MAF1_RAT
ID MAF1_RAT Reviewed; 260 AA.
AC Q5XIH0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Repressor of RNA polymerase III transcription MAF1 homolog;
GN Name=Maf1;
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=Heart;
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: Plays a role in the repression of RNA polymerase III-mediated
CC transcription in response to changing nutritional, environmental and
CC cellular stress conditions to balance the production of highly abundant
CC tRNAs, 5S rRNA, and other small non-coding RNAs with cell growth and
CC maintenance (By similarity). Also plays a key role in cell fate
CC determination by promoting mesorderm induction and adipocyte
CC differentiation (By similarity). Mechanistically, associates with the
CC RNA polymerase III clamp and thereby impairs its recruitment to the
CC complex made of the promoter DNA, TBP and the initiation factor TFIIIB.
CC When nutrients are available and mTOR kinase is active, MAF1 is
CC hyperphosphorylated and RNA polymerase III is engaged in transcription.
CC Stress-induced MAF1 dephosphorylation results in nuclear localization,
CC increased targeting of gene-bound RNA polymerase III and a decrease in
CC the transcriptional readout. Additionally, may also regulate RNA
CC polymerase I and RNA polymerase II-dependent transcription through its
CC ability to regulate expression of the central initiation factor TBP (By
CC similarity). {ECO:0000250|UniProtKB:Q9D0U6,
CC ECO:0000250|UniProtKB:Q9H063}.
CC -!- SUBUNIT: Interacts with TFIIIB subunits BRF1 and BRF2. Interacts with
CC Pol III subunit POLR3F. Interacts with TFIIIC subunit GTF3C1.
CC {ECO:0000250|UniProtKB:Q9H063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H063}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H063}.
CC -!- PTM: Phosphorylated at Ser-60, Ser-68 and Ser-75; the major sites of
CC phosphorylation. Nuclear accumulation correlates with a concomitant
CC dephosphorylation. Phosphorylation may attenuate its RNA polymerase
CC III-repressive function (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2, mainly on Lys-35. Desumoylated by
CC SENP1. SUMOylation promotes the ability of MAF1 to repress
CC transcription and suppress colony formation (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAF1 family. {ECO:0000305}.
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DR EMBL; BC083712; AAH83712.1; -; mRNA.
DR RefSeq; NP_001014107.1; NM_001014085.1.
DR AlphaFoldDB; Q5XIH0; -.
DR SMR; Q5XIH0; -.
DR STRING; 10116.ENSRNOP00000018240; -.
DR iPTMnet; Q5XIH0; -.
DR PhosphoSitePlus; Q5XIH0; -.
DR PaxDb; Q5XIH0; -.
DR GeneID; 315093; -.
DR KEGG; rno:315093; -.
DR UCSC; RGD:1359315; rat.
DR CTD; 84232; -.
DR RGD; 1359315; Maf1.
DR VEuPathDB; HostDB:ENSRNOG00000013514; -.
DR eggNOG; KOG3104; Eukaryota.
DR HOGENOM; CLU_037043_3_1_1; -.
DR InParanoid; Q5XIH0; -.
DR OMA; DKVCRKT; -.
DR OrthoDB; 939345at2759; -.
DR PhylomeDB; Q5XIH0; -.
DR TreeFam; TF315149; -.
DR Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
DR PRO; PR:Q5XIH0; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000013514; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q5XIH0; RN.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0050811; F:GABA receptor binding; IPI:RGD.
DR GO; GO:0000994; F:RNA polymerase III core binding; IBA:GO_Central.
DR GO; GO:0001002; F:RNA polymerase III type 1 promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001003; F:RNA polymerase III type 2 promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; ISO:RGD.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR Gene3D; 3.40.1000.50; -; 1.
DR InterPro; IPR015257; Maf1.
DR InterPro; IPR038564; Maf1_sf.
DR PANTHER; PTHR22504; PTHR22504; 1.
DR Pfam; PF09174; Maf1; 1.
DR PIRSF; PIRSF037240; RNA_polIII_Trep_MAF1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..260
FT /note="Repressor of RNA polymerase III transcription MAF1
FT homolog"
FT /id="PRO_0000337195"
FT REGION 58..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT MOD_RES 68
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT MOD_RES 75
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H063"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1 and SUMO2)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 260 AA; 28922 MW; 83D7369A5294D051 CRC64;
MKLLENSSFE AINSQLTVET GDAHIIGRIE SYSCKMAGDD KHMFKQFCQE GQPHVLEALS
PPQTSGLSPS RLSKSQGGED ESPLSDKCSR KTLFYLIATL NESFRPDYDF STARSHEFSR
EPSLRWVVNA VNCSLFSAVR EDFKALKPQL WNAVDEEICL AECDIYSYNP DLDSDPFGED
GSLWSFNYFF YNKRLKRIVF FSCRSISGST YTPSEAGNAL DLELGAEEVD EESGGGGGGG
EGRAEETSTM EEDRVPVICM
