General information | DisProt: | DP00586 | Name: | Protease A inhibitor 3 | Synonym(s): | IPA3_YEAST
Proteinase inhibitor I(A)3
Saccharopepsin inhibitor
Proteinase yscA-inhibitor
| First appeared in release: | Release 4.9 (01/06/2009) | UniProt: | P01094 | UniGene: | | SwissProt: | IPA3_YEAST | TrEMBL: | | NCBI (GI): | 124811 | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | Sequence length: | 68 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MNTDQQKVSE IFQSSKEKLQ GDAKVVSDAF KKMASQDKDG KTTDADESEK HNYQEQYNKL - 60 KGAGHKKE
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Functional narrative |
Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
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Map of ordered and disordered regions |


Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 68 | Length: | 68 | Region sequence: |
MNTDQQKVSEIFQSSKEKLQGDAKVVSDAFKKMASQDKDGKTTDADESEKHNYQEQYNKL KGAGHKKE | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | | Functional subclasses: | Regulation of proteolysis in vivo
| Detection methods: | References:
- Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS. "IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution." Biochemistry. 2004; 43(14): 4071-81. PubMed: 15065849
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References |
- Phylip LH, Lees WE, Brownsey BG, Bur D, Dunn BM, Winther JR, Gustchina A, Li M, Copeland T, Wlodawer A, Kay J. "The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae." J Biol Chem. 2001; 276(3): 2023-30. PubMed: 11042188
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