Full text data of ACAT2
ACAT2
(ACTL)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Acetyl-CoA acetyltransferase, cytosolic; 2.3.1.9 (Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Acetyl-CoA acetyltransferase, cytosolic; 2.3.1.9 (Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00291419
IPI00291419 Cytosolic acetoacetyl-coenzyme A thiolase Acetyl-CoA acetyltransferase, 2 acetyl-CoA = CoA + acetoacetyl-CoA, lipid metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00291419 Cytosolic acetoacetyl-coenzyme A thiolase Acetyl-CoA acetyltransferase, 2 acetyl-CoA = CoA + acetoacetyl-CoA, lipid metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q9BWD1
ID THIC_HUMAN Reviewed; 397 AA.
AC Q9BWD1; E1P5B1; Q16146; Q5TCL7; Q8TDM4;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Acetyl-CoA acetyltransferase, cytosolic;
DE EC=2.3.1.9;
DE AltName: Full=Acetyl-CoA transferase-like protein;
DE AltName: Full=Cytosolic acetoacetyl-CoA thiolase;
GN Name=ACAT2; Synonyms=ACTL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7911016; DOI=10.1006/bbrc.1994.1726;
RA Song X.-Q., Fukao T., Yamaguchi S., Miyazawa S., Hashimoto T.,
RA Orii T.;
RT "Molecular cloning and nucleotide sequence of complementary DNA for
RT human hepatic cytosolic acetoacetyl-coenzyme A thiolase.";
RL Biochem. Biophys. Res. Commun. 201:478-485(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Chen H., Peng J., Huang C.-H.;
RT "Identification of the human acetyl CoA transferase like (ACTL)
RT protein by yeast two-hybrid screen.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-211.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 16-39; 195-210; 280-302 AND 342-361, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-233 AND LYS-235,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=15733928; DOI=10.1016/j.jmb.2005.01.018;
RA Kursula P., Sikkila H., Fukao T., Kondo N., Wierenga R.K.;
RT "High resolution crystal structures of human cytosolic thiolase (CT):
RT a comparison of the active sites of human CT, bacterial thiolase, and
RT bacterial KAS I.";
RL J. Mol. Biol. 347:189-201(2005).
CC -!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the thiolase family.
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DR EMBL; S70154; AAB30856.1; -; mRNA.
DR EMBL; AF356877; AAM00223.1; -; mRNA.
DR EMBL; AL135914; CAI21850.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47619.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47620.1; -; Genomic_DNA.
DR EMBL; BC000408; AAH00408.1; -; mRNA.
DR PIR; JC2378; JC2378.
DR RefSeq; NP_005882.2; NM_005891.2.
DR UniGene; Hs.571037; -.
DR PDB; 1WL4; X-ray; 1.55 A; A=1-397.
DR PDB; 1WL5; X-ray; 2.26 A; A=1-397.
DR PDBsum; 1WL4; -.
DR PDBsum; 1WL5; -.
DR ProteinModelPortal; Q9BWD1; -.
DR SMR; Q9BWD1; 4-397.
DR STRING; 9606.ENSP00000356015; -.
DR ChEMBL; CHEMBL2240; -.
DR PhosphoSite; Q9BWD1; -.
DR DMDM; 52000838; -.
DR OGP; Q9BWD1; -.
DR REPRODUCTION-2DPAGE; IPI00291419; -.
DR PaxDb; Q9BWD1; -.
DR PeptideAtlas; Q9BWD1; -.
DR PRIDE; Q9BWD1; -.
DR DNASU; 39; -.
DR Ensembl; ENST00000367048; ENSP00000356015; ENSG00000120437.
DR GeneID; 39; -.
DR KEGG; hsa:39; -.
DR UCSC; uc010kjy.3; human.
DR CTD; 39; -.
DR GeneCards; GC06P160153; -.
DR HGNC; HGNC:94; ACAT2.
DR HPA; CAB021106; -.
DR HPA; HPA025736; -.
DR HPA; HPA025765; -.
DR HPA; HPA025811; -.
DR MIM; 100678; gene+phenotype.
DR neXtProt; NX_Q9BWD1; -.
DR PharmGKB; PA19; -.
