ID   MBR1_YEAST              Reviewed;         339 AA.
AC   P23493; D6VXJ5; Q2VQW7;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Mitochondrial biogenesis regulation protein 1;
GN   Name=MBR1; OrderedLocusNames=YKL093W; ORFNames=YKL440;
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=R100;
RX   PubMed=8208248; DOI=10.1007/bf00284206;
RA   Daignan-Fornier B., Nguyen C.C., Reisdorf P., Lemeignan B.,
RA   Bolotin-Fukuhara M.;
RT   "MBR1 and MBR3, two related yeast genes that can suppress the growth defect
RT   of hap2, hap3 and hap4 mutants.";
RL   Mol. Gen. Genet. 243:575-583(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8256524; DOI=10.1002/yea.320091016;
RA   Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA   Bolotin-Fukuhara M.;
RT   "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT   physically localizes the MRB1 gene and reveals eight new open reading
RT   frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL   Yeast 9:1149-1155(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-98.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=15905473; DOI=10.1093/nar/gki583;
RA   Zhang Z., Dietrich F.S.;
RT   "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT   SAGE.";
RL   Nucleic Acids Res. 33:2838-2851(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 169-339.
RX   PubMed=8203166; DOI=10.1002/yea.320100212;
RA   James C.M., Gent M.E., Oliver S.G.;
RT   "Sequence analysis of a 3.5 Kb EcoRI fragment from the left arm of
RT   Saccharomyces cerevisiae chromosome XI reveals the location of the MBR1
RT   gene and a sequence related to a GTPase-activating protein.";
RL   Yeast 10:257-264(1994).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=1725263; DOI=10.1016/0300-9084(91)90187-6;
RA   Valens M., Rinaldi T., Daignan-Fornier B., Bolotin-Fukuhara M.;
RT   "Identification of nuclear genes which participate in mitochondrial
RT   translation in Saccharomyces cerevisiae.";
RL   Biochimie 73:1525-1532(1991).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=9267436; DOI=10.1007/s004380050512;
RA   Reisdorf P., Boy-Marcotte E., Bolotin-Fukuhara M.;
RT   "The MBR1 gene from Saccharomyces cerevisiae is activated by and required
RT   for growth under sub-optimal conditions.";
RL   Mol. Gen. Genet. 255:400-409(1997).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159; SER-177; SER-224 AND
RP   SER-227, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Participates in mitochondrial biogenesis and stress response.
CC       {ECO:0000269|PubMed:8208248, ECO:0000269|PubMed:9267436}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- INDUCTION: Expression is induced in the late growth phase and is
CC       negatively controlled by the cAMP-dependent protein kinase A (PKA).
CC       {ECO:0000269|PubMed:9267436}.
CC   -!- SIMILARITY: Belongs to the ISF1/MBR1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M63309; AAA88725.1; -; Genomic_DNA.
DR   EMBL; X71133; CAA50464.1; -; Genomic_DNA.
DR   EMBL; Z28093; CAA81931.1; -; Genomic_DNA.
DR   EMBL; X75561; CAA53240.1; -; Genomic_DNA.
DR   EMBL; AY899251; AAX83936.1; -; mRNA.
DR   EMBL; BK006944; DAA09065.1; -; Genomic_DNA.
DR   PIR; S37920; S37920.
DR   RefSeq; NP_012830.1; NM_001179659.1.
DR   AlphaFoldDB; P23493; -.
DR   BioGRID; 34040; 127.
DR   DIP; DIP-4119N; -.
DR   MINT; P23493; -.
DR   STRING; 4932.YKL093W; -.
DR   GlyGen; P23493; 9 sites, 1 O-linked glycan (9 sites).
DR   iPTMnet; P23493; -.
DR   PaxDb; 4932-YKL093W; -.
DR   PeptideAtlas; P23493; -.
DR   EnsemblFungi; YKL093W_mRNA; YKL093W; YKL093W.
DR   GeneID; 853769; -.
DR   KEGG; sce:YKL093W; -.
DR   AGR; SGD:S000001576; -.
DR   SGD; S000001576; MBR1.
DR   VEuPathDB; FungiDB:YKL093W; -.
DR   HOGENOM; CLU_778649_0_0_1; -.
DR   InParanoid; P23493; -.
DR   OMA; NXRSSSS; -.
DR   OrthoDB; 2032933at2759; -.
DR   BioCyc; YEAST:G3O-31884-MONOMER; -.
DR   BioGRID-ORCS; 853769; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P23493; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P23493; Protein.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR   InterPro; IPR031443; Mbr1.
DR   Pfam; PF17058; MBR1; 1.
PE   1: Evidence at protein level;
KW   Mitochondrion; Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..339
FT                   /note="Mitochondrial biogenesis regulation protein 1"
FT                   /id="PRO_0000096271"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        88
FT                   /note="A -> G (in Ref. 1; AAA88725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="G -> R (in Ref. 1; AAA88725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="S -> T (in Ref. 1; AAA88725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="G -> E (in Ref. 1; AAA88725)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   339 AA;  36935 MW;  A38E7EA7049754A0 CRC64;
     MRMEKTTDKP LSAGDMNDEY SRGPIDDIDC LNFFERAVQD PCCEACDTED ADEELRAKLS
     SFNFQPDSSP CNAKCQQTLN PLCKIDEALP AESELAPSRN GSVSEANSDT NSIASTVHDP
     VDSKYGGMPS LRKAKTTSYF TSSSSNNTTM RNPLKKCNTN INGLLVNGRS SSSSRQSIPE
     LFSGACTKKK NNVLLKSETP NSEFSSNSLQ HCNSRSFSLP RSRSRSSAIA IPTHLYGLEK
     YVSPGLDTLT ADPEESIERF SNNRPREISS CCPNDTGDTS SSLSHSNTSS SLNFPLGTNT
     NQFHQPRQPV QQQQSSKPNF GAGRKKSFIE MSLASSFAG
//