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Acyl-coenzyme A thioesterase 12 (Acyl-CoA thioesterase 12) (EC 3.1.2.1) (Acyl-CoA thioester hydrolase 12) (Cytoplasmic acetyl-CoA hydrolase 1) (CACH-1) (hCACH-1) (START domain-containing protein 15) (StARD15)

 ACO12_HUMAN             Reviewed;         555 AA.
Q8WYK0; B3KVK9; Q5FWE9;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=Acyl-coenzyme A thioesterase 12;
Short=Acyl-CoA thioesterase 12;
EC=3.1.2.1;
AltName: Full=Acyl-CoA thioester hydrolase 12;
AltName: Full=Cytoplasmic acetyl-CoA hydrolase 1;
Short=CACH-1;
Short=hCACH-1;
AltName: Full=START domain-containing protein 15;
Short=StARD15;
Name=ACOT12; Synonyms=CACH, CACH1, STARD15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, ENZYME
REGULATION, AND FUNCTION.
TISSUE=Liver;
PubMed=16951743;
Suematsu N., Isohashi F.;
"Molecular cloning and functional expression of human cytosolic
acetyl-CoA hydrolase.";
Acta Biochim. Pol. 53:553-561(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Chondrosarcoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[7]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-316 IN COMPLEX WITH
COENZYME A.
Structural genomics consortium (SGC);
"Human acyl-coenzyme A thioesterase 12.";
Submitted (NOV-2007) to the PDB data bank.
[8]
VARIANT HIS-190.
PubMed=21248752; DOI=10.1038/nature09639;
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.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
-!- FUNCTION: Hydrolyzes acetyl-CoA to acetate and CoA.
{ECO:0000269|PubMed:16951743}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O = CoA + acetate.
-!- ENZYME REGULATION: Inhibited by ADP. Active in the presence of
ATP. {ECO:0000269|PubMed:16951743}.
-!- PATHWAY: Carbohydrate metabolism; pyruvate metabolism.
-!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16951743}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8WYK0-1; Sequence=Displayed;
Name=2;
IsoId=Q8WYK0-2; Sequence=VSP_055785, VSP_055786;
Note=No experimental confirmation available.;
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EMBL; AB078619; BAB84022.1; -; mRNA.
EMBL; AK122960; BAG53821.1; -; mRNA.
EMBL; AC008411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471084; EAW95875.1; -; Genomic_DNA.
EMBL; BC089437; AAH89437.1; -; mRNA.
EMBL; BC075010; AAH75010.1; -; mRNA.
EMBL; BC075011; AAH75011.1; -; mRNA.
CCDS; CCDS4055.1; -. [Q8WYK0-1]
RefSeq; NP_570123.1; NM_130767.2. [Q8WYK0-1]
UniGene; Hs.591756; -.
PDB; 3B7K; X-ray; 2.70 A; A/B/C=7-316.
PDB; 4MOB; X-ray; 2.40 A; A=7-336.
PDB; 4MOC; X-ray; 2.50 A; A=7-336.
PDBsum; 3B7K; -.
PDBsum; 4MOB; -.
PDBsum; 4MOC; -.
ProteinModelPortal; Q8WYK0; -.
SMR; Q8WYK0; -.
BioGrid; 126405; 6.
IntAct; Q8WYK0; 9.
STRING; 9606.ENSP00000303246; -.
SwissLipids; SLP:000001187; -.
TCDB; 4.C.3.1.2; the acyl-coa thioesterase (acot) family.
iPTMnet; Q8WYK0; -.
PhosphoSitePlus; Q8WYK0; -.
BioMuta; ACOT12; -.
DMDM; 25008183; -.
PaxDb; Q8WYK0; -.
PeptideAtlas; Q8WYK0; -.
PRIDE; Q8WYK0; -.
Ensembl; ENST00000307624; ENSP00000303246; ENSG00000172497. [Q8WYK0-1]
Ensembl; ENST00000513751; ENSP00000421628; ENSG00000172497. [Q8WYK0-2]
GeneID; 134526; -.
KEGG; hsa:134526; -.
UCSC; uc003khl.5; human. [Q8WYK0-1]
CTD; 134526; -.
DisGeNET; 134526; -.
EuPathDB; HostDB:ENSG00000172497.8; -.
GeneCards; ACOT12; -.
HGNC; HGNC:24436; ACOT12.
HPA; HPA037723; -.
HPA; HPA037724; -.
MIM; 614315; gene.
neXtProt; NX_Q8WYK0; -.
OpenTargets; ENSG00000172497; -.
PharmGKB; PA142672657; -.
eggNOG; KOG2763; Eukaryota.
eggNOG; COG1607; LUCA.
GeneTree; ENSGT00760000119297; -.
HOGENOM; HOG000294223; -.
HOVERGEN; HBG023847; -.
InParanoid; Q8WYK0; -.
KO; K01067; -.
OMA; RPLWDPH; -.
OrthoDB; EOG091G06LZ; -.
PhylomeDB; Q8WYK0; -.
TreeFam; TF328368; -.
BRENDA; 3.1.2.1; 2681.
Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
UniPathway; UPA00231; -.
EvolutionaryTrace; Q8WYK0; -.
GeneWiki; ACOT12; -.
GenomeRNAi; 134526; -.
PRO; PR:Q8WYK0; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000172497; -.
CleanEx; HS_ACOT12; -.
Genevisible; Q8WYK0; HS.
