ID M4ABV7_XIPMA Unreviewed; 2358 AA.
AC M4ABV7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000011951.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000011951.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000011951.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSXMAT00000011967.2; ENSXMAP00000011951.2; ENSXMAG00000011929.2.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000155364; -.
DR HOGENOM; CLU_022938_0_0_1; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
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:SF34; CREB-BINDING PROTEIN; 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:UP000002852};
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 359..445
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 604..683
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 986..1058
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1206..1583
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1585..1633
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1647..1728
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 359..445
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1647..1728
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1439..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1903..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1950..1981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2106..2136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2191..2341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1485
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2024..2048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2191..2233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2248..2264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2273..2287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2314..2336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2358 AA; 256594 MW; A81F90AE6C9F3F73 CRC64;
MAENLLDVGP PSSKRPKLNS PALSASDGQD LGSLPWDDLE NDLPDELIPN GGELSQLSGL
PSNGGATPGG GPGGTAGALG GGAAIVPDAA SKHKQLSELL RAGSTSSITG TGLNSASPQP
GSMAPQLGTP LGKSPLGQGS PNSHSSPQGQ KPGTPTGVVG QNSNNNAAAM GLSATGFSQA
MINNSPGHSG LLGQGGQPQP GQVMNGGLVP SGGRGRGAGV AGLQYQGQTI PGSTAGPGAS
GSALVETLTQ GGQQMGAHAA QQAGNMNKMS LGSNGSLFGA QPYGQGAAGP GQQLNPQQQL
QNKAALASSL PPFPNELKGA AVTSGPNMQL QQPPQQQAGM LPLANSGGVA VSSAGPTADP
EKRKLIQQQL VLLLHAHKCQ RREQANGEVR QCALPHCRTM KNVLNHMTHC QAGKSCQVAH
CASSRQIISH WKNCTRHDCP VCLPLKNASD KRTQQPLLSS PNTGLQNPMS TVGMGQPSAP
TINTSAPIDP SSMQRAYAAL GLPYSSQAAG QAAAQQAPGQ AAGAQNSQAQ QQQQLPQQMR
PINTIGNQMA LGGGAMGVAT SEQTNLHTDS LSNTLNTNNQ LLSDGSAVGQ MGSLPTAAPV
SSASARKAWH EHVTQDLRNH LVHKLVQAIF PTPDPAALKD RRMENLVAYA RKVEGDMYES
ANSRDEYYHF LAEKIYKIQK ELEEKRRSRL QKQIISQAPI AGQGTQQPGL PQPNALGPRP
QNGPVSLPNM PNQIMNRIQV PQGMNQFNHM TLSNAQTSMG PRAASPMTHP QQMNISSVPA
VGMSPSRMPQ AQGIMPGHSN MVGQTPSQGQ FLPQTHFTPG SGAVSVSSAM NVTVGPGMGQ
PPAQAPVTQL SQPGASLDNR VPTPASAASA DLHSQHVGAD LPAQDLKAET RTDQQEFEAA
GGKIEPKTEA ENDSASASVK KEEPEEKPEP MEVEEKKPEM KTEPKEEEEN GTNGTTSSSP
SQSRRKIFKP EELRQALMPT LESLYRQDPE SLPFRQPVDP MLLGIPDYFD IVKNPIDLST
IKRKLDTGQY QEPWQYVDDV WLMFNNAWLY NRKTSRVYKY CSKLAEVFES EIDPVMQGLG
YCCGRKYEFS PQTLCCYGKQ LCTIPTGGTY YSYQNRYHFC EKCFNEIQGD SVTLGDDPAQ
PQTMISKDQF ERRKNDVLDP EPFVECKDCG RKMHQICVLH YEVIWPSGFI CDNCLKKSAK
SRKENKFTAK RLQSTRLGMY IEDRVNKYLK RQNHPEAGEV FVRVVASSDK TVEVKPGMKA
RFVDTGEMPD TFPYRTKALF AFEEIDGVDV CFFGMHVQEY GSECPFPNTR RVYISYLDSI
HFFRPRVLRT AVYHEILIGY LEYVKKLGYT QGHIWACPPS EGDDYIFHCH PPEQKIPKPK
RLQEWYRKML DKAFAERILH DYKDIFKQAT EDRLTSANEL PYFEGDFWPN VLEESIKELE
QEEEERKKEE TTAATETPEG TPSDSKNAKK KNNKKTNKNK SSVSRANKKK PGMPNVANDL
SQKLYATMEK HKEVFFVIHL HSGPLANTLP PIVDPDPMIS CDLMDGRDAF LTLARDKHWE
FSSLRRCKWS TMCMLVELHN QGQDRFVYTC NECKHHVETR WHCTVCEDFD LCISCYNTKG
HEHQMVKWGL GLDDDNSQSG EASKSPQESR RLSIQRCIQS LVHACQCRNA NCSLPSCQKM
KRVVQHTKGC KRKTNGGCPV CKQLIALCCY HAKHCQENKC PVPFCLNIKH KLRQQQLQHR
LQQAQLMRRR MATMQGRTMP LPSPPAAAAP STPTSHAQPS TPQTPQQPLS NQPPTPNSAG
VTSPTFPGVP RAGPPQASVS QGKPGPHASP LHQQQSPLPQ PPQQRQQQAP LAAIKMAHHI
EMMAQAQQNQ QNYRVNMNGL PMTPQQTQQQ RMAQTMQMVA GPRGPQVMQQ PSLGQWPAAA
GPMPAQNQQP GVVPNQNTPQ QAMSIQRAMM APGQQGQQRM LMPQQPGPRP QTPQRTGTIP
PNALQDLLRT LKSPSSPQQQ QQVLNILKSN PQLMAAFIKQ RTAKYHASQP QPQAGQPQQP
QQQQPGMPAM QTIAMQGGPV QRAAMPPQQP QQAPVQGMAQ LGSGQLMNAA HNANPQIQEL
YRRQLLRQQQ QQQQPQQQGV MPQGHLGQFP NQPQGTSVMY SHIRMQQQQQ QQIAMQQAGA
AGAGGVTMGQ LPPMAQMAQP GMSMDSAQNL LHQRMQQQQQ QAQLPQQQQA VLKQQMGSPA
HPSPMSPQTH LLAGQAQGAA HLSAQPGLAN ALGNQVRSPA PVQSPAQQQQ PPPHSSPSRQ
VQNQPQPSPQ HPALPHSGSP HPVLGGPLQS LEQGHLGTPE QSAMLPQLNT PNRGALSSDL
GLVGDATGDT LERFVEGL
//