DR eggNOG; COG0183; -.
DR HOVERGEN; HBG003112; -.
DR InParanoid; Q9BWD1; -.
DR KO; K00626; -.
DR OrthoDB; EOG7JQBNG; -.
DR PhylomeDB; Q9BWD1; -.
DR BioCyc; MetaCyc:ENSG00000120437-MONOMER; -.
DR EvolutionaryTrace; Q9BWD1; -.
DR GeneWiki; ACAT2; -.
DR GenomeRNAi; 39; -.
DR NextBio; 153; -.
DR PRO; PR:Q9BWD1; -.
DR ArrayExpress; Q9BWD1; -.
DR Bgee; Q9BWD1; -.
DR CleanEx; HS_ACAT2; -.
DR Genevestigator; Q9BWD1; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0006629; P:lipid metabolic process; IC:BHF-UCL.
DR Gene3D; 3.40.47.10; -; 4.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR016038; Thiolase-like_subgr.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR18919; PTHR18919; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; FALSE_NEG.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 397 Acetyl-CoA acetyltransferase, cytosolic.
FT /FTId=PRO_0000206409.
FT ACT_SITE 92 92 Acyl-thioester intermediate.
FT ACT_SITE 353 353 Proton acceptor.
FT ACT_SITE 383 383 Proton acceptor.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 200 200 N6-acetyllysine.
FT MOD_RES 233 233 N6-acetyllysine.
FT MOD_RES 235 235 N6-acetyllysine.
FT VARIANT 211 211 K -> R (in dbSNP:rs25683).
FT /FTId=VAR_019686.
FT CONFLICT 169 169 K -> T (in Ref. 1; AAB30856).
FT CONFLICT 262 262 V -> A (in Ref. 1; AAB30856).
FT CONFLICT 375 375 R -> G (in Ref. 2; AAM00223).
FT STRAND 8 15
FT TURN 24 27
FT HELIX 30 45
FT HELIX 49 51
FT STRAND 54 58
FT HELIX 69 76
FT STRAND 85 88
FT HELIX 91 93
FT HELIX 94 107
FT STRAND 112 122
FT STRAND 136 138
FT HELIX 145 149
FT TURN 154 156
FT HELIX 160 171
FT HELIX 175 194
FT TURN 195 201
FT STRAND 205 209
FT STRAND 212 216
FT HELIX 228 232
FT TURN 240 243
FT HELIX 248 250
FT STRAND 255 265
FT HELIX 266 271
FT STRAND 277 287
FT HELIX 290 295
FT HELIX 297 308
FT HELIX 312 314
FT STRAND 317 320
FT HELIX 325 335
FT HELIX 339 341
FT HELIX 348 351
FT TURN 355 357
FT HELIX 358 373
FT STRAND 377 384
FT TURN 385 387
FT STRAND 388 396
SQ SEQUENCE 397 AA; 41351 MW; E3A8DAFB6F341B18 CRC64;
MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE DVSEVIFGHV
LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAVQSIGIGD SSIVVAGGME
NMSKAPHLAY LRTGVKIGEM PLTDSILCDG LTDAFHNCHM GITAENVAKK WQVSREDQDK
VAVLSQNRTE NAQKAGHFDK EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT
DGTGTVTPAN ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA
IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA LGHPLGASGC
RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE
//
ID THIC_HUMAN Reviewed; 397 AA.
AC Q9BWD1; E1P5B1; Q16146; Q5TCL7; Q8TDM4;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Acetyl-CoA acetyltransferase, cytosolic;
DE EC=2.3.1.9;
DE AltName: Full=Acetyl-CoA transferase-like protein;
DE AltName: Full=Cytosolic acetoacetyl-CoA thiolase;
GN Name=ACAT2; Synonyms=ACTL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7911016; DOI=10.1006/bbrc.1994.1726;
RA Song X.-Q., Fukao T., Yamaguchi S., Miyazawa S., Hashimoto T.,
RA Orii T.;
RT "Molecular cloning and nucleotide sequence of complementary DNA for
RT human hepatic cytosolic acetoacetyl-coenzyme A thiolase.";
RL Biochem. Biophys. Res. Commun. 201:478-485(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Chen H., Peng J., Huang C.-H.;
RT "Identification of the human acetyl CoA transferase like (ACTL)
RT protein by yeast two-hybrid screen.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-211.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 16-39; 195-210; 280-302 AND 342-361, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200; LYS-233 AND LYS-235,
RP AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=15733928; DOI=10.1016/j.jmb.2005.01.018;
RA Kursula P., Sikkila H., Fukao T., Kondo N., Wierenga R.K.;
RT "High resolution crystal structures of human cytosolic thiolase (CT):
RT a comparison of the active sites of human CT, bacterial thiolase, and
RT bacterial KAS I.";
RL J. Mol. Biol. 347:189-201(2005).
