ID H2LWE6_ORYLA Unreviewed; 2423 AA.
AC H2LWE6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=LOC101155770 {ECO:0000313|Ensembl:ENSORLP00000010434.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000010434.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000010434.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000010434.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000010434.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000010434.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR STRING; 8090.ENSORLP00000010434; -.
DR Ensembl; ENSORLT00000010435.2; ENSORLP00000010434.2; ENSORLG00000008296.2.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000155364; -.
DR HOGENOM; CLU_000162_2_0_1; -.
DR InParanoid; H2LWE6; -.
DR OrthoDB; 5490807at2759; -.
DR TreeFam; TF101097; -.
DR Proteomes; UP000001038; Chromosome 8.
DR Bgee; ENSORLG00000008296; Expressed in testis and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15647; PHD_CBP; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF56; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 307..393
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 544..623
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1045..1117
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1275..1652
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1654..1702
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1717..1798
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 307..393
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1717..1798
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1825..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1985..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2114..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2278..2304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2323..2395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..892
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1554
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1889..1903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2114..2171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2337..2371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2379..2395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2423 AA; 266062 MW; 77D119F3A1F4B940 CRC64;
MADNLLDAVP PMAKRPKLNS PLSGSDGPDL VSLFDLENDL PDELIPNGET GLSTISGPGG
GGPGHNSVIP DAAAKHKQLS ELLRPGSSST LGGTFNSSIG SQLGSVLGKG PLGQGSPNHQ
NSPQGQKVGV PSGQSNGSTG MGFNQALLNS GQSHGMMGQT GQVMNGAMGP MGRGRPGMQY
QGQGMQGTQV SPGPGVGGSA LAETLTQGGP QMAVHNTMNA QQSGNMNKMA MSGAQFSQQY
GPTGVQQMGS AVNPQLQSKA AISNNLPQFH AADLKGVGNV PNMMQQQVAS MGMVAGAGGV
SGGPTADPEK RKLIQQQLVL LLHAHKCQRR EQANGEVRSC ALPHCRTMKN VLNHMTHCQA
GKSCQVAHCA SSRQIISHWK NCTRHDCPVC LPLKNASDKR NQQPLLSSPG ANLQKAINTA
GPSQPSATTI SSGTSHIDPS SMQRAYAALG LPYGNQSSAQ VQGQGPAQQN PPGTQHQQLR
NMNALGANQM NQMPGNMGTS STDQSGLHSD SSLPSTLHNQ LMTDGSVLGG IGNLPTATPL
SATGVRKAWH EHVTQDLRTH LVHKLVQAIF PTPDPAALKD RRMDNLVAYA RKVEGDMYES
ANSRDEYYHF LAEKIYKIQK ELEEKRRSRE KDRNVVATAR SQQPGLPQPN TMCPAQPVRP
PNGPVSMPNM PNQMMNRMQV PQGINHFNPM TMQNPQMPQA PMGARAPSPM SHPQQMNMPP
VQPMGVSPTG ISHNQGVMSS HTNNMVSQQP NQVQFMPQGQ FQSSTSGAMN VNVGSGQAMS
QAAAAQQPQN SSLPMNALGS LGSQLPPGPT AQPPLGTTPP PNASATLQPH QQQTPHAAAQ
AQVPRPSTPS SSMGSSFTPS HIPNSLPRPP STMGPPSVPS QPVTPQQPQP EPPSQMQQCT
SVQAQHPSTP LSQAAASVDN RVPTPGSVAE PGSHPVLPDM NGTEVKSVKN EEDENCIEKK
PDDIKMEQDD ETKPSVVKKE EPDAAKPKQE PMEAEPAIKT EVKTEPKEEE EGGANSTSTS
QNHKKIFKPE ELRQALMPTL EALYRQDPES LPFRQPVDPM LLGIPDYFDI VKNPIDLSTI
KRKLDTGQYQ EPWQYVEDVW LMFNNAWLYN RKTSRVYKYC TKLAEVFEVE IDPVMQSLGY
CCGRKYEFSP QTLCCYGKQL CTISRDGTYY SYQNSSPKYG LIADRYHFCE KCFNEIQGNS
VTLGDDPAQP QTVISKEQFE KKKNDTLDPE PFVECKDCER KMHQICVLHY EVIWPSGFIC
DNCLKKSGKT KKENKFSARR LQTTRLGTYI EDRVNKYLKR QNHPEAGEVF VRVVASSDKS
VDVKPGMKSR FVDSGEMMEN FPYRTKALFA FEEIDGVDVC FFGMHVQEYG SDCPFPNTRR
VYISYLDSVH FFKPRLLRTA VYHEILIGYL EYVKKLGYVM GHIWACPPSE GDDYIFHCHP
PDQKIPKPKR LQEWYRKMLD KAFAERILHD YKDIFKQATE DRLTSANELP YFEGDFWPNV
LEESIKELEQ EEEERKKEEN TASSETTEGA QADSKNAKKK NNKKTNKNKS SLSRANKKKP
GMPNVANDLS QKLYATMEKH KEVFFVIHLH AGPVINTLPP IMDPDPLLTC DLMDGRDAFL
TLARDKHWEF SSLRRCKWST MCMLVELHNQ GQDRFVYTCN ECKHHVETRW HCTVCEDYDL
CINCYKTKGH EHQMVKWGLG LDDDSNGQGG EASKSPQENR RLSIQRCIQS LVHACQCRNA
NCSLSSCQKM KRVVQHTKGC KRKTNGGCPV CKQLIALCCY HAKHCQENKC PVPFCLNIKQ
KLHQQQLQHR LHQAQMMRRR MATMAGRGMP MPSPPTSTAL DTPNSLQQPN TPQTPQPMPN
QPQQQPPNPA NIAQGFPGNG RGSQPTTPVP QGKPGPPSSP LHQQLSPMPN MPHQQQPPPP
QQQQQLLAAQ KVAHEIQMVA KAKQLQTNYA MNGMHMNHSR MMGPGPNQMQ MVQGPRGPQV
MPAMQQGQWN PGMQKPQGSQ PQVPPQQGPM VSQQAQGTPM LQPGQLMQRP MMPQQHGLQM
PGVMPSQMPS QQGMTQQQQN MPRGIPSNIT QNALQELLHF LKSPSSPHQQ QQVLTILKSN
PHLMAAFIKQ RTAKYQASQQ PQQQQQQQAQ QQQNPQAMMG SQAGMQVMSS MANQVPRPGI
SPQQQPRQPA GPQGMMSIGP QGQMMNPAQN GNPQLYRRQQ MFRMQQMQSQ GGLNQVHGQF
PPQQTGQANF SQICMQQQMT MQGGGGPMSQ LPPTSQMGQP GMGVDSSRMV LQQRLLQPQQ
MKQQMGSPAQ ANSMSPQPHM LQGQAPGVAH LQGQTMANTL GNQVRSPAPV QSPRPPSQQA
PHSGSSPRIQ PHPSPQHAAL HSNSPHPSLA PMSGSMEQGH MGTPEQSAML PQLNTPNRGA
LGNDMGMVGD TTGDTLEKFV EGL
//