| IED ID | IndEnz0002001162 |
| Enzyme Type ID | protease001162 |
| Protein Name |
pH-response transcription factor pacC/RIM101 pH-response regulator protein 2 |
| Gene Name | RIM101 HRM101 PRR2 CAALFM_C114340CA CaO19.7247 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MNYNIHPVTYLNADSNTGASESTASHHGSKKSPSSDIDVDNATSPSSFTSSQSPHINAMGNSPHSSFTSQSAANSPITDAKQHLVKPTTTKPAAFAPSANQSNTTASQSYTQPAQQLPTQLHPSLNQAYNNQPSYYLHQPTYGYQQQQQQQQQHQEFNQPSQQYHDHHGYYSNNNILNQNQPAPQQNPVKPFKKTYKKIRDEDLKGPFKCLWSNCNIIFETPEILYDHLCDDHVGRKSSNNLSLTCLWENCGTTTVKRDHITSHLRVHVPLKPFHCDLCPKSFKRPQDLKKHSKTHAEDHPKKLKKAQRELMKQQQKEAKQQQKLANKRANSMNATTASDLQLNYYSGNPADGLNYDDTSRKRRYENNSQHNMYVVNSILNDFNFQQMAQAPQQPGVVGTAGSAEFTTKRMKAGTEYNIDVFNKLNHLDDHLHHHHPQQQHPQQQYGGNIYEAEKFFNSLSNSIDMQYQNMSTQYQQQHAGSTFAQQKPTQQASGQLYPSLPTIGNGSYTTSGSSHKEGLVNNHNGYLPSYPQINRSLPYSSGVAQQPPSALEFGGVSTYQKSAQSYEEDSSDSSEEDDYSTSSEDELDTLFDKLNIDDNKVEEVTIDGFNLKDVAKHREMIHAVLGYLRNQIEQQEKEKSKEQKEVDVNETKLYPTITAF |
| Enzyme Length | 661 |
| Uniprot Accession Number | Q9UW14 |
| 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) and represses transcription of acid-expressed genes. Specifically recognizes and binds the consensus sequence 5'-CCAAGAA-3'. Required for the control of alkaline pH-induced filamentation (dimorphic switch) and virulence. {ECO:0000269|PubMed:10601210, ECO:0000269|PubMed:12912891}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Coiled coil (1); Compositional bias (4); Erroneous initiation (1); Motif (4); Mutagenesis (3); Region (6); Sequence conflict (1); Zinc finger (3) |
| Keywords | Coiled coil;Cytoplasm;Metal-binding;Nucleus;Reference proteome;Repeat;Repressor;Zinc;Zinc-finger |
| Interact With | |
| Induction | INDUCTION: By alkaline conditions. {ECO:0000269|PubMed:10601210}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. |
| 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 to yield the 74 kDa functional form. Also exists as a 65 kDa form at acidic pH, which may govern pH-independent processes. {ECO:0000269|PubMed:15189995}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11698381; |
| Motif | MOTIF 290..296; /note=Nuclear localization signal; MOTIF 498..501; /note=YPX[LI] motif 1; MOTIF 531..534; /note=YPX[LI] motif 2; MOTIF 655..658; /note=YPX[LI] motif 3 |
| Gene Encoded By | |
| Mass | 74,695 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |