ID A0A8L2QED5_RAT Unreviewed; 523 AA. AC A0A8L2QED5; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 14-DEC-2022, entry version 3. DE RecName: Full=Histone acetyltransferase {ECO:0000256|RuleBase:RU361211}; DE EC=2.3.1.48 {ECO:0000256|RuleBase:RU361211}; GN Name=Bckdk {ECO:0000313|Ensembl:ENSRNOP00000026527.4, GN ECO:0000313|RGD:2198}; Synonyms=Kat8 {ECO:0000313|RGD:1311512}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000026527.4, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000026527.4, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026527.4, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000026527.4} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026527.4}; RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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:0000256|RuleBase:RU361211}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}. CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSRNOT00000026527.5; ENSRNOP00000026527.4; ENSRNOG00000019485.7. DR RGD; 2198; Bckdk. DR RGD; 1311512; Kat8. DR GeneTree; ENSGT00940000159512; -. DR Proteomes; UP000002494; Chromosome 1. DR GO; GO:0072487; C:MSL complex; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro. DR GO; GO:0016573; P:histone acetylation; IEA:InterPro. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:UniProt. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR002717; HAT_MYST-type. DR InterPro; IPR037906; KAT8. DR InterPro; IPR025995; Tudor-knot. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR040706; Zf-MYST. DR PANTHER; PTHR10615:SF82; HISTONE ACETYLTRANSFERASE KAT8; 1. DR Pfam; PF01853; MOZ_SAS; 1. DR Pfam; PF11717; Tudor-knot; 1. DR Pfam; PF17772; zf-MYST; 1. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR PROSITE; PS51726; MYST_HAT; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Activator {ECO:0000256|ARBA:ARBA00023159}; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Chromosome {ECO:0000256|ARBA:ARBA00022454}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022771}; KW Nucleus {ECO:0000256|RuleBase:RU361211}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Zinc {ECO:0000256|ARBA:ARBA00022771}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 239..512 FT /note="MYST-type HAT" FT /evidence="ECO:0000259|PROSITE:PS51726" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 81..116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..47 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 415 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51" SQ SEQUENCE 523 AA; 59679 MW; BA675E84F663A50F CRC64; MSSKRKRNQI GPISSNNSPT EYALLNKTLP RHNLPTSNTQ TMPAPTDPEL KTSLCLIARI TSGTAMAAQG ATAAVAATTS GIVGEGEPGP GENTSVEGPA RSPGRVSPPT PARGEPEVTV EIGETYLCRR PDSTWHSAEV IQSRVNDQEG REEFYVHYVG FNRRLDEWVD KNRLALTKTV KDAVQKNSEK YLSELAEQPE RKITRNQKRK HDEINHVQKT YAEMDPTTAA LEKEHEAITK VKYVDKIHIG NYEIDAWYFS PFPEDYGKQP KLWLCEYCLK YMKFEKSYRF HLGQCQWRQP PGKEIYRKSN ISVYEVDGKD HKIYCQNLCL LAKLFLDHKT LYFDVEPFVF YILTEVDRQG AHIVGYFSKE KESPDGNNVA CILTLPPYQR RGYGKFLIAF SYELSKLEST VGSPEKPLSD LGKLSYRSYW SWVLLEILRD FRGTLSIKDL SQMTSITQND IISTLQSLNM VKYWKGQHVI CVTPKLVEEH LKSAQYKKPP ITVDSVCLKW APPKHKQVKL SKK //