KAT2B_MOUSE
ID KAT2B_MOUSE Reviewed; 813 AA.
AC Q9JHD1; Q3U142; Q640M9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Histone acetyltransferase KAT2B;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92831};
DE AltName: Full=Histone acetyltransferase PCAF {ECO:0000303|PubMed:11017084};
DE Short=Histone acetylase PCAF {ECO:0000303|PubMed:11017084};
DE AltName: Full=Lysine acetyltransferase 2B {ECO:0000305};
DE AltName: Full=P300/CBP-associated factor {ECO:0000303|PubMed:11017084};
DE Short=P/CAF {ECO:0000303|PubMed:11017084};
DE AltName: Full=Spermidine acetyltransferase KAT2B;
DE EC=2.3.1.57 {ECO:0000250|UniProtKB:Q92831};
GN Name=Kat2b {ECO:0000312|MGI:MGI:1343094};
GN Synonyms=Pcaf {ECO:0000303|PubMed:11017084};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9742083; DOI=10.1128/mcb.18.10.5659;
RA Xu W., Edmondson D.G., Roth S.Y.;
RT "Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal
RT domains important for recognition of nucleosomal substrates.";
RL Mol. Cell. Biol. 18:5659-5669(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11017084; DOI=10.1038/79973;
RA Xu W., Edmondson D.G., Evrard Y.A., Wakamiya M., Behringer R.R., Roth S.Y.;
RT "Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects during
RT mouse development.";
RL Nat. Genet. 26:229-232(2000).
RN [5]
RP INTERACTION WITH NR4A3.
RX PubMed=12709428; DOI=10.1074/jbc.m300088200;
RA Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.;
RT "The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans-
RT activation, coactivator recruitment, and activation by the purine anti-
RT metabolite 6-mercaptopurine.";
RL J. Biol. Chem. 278:24776-24790(2003).
RN [6]
RP INTERACTION WITH NR2C1.
RX PubMed=17187077; DOI=10.1038/nsmb1185;
RA Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
RT "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
RT expression in stem cells.";
RL Nat. Struct. Mol. Biol. 14:68-75(2007).
RN [7]
RP INTERACTION WITH NR2C1.
RX PubMed=18682553; DOI=10.1073/pnas.0710561105;
RA Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P.,
RA Wei L.N.;
RT "Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and
RT SUMOylation of nuclear receptor TR2 to suppress Oct4 expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008).
RN [8]
RP INTERACTION WITH RB1.
RX PubMed=20940255; DOI=10.1242/jcs.068924;
RA Pickard A., Wong P.P., McCance D.J.;
RT "Acetylation of Rb by PCAF is required for nuclear localization and
RT keratinocyte differentiation.";
RL J. Cell Sci. 123:3718-3726(2010).
CC -!- FUNCTION: Functions as a histone acetyltransferase (HAT) to promote
CC transcriptional activation. Has significant histone acetyltransferase
CC activity with core histones (H3 and H4), and also with nucleosome core
CC particles. Also acetylates non-histone proteins, such as ACLY,
CC MAPRE1/EB1, PLK4, RRP9/U3-55K and TBX5. Acts as a circadian
CC transcriptional coactivator which enhances the activity of the
CC circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-
CC ARNTL/BMAL1 heterodimers. Involved in heart and limb development by
CC mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic
CC shuttling of TBX5. Acts as a negative regulator of centrosome
CC amplification by mediating acetylation of PLK4. Acetylates RRP9/U3-55K,
CC a core subunit of the U3 snoRNP complex, impairing pre-rRNA processing.
CC Acetylates MAPRE1/EB1, promoting dynamic kinetochore-microtubule
CC interactions in early mitosis. Also acetylates spermidine.
CC {ECO:0000250|UniProtKB:Q92831}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q92831};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(8)-acetylspermidine;
CC Xref=Rhea:RHEA:28270, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:Q92831};
CC -!- SUBUNIT: Interacts with BCAS3. Interacts with SIRT1. Interacts with
CC EP300, CREBBP and DDX17. Component of a large chromatin remodeling
CC complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5.