CC -!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the thiolase family.
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DR EMBL; S70154; AAB30856.1; -; mRNA.
DR EMBL; AF356877; AAM00223.1; -; mRNA.
DR EMBL; AL135914; CAI21850.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47619.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47620.1; -; Genomic_DNA.
DR EMBL; BC000408; AAH00408.1; -; mRNA.
DR PIR; JC2378; JC2378.
DR RefSeq; NP_005882.2; NM_005891.2.
DR UniGene; Hs.571037; -.
DR PDB; 1WL4; X-ray; 1.55 A; A=1-397.
DR PDB; 1WL5; X-ray; 2.26 A; A=1-397.
DR PDBsum; 1WL4; -.
DR PDBsum; 1WL5; -.
DR ProteinModelPortal; Q9BWD1; -.
DR SMR; Q9BWD1; 4-397.
DR STRING; 9606.ENSP00000356015; -.
DR ChEMBL; CHEMBL2240; -.
DR PhosphoSite; Q9BWD1; -.
DR DMDM; 52000838; -.
DR OGP; Q9BWD1; -.
DR REPRODUCTION-2DPAGE; IPI00291419; -.
DR PaxDb; Q9BWD1; -.
DR PeptideAtlas; Q9BWD1; -.
DR PRIDE; Q9BWD1; -.
DR DNASU; 39; -.
DR Ensembl; ENST00000367048; ENSP00000356015; ENSG00000120437.
DR GeneID; 39; -.
DR KEGG; hsa:39; -.
DR UCSC; uc010kjy.3; human.
DR CTD; 39; -.
DR GeneCards; GC06P160153; -.
DR HGNC; HGNC:94; ACAT2.
DR HPA; CAB021106; -.
DR HPA; HPA025736; -.
DR HPA; HPA025765; -.
DR HPA; HPA025811; -.
DR MIM; 100678; gene+phenotype.
DR neXtProt; NX_Q9BWD1; -.
DR PharmGKB; PA19; -.
DR eggNOG; COG0183; -.
DR HOVERGEN; HBG003112; -.
DR InParanoid; Q9BWD1; -.
DR KO; K00626; -.
DR OrthoDB; EOG7JQBNG; -.
DR PhylomeDB; Q9BWD1; -.
DR BioCyc; MetaCyc:ENSG00000120437-MONOMER; -.
DR EvolutionaryTrace; Q9BWD1; -.
DR GeneWiki; ACAT2; -.
DR GenomeRNAi; 39; -.
DR NextBio; 153; -.
DR PRO; PR:Q9BWD1; -.
DR ArrayExpress; Q9BWD1; -.
DR Bgee; Q9BWD1; -.
DR CleanEx; HS_ACAT2; -.
DR Genevestigator; Q9BWD1; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0006629; P:lipid metabolic process; IC:BHF-UCL.
DR Gene3D; 3.40.47.10; -; 4.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR016038; Thiolase-like_subgr.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR18919; PTHR18919; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; FALSE_NEG.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 397 Acetyl-CoA acetyltransferase, cytosolic.
FT /FTId=PRO_0000206409.
FT ACT_SITE 92 92 Acyl-thioester intermediate.
FT ACT_SITE 353 353 Proton acceptor.
FT ACT_SITE 383 383 Proton acceptor.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 200 200 N6-acetyllysine.
FT MOD_RES 233 233 N6-acetyllysine.
FT MOD_RES 235 235 N6-acetyllysine.
