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MO4L2_RAT
ID   MO4L2_RAT               Reviewed;         288 AA.
AC   Q6QI89;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Mortality factor 4-like protein 2;
DE   AltName: Full=Liver regeneration-related protein LRRG00119;
DE   AltName: Full=MORF-related gene X protein;
DE   AltName: Full=Transcription factor-like protein MRGX;
GN   Name=Morf4l2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RA   Xu C.S., Zhang L., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA   Yang K.J., Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M.,
RA   Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; AY539870; AAS66210.1; -; mRNA.
DR   EMBL; BC083606; AAH83606.1; -; mRNA.
DR   RefSeq; NP_001007715.1; NM_001007714.1.
DR   RefSeq; XP_006257357.1; XM_006257295.2.
DR   RefSeq; XP_006257358.1; XM_006257296.3.
DR   RefSeq; XP_006257359.1; XM_006257297.2.
DR   RefSeq; XP_017457558.1; XM_017602069.1.
DR   AlphaFoldDB; Q6QI89; -.
DR   SMR; Q6QI89; -.
DR   IntAct; Q6QI89; 1.
DR   MINT; Q6QI89; -.
DR   STRING; 10116.ENSRNOP00000003247; -.
DR   PhosphoSitePlus; Q6QI89; -.
DR   jPOST; Q6QI89; -.
DR   PaxDb; Q6QI89; -.
DR   PRIDE; Q6QI89; -.
DR   Ensembl; ENSRNOT00000003247; ENSRNOP00000003247; ENSRNOG00000002389.
DR   Ensembl; ENSRNOT00000093840; ENSRNOP00000077798; ENSRNOG00000002389.
DR   Ensembl; ENSRNOT00000103331; ENSRNOP00000083693; ENSRNOG00000002389.
DR   Ensembl; ENSRNOT00000108398; ENSRNOP00000084568; ENSRNOG00000002389.
DR   Ensembl; ENSRNOT00000108536; ENSRNOP00000081349; ENSRNOG00000002389.
DR   Ensembl; ENSRNOT00000113826; ENSRNOP00000094505; ENSRNOG00000002389.
DR   Ensembl; ENSRNOT00000116026; ENSRNOP00000076571; ENSRNOG00000002389.
DR   GeneID; 317413; -.
DR   KEGG; rno:317413; -.
DR   UCSC; RGD:1359471; rat.
DR   CTD; 9643; -.
DR   RGD; 1359471; Morf4l2.
DR   eggNOG; KOG3001; Eukaryota.
DR   GeneTree; ENSGT00950000182965; -.
DR   HOGENOM; CLU_039566_4_0_1; -.
DR   InParanoid; Q6QI89; -.
DR   OMA; RGNMQRS; -.
DR   OrthoDB; 1624495at2759; -.
DR   PhylomeDB; Q6QI89; -.
DR   TreeFam; TF323400; -.
DR   PRO; PR:Q6QI89; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000002389; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q6QI89; RN.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISO:RGD.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0000786; C:nucleosome; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0043968; P:histone H2A acetylation; ISO:RGD.
DR   GO; GO:0043967; P:histone H4 acetylation; ISO:RGD.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:RGD.
DR   GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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   PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 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_0000088770"
FT   DOMAIN          117..288
FT                   /note="MRG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT   REGION          1..115
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        97..115
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;  32214 MW;  25C3B5D3C9E6FE42 CRC64;
     MSSRKQASQT RGQQSAEEDN FKKPTRSNMQ RSKMRGAASG KKSAGSQPKN LDPALPGRWG
     GRSAENPPSG SVRKTRKNKQ KTPGNGDGGS TSEVPQPPRK KRARADPTVE SEEAFKSRME
     VKVKIPEELK PWLVEDWDLV TRQKQLFQLP AKKNVDAILE EYANCKKSQG NVDNKEYAVN
     EVVGGIKEYF NVMLGTQLLY KFERPQYAEI LLAHPDAPMS QIYGAPHLLR LFVRIGAMLA
     YTPLDEKSLA LLLGYLHDFL KYLAKNSASL FTASDYKVAS ADYHRKAL
 
 
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