CC Interacts with KLF1; the interaction does not acetylate KLF1 and there
CC is no enhancement of its transactivational activity. Interacts with
CC NFE4. Interacts with MECOM. Interacts with NR2C2 (hypophosphorylated
CC and unsumoylated form); the interaction promotes the transactivation
CC activity of NR2C2. Interacts with NFE4. Interacts with MECOM. Interacts
CC with E2F1; the interaction acetylates E2F1 augmenting its DNA-binding
CC and transcriptional activity. Interacts with NPAS2, ARNTL/BMAL1 and
CC CLOCK (By similarity). Interacts (unsumoylated form) with NR2C1; the
CC interaction promotes transactivation activity. Interacts with CEBPB (By
CC similarity). Interacts with NR4A3 (PubMed:12709428). Interacts with
CC TBX5 (By similarity). Interacts with PLK4 (By similarity). Interacts
CC with RB1; this interaction leads to RB1 acetylation (PubMed:20940255).
CC {ECO:0000250|UniProtKB:Q92831, ECO:0000269|PubMed:12709428,
CC ECO:0000269|PubMed:17187077, ECO:0000269|PubMed:18682553,
CC ECO:0000269|PubMed:20940255}.
CC -!- INTERACTION:
CC Q9JHD1; Q505F1: Nr2c1; NbExp=3; IntAct=EBI-2325611, EBI-15617004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92831}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q92831}. Note=Mainly localizes to the nucleus.
CC Also localizes to centrosomes in late G1 and around the G1/S
CC transition, coinciding with the onset of centriole formation.
CC {ECO:0000250|UniProtKB:Q92831}.
CC -!- DEVELOPMENTAL STAGE: Expression is low during embryogenesis and becomes
CC up-regulated in some adult tissues including heart and skeletal muscle.
CC {ECO:0000269|PubMed:11017084}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:11017084).
CC {ECO:0000269|PubMed:11017084}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF254442; AAF70498.1; -; mRNA.
DR EMBL; AK156290; BAE33658.1; -; mRNA.
DR EMBL; BC082581; AAH82581.1; -; mRNA.
DR EMBL; BC145896; AAI45897.1; -; mRNA.
DR CCDS; CCDS28880.1; -.
DR RefSeq; NP_064389.2; NM_020005.4.
DR PDB; 5ML0; X-ray; 1.64 A; A=705-813.
DR PDBsum; 5ML0; -.
DR AlphaFoldDB; Q9JHD1; -.
DR SMR; Q9JHD1; -.
DR BioGRID; 202042; 23.
DR ComplexPortal; CPX-1024; PCAF histone acetylase complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR CORUM; Q9JHD1; -.
DR DIP; DIP-29281N; -.
DR IntAct; Q9JHD1; 4.
DR MINT; Q9JHD1; -.
DR STRING; 10090.ENSMUSP00000000724; -.
DR iPTMnet; Q9JHD1; -.
DR PhosphoSitePlus; Q9JHD1; -.
DR jPOST; Q9JHD1; -.
DR MaxQB; Q9JHD1; -.
DR PaxDb; Q9JHD1; -.
DR PRIDE; Q9JHD1; -.
DR ProteomicsDB; 263573; -.
DR Antibodypedia; 3865; 463 antibodies from 39 providers.
DR DNASU; 18519; -.
DR Ensembl; ENSMUST00000000724; ENSMUSP00000000724; ENSMUSG00000000708.
DR GeneID; 18519; -.
DR KEGG; mmu:18519; -.
DR UCSC; uc008czp.2; mouse.
DR CTD; 8850; -.
DR MGI; MGI:1343094; Kat2b.
DR VEuPathDB; HostDB:ENSMUSG00000000708; -.
DR eggNOG; KOG1472; Eukaryota.
DR GeneTree; ENSGT00940000154995; -.
DR HOGENOM; CLU_015901_0_0_1; -.
DR InParanoid; Q9JHD1; -.
DR OMA; DFAIGYF; -.
DR OrthoDB; 349249at2759; -.
DR PhylomeDB; Q9JHD1; -.
DR TreeFam; TF105399; -.
DR BRENDA; 2.3.1.48; 3474.
DR Reactome; R-MMU-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR Reactome; R-MMU-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR BioGRID-ORCS; 18519; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Kat2b; mouse.