FT VARIANT 211 211 K -> R (in dbSNP:rs25683).
FT /FTId=VAR_019686.
FT CONFLICT 169 169 K -> T (in Ref. 1; AAB30856).
FT CONFLICT 262 262 V -> A (in Ref. 1; AAB30856).
FT CONFLICT 375 375 R -> G (in Ref. 2; AAM00223).
FT STRAND 8 15
FT TURN 24 27
FT HELIX 30 45
FT HELIX 49 51
FT STRAND 54 58
FT HELIX 69 76
FT STRAND 85 88
FT HELIX 91 93
FT HELIX 94 107
FT STRAND 112 122
FT STRAND 136 138
FT HELIX 145 149
FT TURN 154 156
FT HELIX 160 171
FT HELIX 175 194
FT TURN 195 201
FT STRAND 205 209
FT STRAND 212 216
FT HELIX 228 232
FT TURN 240 243
FT HELIX 248 250
FT STRAND 255 265
FT HELIX 266 271
FT STRAND 277 287
FT HELIX 290 295
FT HELIX 297 308
FT HELIX 312 314
FT STRAND 317 320
FT HELIX 325 335
FT HELIX 339 341
FT HELIX 348 351
FT TURN 355 357
FT HELIX 358 373
FT STRAND 377 384
FT TURN 385 387
FT STRAND 388 396
SQ SEQUENCE 397 AA; 41351 MW; E3A8DAFB6F341B18 CRC64;
MNAGSDPVVI VSAARTIIGS FNGALAAVPV QDLGSTVIKE VLKRATVAPE DVSEVIFGHV
LAAGCGQNPV RQASVGAGIP YSVPAWSCQM ICGSGLKAVC LAVQSIGIGD SSIVVAGGME
NMSKAPHLAY LRTGVKIGEM PLTDSILCDG LTDAFHNCHM GITAENVAKK WQVSREDQDK
VAVLSQNRTE NAQKAGHFDK EIVPVLVSTR KGLIEVKTDE FPRHGSNIEA MSKLKPYFLT
DGTGTVTPAN ASGINDGAAA VVLMKKSEAD KRGLTPLARI VSWSQVGVEP SIMGIGPIPA
IKQAVTKAGW SLEDVDIFEI NEAFAAVSAA IVKELGLNPE KVNIEGGAIA LGHPLGASGC
RILVTLLHTL ERMGRSRGVA ALCIGGGMGI AMCVQRE
//
MIM
100678
*RECORD*
*FIELD* NO
100678
*FIELD* TI
*100678 ACETYL-CoA ACETYLTRANSFERASE 2; ACAT2
;;ACETOCOENZYME A ACETYLTRANSFERASE 2;;
read moreACETOACETYL-CoA THIOLASE, CYTOSOLIC
*FIELD* TX
DESCRIPTION
The ACAT2 gene encodes cytosolic acetoacetyl-CoA thiolase (EC 2.3.1.9),
which is important in the utilization of ketone bodies (de Groot et al.,
1977). Mitochondrial acetoacetyl-CoA thiolase is encoded by the ACAT1
gene (607809).
CLONING
Song et al. (1994) cloned an ACAT2 cDNA by use of an antibody against
the human enzyme. The deduced amino acid sequence had 34 to 57% homology
with 4 other human thiolases and 4 acetoacetyl-CoA thiolases of
microorganisms.
MAPPING
The TCP1 gene (186980) is located on 6p in the vicinity of the major
histocompatibility complex, and the murine homolog, Tcp1, is located in
the t-complex region of mouse chromosome 17. In the mouse, a related
gene, Tcp1x, is tightly linked to Tcp1. Ashworth (1993) showed that 2
genes located 3-prime to the murine Tcp1 and Tcp1x genes code for
proteins highly homologous to acetyl-CoA acetyltransferases. These Acat
genes are in opposite orientation to the Tcp1 genes, and transcription
results in mRNA species that contain the last exon of Tcp1 or Tcp1x
within the 3-prime untranslated region of the respective Acat mRNA.
