MAF1_BOVIN
ID MAF1_BOVIN Reviewed; 260 AA.
AC A5D9C6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Repressor of RNA polymerase III transcription MAF1 homolog;
GN Name=MAF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; BT030545; ABQ12985.1; -; mRNA.
DR RefSeq; XP_005215224.1; XM_005215167.3.
DR RefSeq; XP_005215225.1; XM_005215168.3.
DR RefSeq; XP_015329821.1; XM_015474335.1.
DR AlphaFoldDB; A5D9C6; -.
DR SMR; A5D9C6; -.
DR STRING; 9913.ENSBTAP00000016239; -.
DR PaxDb; A5D9C6; -.
DR PRIDE; A5D9C6; -.
DR Ensembl; ENSBTAT00000016239; ENSBTAP00000016239; ENSBTAG00000012242.
DR GeneID; 512498; -.
DR CTD; 84232; -.
DR VEuPathDB; HostDB:ENSBTAG00000012242; -.
DR VGNC; VGNC:31137; MAF1.
DR eggNOG; KOG3104; Eukaryota.
DR GeneTree; ENSGT00390000006896; -.
DR InParanoid; A5D9C6; -.
DR OMA; DKVCRKT; -.
DR OrthoDB; 939345at2759; -.
DR TreeFam; TF315149; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000012242; Expressed in biceps femoris and 107 other tissues.
DR ExpressionAtlas; A5D9C6; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000994; F:RNA polymerase III core binding; IBA:GO_Central.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR Gene3D; 3.40.1000.50; -; 2.
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_0000337194"
FT REGION 58..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..239
FT /note="Acidic 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; 29054 MW; 835FC737F0AC4E8E CRC64;
MKLLENSSFE AINSQLTVET GDAHIIGRIE SYSCKMAGDD KHMFKQFCQE GQPHVLEALS
PPQTSGLSPS RLSKSQGGED EGPLSDKCSR KTLFYLIATL NESFRPDYDF STARSHEFSR
EPSLSWVVNA VNCSLFSAVR EDFKALKPQL WNAVDEEICL AECDIYSYNP DLDSDPFGED
GSLWSFNYFF YNKRLKRIVF FSCRSISGST YTPSEAGNEL DMELGEEDEE EEEESGGGGS
EGGPEEPGTM EEDRVPVICM
