| IED ID | IndEnz0002008668 |
| Enzyme Type ID | protease008668 |
| Protein Name |
pH-response transcription factor pacC/RIM101 Regulator of IME2 protein 1 pH-response regulator protein RIM101 |
| Gene Name | RIM101 RIM1 YHL027W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MVPLEDLLNKENGTAAPQHSRESIVENGTDVSNVTKKDGLPSPNLSKRSSDCSKRPRIRCTTEAIGLNGQEDERMSPGSTSSSCLPYHSTSHLNTPPYDLLGASAVSPTTSSSSDSSSSSPLAQAHNPAGDDDDADNDGDSEDITLYCKWDNCGMIFNQPELLYNHLCHDHVGRKSHKNLQLNCHWGDCTTKTEKRDHITSHLRVHVPLKPFGCSTCSKKFKRPQDLKKHLKIHLESGGILKRKRGPKWGSKRTSKKNKSCASDAVSSCSASVPSAIAGSFKSHSTSPQILPPLPVGISQHLPSQQQQRAISLNQLCSDELSQYKPVYSPQLSARLQTILPPLYYNNGSTVSQGANSRSMNVYEDGCSNKTIANATQFFTKLSRNMTNNYILQQSGGSTESSSSSGRIPVAQTSYVQPPNAPSYQSVQGGSSISATANTATYVPVRLAKYPTGPSLTEHLPPLHSNTAGGVFNRQSQYAMPHYPSVRAAPSYSSSGCSILPPLQSKIPMLPSRRTMAGGTSLKPNWEFSLNQKSCTNDIIMSKLAIEEVDDESEIEDDFVEMLGIVNIIKDYLLCCVMEDLDDEESEDKDEENAFLQESLEKLSLQNQMGTNSVRILTKYPKILV |
| Enzyme Length | 625 |
| Uniprot Accession Number | P33400 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including RIM101 itself), mainly by repressing transcriptional repressors of those genes, and represses transcription of acid-expressed genes. Required for meiosis, sporulation and invasive growth. {ECO:0000269|PubMed:11050096, ECO:0000269|PubMed:12509465}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (3); Motif (3); Mutagenesis (4); Region (1); Sequence conflict (10); Zinc finger (3) |
| Keywords | Activator;Cytoplasm;DNA-binding;Meiosis;Metal-binding;Nucleus;Reference proteome;Repeat;Repressor;Transcription;Transcription regulation;Zinc;Zinc-finger |
| Interact With | P43603; Q12033; P32793 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by C-terminal proteolytic cleavage. At neutral to alkaline ambient pH, the signaling protease (probably RIM13) cleaves RIM101, removing a C-terminal 8 kDa peptide to yield the active form. {ECO:0000269|PubMed:9017390}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10688190; 11152942; 11283351; 11606256; 11743162; 12208998; 14690591; 14737190; 15371534; 15487944; 15879523; 15932646; 16024810; 16227598; 16380504; 16407402; 16524906; 17023428; 18202364; 18287536; 18394190; 18457952; 18595705; 18769540; 18806212; 19220866; 19243079; 19536198; 19596888; 19633265; 19841731; 20038633; 20197501; 20333241; 20379744; 20382759; 20402793; 20625544; 20726779; 20739709; 20842291; 20955006; 21421024; 21521246; 21763361; 21908597; 21962291; 22084379; 22113266; 22189060; 22219507; 22345606; 22360598; 22460637; 22465496; 22609971; 22865500; 22984072; 23454581; 23661198; 23689276; 23836928; 23893744; 23974285; 24223957; 25002535; 25009170; 25009286; 25239548; 25384977; 25460796; 25483081; 25660547; 25851600; 25859664; 25934176; 26067383; 26150415; 26692264; 26721270; 26751950; 27400980; 27557053; 27803246; 27917388; 29230001; 29931186; 32741024; 32891431; 33184698; 8417990; 9199331; 9560430; 9791171; 9874208; 9928935; |
| Motif | MOTIF 228..234; /note=Nuclear localization signal; /evidence=ECO:0000250; MOTIF 450..453; /note=YPX[LI] motif 1; MOTIF 620..623; /note=YPX[LI] motif 2 |
| Gene Encoded By | |
| Mass | 68,232 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |