ID   MO4L2_MACFA             Reviewed;         288 AA.
AC   Q4R578;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Mortality factor 4-like protein 2;
GN   Name=MORF4L2; ORFNames=QccE-15641;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC       is involved in transcriptional activation of select genes principally
CC       by acetylation of nucleosomal histone H4 and H2A. This modification may
CC       both alter nucleosome - DNA interactions and promote interaction of the
CC       modified histones with other proteins which positively regulate
CC       transcription. This complex may be required for the activation of
CC       transcriptional programs associated with oncogene and proto-oncogene
CC       mediated growth induction, tumor suppressor mediated growth arrest and
CC       replicative senescence, apoptosis, and DNA repair. The NuA4 complex
CC       ATPase and helicase activities seem to be, at least in part,
CC       contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4
CC       may also play a direct role in DNA repair when directly recruited to
CC       sites of DNA damage. Also a component of the MSIN3A complex which acts
CC       to repress transcription by deacetylation of nucleosomal histones (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC       contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC       TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC       ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC       YEATS4/GAS41 and VPS72/YL1. The NuA4 complex interacts with MYC and the
CC       adenovirus E1A protein. MORF4L1 may also participate in the formation
CC       of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit,
CC       but which include the SWI/SNF related protein SRCAP. Component of the
CC       MSIN3A histone deacetylase complex, which includes SIN3A, HDAC2,
CC       ARID4B, MORF4L1, RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with MRFAP1
CC       and RB1. May also interact with one or more as yet undefined members of
CC       the TLE (transducin-like enhancer of split) family of transcriptional
CC       repressors (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}.
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DR   EMBL; AB169666; BAE01747.1; -; mRNA.
DR   RefSeq; NP_001270298.1; NM_001283369.1.
DR   AlphaFoldDB; Q4R578; -.
DR   SMR; Q4R578; -.
DR   STRING; 9541.XP_005594299.1; -.
DR   GeneID; 101865513; -.
DR   CTD; 9643; -.
DR   eggNOG; KOG3001; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.274.30; -; 1.
DR   InterPro; IPR008676; MRG.
DR   InterPro; IPR038217; MRG_C_sf.
DR   InterPro; IPR026541; MRG_dom.
DR   InterPro; IPR038012; MRGX.
DR   PANTHER; PTHR10880; PTHR10880; 1.
DR   PANTHER; PTHR10880:SF25; PTHR10880:SF25; 1.
DR   Pfam; PF05712; MRG; 1.
DR   PROSITE; PS51640; MRG; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; DNA damage; DNA repair; Growth regulation; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..288
FT                   /note="Mortality factor 4-like protein 2"
FT                   /id="PRO_0000247602"
FT   DOMAIN          117..288
FT                   /note="MRG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15014"
SQ   SEQUENCE   288 AA;  32380 MW;  9D0C42C9AC550183 CRC64;
     MSSRKQGSQP RGQQSAEEEN FKKPTRSNMQ RSKMRGASSG KKTAGPQQKN LEPALPGRWG
     GRSAENPPSG SVRKTRKNKQ KTPGNEDGGS TSEAPQPPRK KRARADPTVE SEEAFKNRME
     VKVKIPEELK PWLVEDWDLV TRQKQLFQLP AKKNVDAILE EYANCKKSQG NVDNKEYAVN
     EVVAGIKEYF NVMLGTQLLY KFERPQYAEI LLAHPDAPMS QVYGAPHLLR LFVRIGAMLA
     YTPLDEKSLA LLLGYLHDFL KYLAKNSASL FTASDYKVAS AEYHRKAL