DR PRO; PR:Q9JHD1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JHD1; protein.
DR Bgee; ENSMUSG00000000708; Expressed in pigmented layer of retina and 261 other tissues.
DR ExpressionAtlas; Q9JHD1; baseline and differential.
DR Genevisible; Q9JHD1; MM.
DR GO; GO:0031672; C:A band; IDA:MGI.
DR GO; GO:0042641; C:actomyosin; IDA:MGI.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
DR GO; GO:0031674; C:I band; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000124; C:SAGA complex; IC:ComplexPortal.
DR GO; GO:0016407; F:acetyltransferase activity; EXP:Reactome.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IGI:MGI.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IDA:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IC:ComplexPortal.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IGI:MGI.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IMP:UniProtKB.
DR GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:2000233; P:negative regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; ISO:MGI.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006473; P:protein acetylation; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IC:ComplexPortal.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IC:ComplexPortal.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR016376; GCN5/PCAF.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR009464; PCAF_N.
DR PANTHER; PTHR45750; PTHR45750; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF06466; PCAF_N; 1.
DR PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Acyltransferase; Biological rhythms; Bromodomain;
KW Cell cycle; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..813
FT /note="Histone acetyltransferase KAT2B"
FT /id="PRO_0000322986"
FT DOMAIN 484..632
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 721..791
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 551
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 555..557
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 562..568
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 593..596
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT CONFLICT 293..294
FT /note="LL -> FV (in Ref. 1; AAF70498)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="E -> G (in Ref. 2; BAE33658)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="H -> L (in Ref. 1; AAF70498)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="G -> A (in Ref. 1; AAF70498)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="F -> L (in Ref. 1; AAF70498)"
FT /evidence="ECO:0000305"
FT HELIX 707..722
FT /evidence="ECO:0007829|PDB:5ML0"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:5ML0"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:5ML0"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:5ML0"
FT HELIX 751..759
FT /evidence="ECO:0007829|PDB:5ML0"
FT HELIX 766..783
FT /evidence="ECO:0007829|PDB:5ML0"
FT HELIX 789..807
FT /evidence="ECO:0007829|PDB:5ML0"
SQ SEQUENCE 813 AA; 91769 MW; 38E52F326794F523 CRC64;
MAEAGGAGSP ALPPAPPHGS PRTLATAAGS SASCGPATAV AAAGTAEGPG GGGSARIAVK
KAQLRSAPRA KKLEKLGVYS ACKAEESCKC NGWKNPNPSP TPPRGDLQQI IVSLTESCRS
CSHALAAHVS HLENVSEEEM DRLLGIVLDV EYLFTCVHKE EDADTKQVYF YLFKLLRKSI
LQRGKPVVEG SLEKKPPFEK PSIEQGVNNF VQYKFSHLPS KERQTTIELA KMFLNRINYW
HLEAPSQRRL RSPNDDISGY KENYTRWLCY CNVPQFCDSL PRYETTKVFG RTLLRSVFTI
MRRQLLEQAR QEKDKLPLEK RTLILTHFPK FLSMLEEEVY SQNSPIWDQD FLSASSRTSP
LGIQTVISPP VTGTALFSSN STSHEQINGG RTSPGCRGSS GLEANPGEKR KMNNSHAPEE
AKRSRVMGDI PVELINEVMS TITDPAGMLG PETNFLSAHS ARDEAARLEE RRGVIEFHVV
GNSLNQKPNK KILMWLVGLQ NVFSHQLPRM PKEYITRLVF DPKHKTLALI KDGRVIGGIC
FRMFPSQGFT EIVFCAVTSN EQVKGYGTHL MNHLKEYHIK HEILNFLTYA DEYAIGYFKK
QGFSKEIKIP KTKYVGYIKD YEGATLMGCE LNPQIPYTEF SVIIKKQKEI IKKLIERKQA
QIRKVYPGLS CFKDGVRQIP IESIPGIRET GWKPSGKEKS KEPKDPEQLY STLKNILQQV
KNHPNAWPFM EPVKRTEAPG YYEVIRFPMD LKTMSERLRN RYYVSKKLFM ADLQRVFTNC
KEYNPPESEY YKCASILEKF FFSKIKEAGL IDK