GO; GO:0005829; C:cytosol; ISS:HGNC.
GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:HGNC.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:Ensembl.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0008289; F:lipid binding; IEA:InterPro.
GO; GO:0006084; P:acetyl-CoA metabolic process; IBA:GO_Central.
GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC.
GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.530.20; -; 1.
InterPro; IPR033120; HOTDOG_ACOT.
InterPro; IPR029069; HotDog_dom_sf.
InterPro; IPR023393; START-like_dom_sf.
InterPro; IPR002913; START_lipid-bd_dom.
InterPro; IPR006683; Thioestr_dom.
Pfam; PF03061; 4HBT; 2.
Pfam; PF01852; START; 1.
SUPFAM; SSF54637; SSF54637; 2.
PROSITE; PS51770; HOTDOG_ACOT; 2.
PROSITE; PS50848; START; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Fatty acid metabolism; Hydrolase; Lipid metabolism; Polymorphism;
Reference proteome; Repeat; Serine esterase.
CHAIN 1 555 Acyl-coenzyme A thioesterase 12.
/FTId=PRO_0000053809.
DOMAIN 5 117 HotDog ACOT-type 1. {ECO:0000255|PROSITE-
ProRule:PRU01106}.
DOMAIN 179 294 HotDog ACOT-type 2. {ECO:0000255|PROSITE-
ProRule:PRU01106}.
DOMAIN 340 549 START. {ECO:0000255|PROSITE-
ProRule:PRU00197}.
REGION 53 55 Coenzyme A binding.
REGION 82 84 Coenzyme A binding.
REGION 234 236 Coenzyme A binding.
BINDING 144 144 Coenzyme A. {ECO:0000269|Ref.7}.
MOD_RES 33 33 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBK0}.
MOD_RES 159 159 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBK0}.
MOD_RES 228 228 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9DBK0}.
VAR_SEQ 166 167 DL -> GQ (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055785.
VAR_SEQ 168 555 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055786.
VARIANT 190 190 L -> H (found in a clear cell renal
carcinoma case; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064691.
VARIANT 230 230 V -> I (in dbSNP:rs34607174).
/FTId=VAR_048192.
VARIANT 403 403 A -> T (in dbSNP:rs10371).
/FTId=VAR_048193.
STRAND 9 14 {ECO:0000244|PDB:4MOB}.
HELIX 17 19 {ECO:0000244|PDB:4MOB}.
STRAND 24 26 {ECO:0000244|PDB:4MOB}.
HELIX 28 47 {ECO:0000244|PDB:4MOB}.
STRAND 51 56 {ECO:0000244|PDB:4MOB}.
STRAND 69 80 {ECO:0000244|PDB:4MOB}.
STRAND 82 95 {ECO:0000244|PDB:4MOB}.
TURN 96 98 {ECO:0000244|PDB:4MOB}.
STRAND 101 113 {ECO:0000244|PDB:4MOB}.
STRAND 116 118 {ECO:0000244|PDB:4MOB}.
HELIX 131 160 {ECO:0000244|PDB:4MOB}.
HELIX 171 173 {ECO:0000244|PDB:4MOB}.
HELIX 179 181 {ECO:0000244|PDB:4MOB}.
STRAND 183 188 {ECO:0000244|PDB:4MOB}.
HELIX 191 193 {ECO:0000244|PDB:4MOB}.
STRAND 198 200 {ECO:0000244|PDB:4MOB}.
HELIX 202 221 {ECO:0000244|PDB:4MOB}.
STRAND 222 230 {ECO:0000244|PDB:4MOB}.
STRAND 244 255 {ECO:0000244|PDB:4MOB}.
STRAND 258 268 {ECO:0000244|PDB:4MOB}.
HELIX 270 274 {ECO:0000244|PDB:4MOB}.
STRAND 279 291 {ECO:0000244|PDB:4MOB}.
STRAND 293 295 {ECO:0000244|PDB:4MOC}.
HELIX 308 325 {ECO:0000244|PDB:4MOB}.
SEQUENCE 555 AA; 62034 MW; 707560D55504732C CRC64;
MERPAPGEVV MSQAIQPAHA TARGELSAGQ LLKWIDTTAC LAAEKHAGVS CVTASVDDIQ
FEETARVGQV ITIKAKVTRA FSTSMEISIK VMVQDMLTGI EKLVSVAFST FVAKPVGKEK
IHLKPVTLLT EQDHVEHNLA AERRKVRLQH EDTFNNLMKE SSKFDDLIFD EEEGAVSTRG
TSVQSIELVL PPHANHHGNT FGGQIMAWME TVATISASRL CWAHPFLKSV DMFKFRGPST
VGDRLVFTAI VNNTFQTCVE VGVRVEAFDC QEWAEGRGRH INSAFLIYNA ADDKENLITF
PRIQPISKDD FRRYRGAIAR KRIRLGRKYV ISHKEEVPLC IHWDISKQAS LSDSNVEALK
KLAAKRGWEV TSTVEKIKIY TLEEHDVLSV WVEKHVGSPA HLAYRLLSDF TKRPLWDPHF
VSCEVIDWVS EDDQLYHITC PILNDDKPKD LVVLVSRRKP LKDGNTYTVA VKSVILPSVP
PSPQYIRSEI ICAGFLIHAI DSNSCIVSYF NHMSASILPY FAGNLGGWSK SIEETAASCI
QFLENPPDDG FVSTF


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