Willison et al. (1987) showed that in humans the TCP1 and ACAT2 genes
also overlap. Retention of this close linkage during mammalian evolution
suggests the possibility of some functional significance. Transcription
of both DNA strands at a given locus is common in prokaryotic and viral
systems. For examples of overlapping transcriptional units in humans,
see Morel et al. (1989) and Laudet et al. (1991).
As the human TCP1 gene had been assigned to 6q25-q27 by study of somatic
cell hybrids and by in situ hybridization, the ACAT2 gene was suspected
to be localized to the same chromosome region. By fluorescence in situ
hybridization, Masuno et al. (1996) demonstrated that the ACAT2 gene is
located on 6q25.3-q26.
*FIELD* RF
1. Ashworth, A.: Two acetyl-CoA acetyltransferase genes located in
the t-complex region of mouse chromosome 17 partially overlap the
Tcp-1 and Tcp-1x genes. Genomics 18: 195-198, 1993.
2. de Groot, C. J.; Luit-de Haan, G.; Hulstaert, C. E.; Hoomes, F.
A.: A patient with severe neurologic symptoms and acetoacetyl-CoA
thiolase deficiency. Pediat. Res. 11: 1112-1116, 1977.
3. Laudet, V.; Begue, A.; Henry-Duthoit, C.; Joubel, A.; Martin, P.;
Stehelin, D.; Saule, S.: Genomic organization of the human thyroid
hormone alpha (c-erbA-1) gene. Nucleic Acids Res. 19: 1105-1112,
1991.
4. Masuno, M.; Fukao, T.; Song, X.-Q.; Yamaguchi, S.; Orii, T.; Kondo,
N.; Imaizumi, K.; Kuroki, Y.: Assignment of the human cytosolic acetoacetyl-coenzyme
A thiolase (ACAT2) gene to chromosome 6q25.3-q26. Genomics 36: 217-218,
1996.
5. Morel, Y.; Bristow, J.; Gitelman, S. E.; Miller, W. L.: Transcript
encoded on the opposite strand of the human steroid 21-hydroxylase/complement
component C4 gene locus. Proc. Nat. Acad. Sci. 86: 6582-6586, 1989.
6. Song, X.-Q.; Fukao, T.; Yamaguchi, S.; Miyazawa, S.; Hashimoto,
T.; Orii, T.: Molecular cloning and nucleotide sequence of complementary
DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase. Biochem.
Biophys. Res. Commun. 201: 478-485, 1994.
7. Willison, K.; Kelly, A.; Dudley, K.; Goodfellow, P.; Spurr, N.;
Groves, V.; Gorman, P.; Sheer, D.; Trowsdale, J.: The human homologue
of the mouse t-complex gene, TCP1, is located on chromosome 6 but
is not near the HLA region. EMBO J. 6: 1967-1974, 1987.
*FIELD* CN
Victor A. McKusick - updated: 3/12/2003
*FIELD* CD
Victor A. McKusick: 12/2/1993
*FIELD* ED
carol: 06/21/2011
ckniffin: 6/21/2011
carol: 11/30/2004
mgross: 3/17/2004
carol: 2/25/2004
carol: 5/23/2003
tkritzer: 3/25/2003
terry: 3/12/2003
dkim: 7/17/1998
mark: 9/12/1996
terry: 9/4/1996
carol: 10/12/1994
carol: 12/20/1993
carol: 12/2/1993
*RECORD*
*FIELD* NO
100678
*FIELD* TI
*100678 ACETYL-CoA ACETYLTRANSFERASE 2; ACAT2
;;ACETOCOENZYME A ACETYLTRANSFERASE 2;;
read moreACETOACETYL-CoA THIOLASE, CYTOSOLIC
*FIELD* TX
DESCRIPTION
The ACAT2 gene encodes cytosolic acetoacetyl-CoA thiolase (EC 2.3.1.9),
which is important in the utilization of ketone bodies (de Groot et al.,
1977). Mitochondrial acetoacetyl-CoA thiolase is encoded by the ACAT1
gene (607809).
CLONING
Song et al. (1994) cloned an ACAT2 cDNA by use of an antibody against
the human enzyme. The deduced amino acid sequence had 34 to 57% homology
with 4 other human thiolases and 4 acetoacetyl-CoA thiolases of
microorganisms.
