MO4L1_RAT
ID MO4L1_RAT Reviewed; 323 AA.
AC Q6AYU1;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Mortality factor 4-like protein 1;
DE AltName: Full=MORF-related gene 15 protein;
DE AltName: Full=Transcription factor-like protein MRG15;
GN Name=Morf4l1;
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=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 histones H4 and H2A. This modification
CC may both alter nucleosome - DNA interactions and promote interaction of
CC the 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.
CC Required for homologous recombination repair (HRR) and resistance to
CC mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and
CC RAD51, but not BRCA1, to DNA-damage foci (By similarity).
CC {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, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC.
CC MORF4L1 may also participate in the formation of NuA4 related complexes
CC which lack the KAT5/TIP60 catalytic subunit, but which include the
CC SWI/SNF related protein SRCAP. Component of the mSin3A histone
CC deacetylase complex, which includes SIN3A, HDAC2, ARID4B, MORF4L1,
CC RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with RB1 and MYST1. May also
CC interact with PHF12 and one or more as yet undefined members of the TLE
CC (transducin-like enhancer of split) family of transcriptional
CC repressors. Interacts with the N-terminus of MRFAP1. Found in a complex
CC composed of MORF4L1, MRFAP1 and RB1. Interacts with the entire BRCA
CC complex, which contains BRCA1, PALB2, BRCA2 and RAD51. Interacts with
CC PALB2 (By similarity). Forms a complex with MSL1 and NUPR1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}.
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DR EMBL; BC078910; AAH78910.1; -; mRNA.
DR RefSeq; NP_001011999.1; NM_001011999.1.
DR AlphaFoldDB; Q6AYU1; -.
DR BMRB; Q6AYU1; -.
DR SMR; Q6AYU1; -.
DR STRING; 10116.ENSRNOP00000019471; -.
DR PhosphoSitePlus; Q6AYU1; -.
DR jPOST; Q6AYU1; -.
DR PaxDb; Q6AYU1; -.
DR DNASU; 300891; -.
DR GeneID; 300891; -.
DR KEGG; rno:300891; -.
DR UCSC; RGD:1307938; rat.
DR CTD; 10933; -.
DR RGD; 1307938; Morf4l1.
DR VEuPathDB; HostDB:ENSRNOG00000058412; -.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_4_0_1; -.
DR InParanoid; Q6AYU1; -.
DR OMA; GLQTYFD; -.
DR OrthoDB; 1624495at2759; -.
DR PRO; PR:Q6AYU1; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000058412; Expressed in cerebellum and 19 other tissues.
DR Genevisible; Q6AYU1; RN.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000786; C:nucleosome; ISO:RGD.
DR GO; GO:0016580; C:Sin3 complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038011; MRG15.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; PTHR10880; 2.
DR PANTHER; PTHR10880:SF29; PTHR10880:SF29; 2.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromatin regulator; DNA damage; DNA recombination;
KW DNA repair; Growth regulation; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..323
FT /note="Mortality factor 4-like protein 1"
FT /id="PRO_0000088767"
FT DOMAIN 12..62
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 152..323
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 77..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..227
FT /note="Sufficient for interaction with SIN3A"
FT /evidence="ECO:0000250"
FT REGION 125..191
FT /note="Interaction with RB1-1"
FT /evidence="ECO:0000250"
FT REGION 149..303
FT /note="Sufficient for interaction with PHF12"
FT /evidence="ECO:0000250"
FT REGION 284..305
FT /note="Interaction with RB1-2"
FT /evidence="ECO:0000250"
FT COMPBIAS 117..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU8"
SQ SEQUENCE 323 AA; 37201 MW; 327DBECBA8CF513A CRC64;
MAPKQDPKPK FQEGERVLCF HGPLLYEAKC VKVAIKDKQV KYFIHYSGWN KNWDEWVPES
RVLKYVDANL QKQRELQKAN QEQYAEGKMR GAAPGKKTSG LQQKNVEVKT KKNKQKTPGN
GDGGSTSETP QPPRKKRARV DPTVENEETF MNRVEVKVKI PEELKPWLVD DWDLITRQKQ
LFYLPAKKNV DSILEDYANY KKSRGNTDNK EYAVNEVVAG IKEYFNVMLG TQLLYKFERP
QYAEILADHP DAPMSQVYGA PHLLRLFVRI GAMLAYTPLD EKSLALLLNY LHDFLKYLAK
NSATLFSASD YEVAPPEYHR KAV
