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Database: UniProt
Entry: A0A286XG95_CAVPO
LinkDB: A0A286XG95_CAVPO
Original site: A0A286XG95_CAVPO 
ID   A0A286XG95_CAVPO        Unreviewed;       753 AA.
AC   A0A286XG95;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   Name=KAT2A {ECO:0000313|Ensembl:ENSCPOP00000024480.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000024480.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000024480.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000024480.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008607}.
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DR   EMBL; AAKN02042412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_013005129.1; XM_013149675.1.
DR   AlphaFoldDB; A0A286XG95; -.
DR   STRING; 10141.ENSCPOP00000024480; -.
DR   Ensembl; ENSCPOT00000046161.1; ENSCPOP00000024480.1; ENSCPOG00000040409.1.
DR   GeneID; 100716533; -.
DR   KEGG; cpoc:100716533; -.
DR   CTD; 2648; -.
DR   VEuPathDB; HostDB:ENSCPOG00000040409; -.
DR   GeneTree; ENSGT00940000158799; -.
DR   InParanoid; A0A286XG95; -.
DR   OMA; YFQTKMR; -.
DR   OrthoDB; 1760108at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000040409; Expressed in frontal cortex and 13 other cell types or tissues.
DR   GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR   GO; GO:0000124; C:SAGA complex; IEA:Ensembl.
DR   GO; GO:0033276; C:transcription factor TFTC complex; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0106229; F:histone glutaryltransferase activity; IEA:Ensembl.
DR   GO; GO:0043993; F:histone H3K18 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0043992; F:histone H3K9 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0106078; F:histone succinyltransferase activity; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR   GO; GO:0022037; P:metencephalon development; IEA:Ensembl.
DR   GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0046600; P:negative regulation of centriole replication; IEA:Ensembl.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1903010; P:regulation of bone development; IEA:Ensembl.
DR   GO; GO:0061035; P:regulation of cartilage development; IEA:Ensembl.
DR   GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR   GO; GO:0045589; P:regulation of regulatory T cell differentiation; IEA:Ensembl.
DR   GO; GO:2000036; P:regulation of stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 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; GH11602P; 1.
DR   PANTHER; PTHR45750:SF1; HISTONE ACETYLTRANSFERASE KAT2A; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          427..572
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          661..731
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   ACT_SITE        491
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
FT   BINDING         495..497
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT   BINDING         502..508
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
FT   BINDING         533..536
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-2"
SQ   SEQUENCE   753 AA;  86457 MW;  742F1B1B878F1FEA CRC64;
     MQAGRWERVG AGCRRWPGVH CHDSPSRTQA NETCKCNGWK NPKPPTAPRM DLHQPAANLG
     ELCRSCEHPL ADHVSHLENV SEDEINRLLG MVVDVENLFM SVHKEEDTDT KQVYFYLFKL
     LRKCILQMTR PVVEGSLGSP PFEKPNIEQG VLNFVQYKFS HLAPRERQTM FELSKMFLLC
     LNYWKLETPA QFRQRSQSED VATYKVNYTR WLCYCHVPQS CDSLPRYETT HVFGRSLLRS
     IFTVTRRQLL EKFRVEKDKL VPEKRTLILT HFPKFLSMLE EEIYGANSPI WESGFTMPPS
     EGTQLVPRPA TVSAAVVPST PIFSPTMGGG NNTSLSLDAA GAEPMPGEKR KLPENLTLED
     AKRLRVMGDI PMELVNEVML TITDPAAMLG PETSLLSANA ARDETARLEE RRGIIEFHVI
     GNSLAPKANR RVLLWLVGLQ NVFSHQLPRM PKEYIARLVF DPKHKTLALI KDGRVIGGIC
     FRMFPTQGFT EIVFCAVTSN EQVKGYGTHL MNHLKEYHIK HGILYFLTYA DEYAIGYFKK
     QGFSKDIKVP KSRYLGYIKD YEGATLMECE LNPRIPYTEL SHIIKKQKEI IKKLIERKQA
     QIRKVYPGLS CFKEGVRQIP VESVPGIRET GWKPLGKEKG KELKDPDQLY TTLKNLLAQI
     KSHPSAWPFM EPVKKSEAPD YYEVIRFPID LRTMSERLRS RYYVTRKLFV ADLQRVIANC
     REYNPPDSEY CRCASALEKF FYFKLKEGGL IDK
//
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