas

Q8WYK0.

PRIDE

Q8WYK0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307624; ENSP00000303246; ENSG00000172497.

GeneID

134526.

KEGG

hsa:134526.

UCSC

uc003khl.4. human.

Organism-specific databases

CTD

134526.

GeneCards

GC05M080662.

HGNC

HGNC:24436. ACOT12.

HPA

HPA037723.

MIM

614315. gene.

neXtProt

NX_Q8WYK0.

PharmGKB

PA142672657.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1607.

HOGENOM

HOG000232032.

HOVERGEN

HBG023847.

InParanoid

Q8WYK0.

KO

K01067.

OMA

KYVISHK.

OrthoDB

EOG4JT058.

PhylomeDB

Q8WYK0.

Enzyme and pathway databases

BRENDA

3.1.2.1. 2681.

SABIO-RK

Q8WYK0.

UniPathway

UPA00231.

Gene expression databases

ArrayExpress

Q8WYK0.

Bgee

Q8WYK0.

CleanEx

HS_ACOT12.

Genevestigator

Q8WYK0.

GermOnline

ENSG00000172497. Homo sapiens.

Family and domain databases

Gene3D

3.30.530.20. 1 hit.

InterPro

IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view]

Pfam

PF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]

PROSITE

PS50848. START. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8WYK0.

GenomeRNAi

134526.

NextBio

83397.

SOURCE

Search...

Entry information

Entry name

ACO12_HUMAN

Accession

Primary (citable) accession number: Q8WYK0
Secondary accession number(s): B3KVK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 98 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.