DIF1_YEAST
ID DIF1_YEAST Reviewed; 133 AA.
AC O13577; D6VZ71;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Damage-regulated import facilitator 1;
GN Name=DIF1; OrderedLocusNames=YLR437C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INDUCTION.
RX PubMed=16278933; DOI=10.1002/yea.1302;
RA de Lichtenberg U., Wernersson R., Jensen T.S., Nielsen H.B., Fausboell A.,
RA Schmidt P., Hansen F.B., Knudsen S., Brunak S.;
RT "New weakly expressed cell cycle-regulated genes in yeast.";
RL Yeast 22:1191-1201(2005).
RN [4]
RP FUNCTION, PHOSPHORYLATION BY DUN1, AND INTERACTION WITH RNR2 AND RNR4.
RX PubMed=18851834; DOI=10.1016/j.molcel.2008.08.018;
RA Lee Y.D., Wang J., Stubbe J., Elledge S.J.;
RT "Dif1 is a DNA-damage-regulated facilitator of nuclear import for
RT ribonucleotide reductase.";
RL Mol. Cell 32:70-80(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=18838542; DOI=10.1128/mcb.01388-08;
RA Wu X., Huang M.;
RT "Dif1 controls subcellular localization of ribonucleotide reductase by
RT mediating nuclear import of the R2 subunit.";
RL Mol. Cell. Biol. 28:7156-7167(2008).
CC -!- FUNCTION: Mediates the nuclear localization of RNR2 and RNR4, 2
CC subunits of the ribonucleotide reductase. {ECO:0000269|PubMed:18838542,
CC ECO:0000269|PubMed:18851834}.
CC -!- SUBUNIT: Interacts with RNR2 and RNR4. {ECO:0000269|PubMed:18851834}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18838542}. Nucleus
CC {ECO:0000269|PubMed:18838542}.
CC -!- INDUCTION: During S phase of cell cycle. {ECO:0000269|PubMed:16278933}.
CC -!- PTM: Phosphorylated by DUN1 in response to DNA damage which leads to
CC its degradation. {ECO:0000269|PubMed:18838542,
CC ECO:0000269|PubMed:18851834}.
CC -!- SIMILARITY: Belongs to the DIF1/spd1 family. {ECO:0000305}.
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DR EMBL; U21094; AAB67525.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09737.1; -; Genomic_DNA.
DR PIR; S69322; S69322.
DR RefSeq; NP_013541.3; NM_001182325.3.
DR AlphaFoldDB; O13577; -.
DR SMR; O13577; -.
DR BioGRID; 31695; 29.
DR DIP; DIP-4632N; -.
DR STRING; 4932.YLR437C; -.
DR iPTMnet; O13577; -.
DR MaxQB; O13577; -.
DR PaxDb; O13577; -.
DR PRIDE; O13577; -.
DR EnsemblFungi; YLR437C_mRNA; YLR437C; YLR437C.
DR GeneID; 851157; -.
DR KEGG; sce:YLR437C; -.
DR SGD; S000004429; DIF1.
DR VEuPathDB; FungiDB:YLR437C; -.
DR eggNOG; ENOG502SGAU; Eukaryota.
DR HOGENOM; CLU_1887371_0_0_1; -.
DR InParanoid; O13577; -.
DR OMA; INQRTMS; -.
DR BioCyc; YEAST:G3O-32494-MON; -.
DR PRO; PR:O13577; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; O13577; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990846; F:ribonucleoside-diphosphate reductase inhibitor activity; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1905117; P:regulation of ribonucleoside-diphosphate reductase activity; IBA:GO_Central.
DR InterPro; IPR013900; RNR_inhibitor.
DR PANTHER; PTHR28081; PTHR28081; 1.
DR Pfam; PF08591; RNR_inhib; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..133
FT /note="Damage-regulated import facilitator 1"
FT /id="PRO_0000247354"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 133 AA; 15165 MW; 14DC77C644D48979 CRC64;
MDAQLEWASS LVPKRQLQQQ QQQQEQQQQQ QQDFHKDQLM TVGMRIRQRV DQGYASRTPS
TSDASLQPGV IRDYSSVIVP QFTRSPLPTA NSLPPMLINQ RTMSTEASSL EKWDVAEPAA
EHETMVNGSK RRL