MAPPING
The TCP1 gene (186980) is located on 6p in the vicinity of the major
histocompatibility complex, and the murine homolog, Tcp1, is located in
the t-complex region of mouse chromosome 17. In the mouse, a related
gene, Tcp1x, is tightly linked to Tcp1. Ashworth (1993) showed that 2
genes located 3-prime to the murine Tcp1 and Tcp1x genes code for
proteins highly homologous to acetyl-CoA acetyltransferases. These Acat
genes are in opposite orientation to the Tcp1 genes, and transcription
results in mRNA species that contain the last exon of Tcp1 or Tcp1x
within the 3-prime untranslated region of the respective Acat mRNA.
Willison et al. (1987) showed that in humans the TCP1 and ACAT2 genes
also overlap. Retention of this close linkage during mammalian evolution
suggests the possibility of some functional significance. Transcription
of both DNA strands at a given locus is common in prokaryotic and viral
systems. For examples of overlapping transcriptional units in humans,
see Morel et al. (1989) and Laudet et al. (1991).
As the human TCP1 gene had been assigned to 6q25-q27 by study of somatic
cell hybrids and by in situ hybridization, the ACAT2 gene was suspected
to be localized to the same chromosome region. By fluorescence in situ
hybridization, Masuno et al. (1996) demonstrated that the ACAT2 gene is
located on 6q25.3-q26.
*FIELD* RF
1. Ashworth, A.: Two acetyl-CoA acetyltransferase genes located in
the t-complex region of mouse chromosome 17 partially overlap the
Tcp-1 and Tcp-1x genes. Genomics 18: 195-198, 1993.
2. de Groot, C. J.; Luit-de Haan, G.; Hulstaert, C. E.; Hoomes, F.
A.: A patient with severe neurologic symptoms and acetoacetyl-CoA
thiolase deficiency. Pediat. Res. 11: 1112-1116, 1977.
3. Laudet, V.; Begue, A.; Henry-Duthoit, C.; Joubel, A.; Martin, P.;
Stehelin, D.; Saule, S.: Genomic organization of the human thyroid
hormone alpha (c-erbA-1) gene. Nucleic Acids Res. 19: 1105-1112,
1991.
4. Masuno, M.; Fukao, T.; Song, X.-Q.; Yamaguchi, S.; Orii, T.; Kondo,
N.; Imaizumi, K.; Kuroki, Y.: Assignment of the human cytosolic acetoacetyl-coenzyme
A thiolase (ACAT2) gene to chromosome 6q25.3-q26. Genomics 36: 217-218,
1996.
5. Morel, Y.; Bristow, J.; Gitelman, S. E.; Miller, W. L.: Transcript
encoded on the opposite strand of the human steroid 21-hydroxylase/complement
component C4 gene locus. Proc. Nat. Acad. Sci. 86: 6582-6586, 1989.
6. Song, X.-Q.; Fukao, T.; Yamaguchi, S.; Miyazawa, S.; Hashimoto,
T.; Orii, T.: Molecular cloning and nucleotide sequence of complementary
DNA for human hepatic cytosolic acetoacetyl-coenzyme A thiolase. Biochem.
Biophys. Res. Commun. 201: 478-485, 1994.
7. Willison, K.; Kelly, A.; Dudley, K.; Goodfellow, P.; Spurr, N.;
Groves, V.; Gorman, P.; Sheer, D.; Trowsdale, J.: The human homologue
of the mouse t-complex gene, TCP1, is located on chromosome 6 but
is not near the HLA region. EMBO J. 6: 1967-1974, 1987.
*FIELD* CN
Victor A. McKusick - updated: 3/12/2003
*FIELD* CD
Victor A. McKusick: 12/2/1993
*FIELD* ED
carol: 06/21/2011
ckniffin: 6/21/2011
carol: 11/30/2004
mgross: 3/17/2004
carol: 2/25/2004
carol: 5/23/2003
tkritzer: 3/25/2003
terry: 3/12/2003
dkim: 7/17/1998
mark: 9/12/1996
terry: 9/4/1996
carol: 10/12/1994
carol: 12/20/1993
carol: 12/2/1993