Primary Information |
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| BoMiProt ID | Bomi241 |
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| Protein Name | Dipeptidyl peptidase 1 |
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| Organism | Bos taurus |
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| Uniprot Id | Q3ZCJ8 |
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| Milk Fraction | Whey |
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| Ref Sequence Id | NP_001028789.1 |
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| Aminoacid Length | 463 |
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| Molecular Weight | 51949 |
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| Fasta Sequence | https://www.uniprot.org/uniprot/Q3ZCJ8.fasta |
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| Gene Name | CTSC |
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| Gene Id | 352958 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Protein Function | cystein cathepsin; involved in a normal cellular
protein degradation and turnover; aminodipeptidase |
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| Biochemical Properties | Cysteine cathepsins are optimally active in a slightly acidic pH and
are mostly unstable at neutral pH; exhibit broad specificity, cleave
substrates preferentially after basic or hydrophobic residues; E-64 is a non-selective inhibitor
of all the cysteine cathepsins, with the exception of cathepsin C,
which is only weakly inhibited |
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| Significance in milk | DPP4 is a key enzyme in intermediary metabolism by regulating important glycemic pathways; expression of DPP4 decreases with the onset of lactation |
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| PTMs | Glycosylated: four glycans |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1. Schulz, K. et al. (2015) ‘Effects of Inhibiting Dipeptidyl Peptidase-4 (DPP4) in Cows with Subclinical Ketosis.’, PloS one. Edited by M. Bader, 10(8), p. e0136078. doi: 10.1371/journal.pone.0136078.
2. Turk, B., Turk, D. and Turk, V. (2000) ‘Lysosomal cysteine proteases: more than scavengers.’, Biochimica et biophysica acta, 1477(1–2), pp. 98–111. doi: 10.1016/s0167-4838(99)00263-0.
3. Turk, D. et al. (2001) ‘Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases’, The EMBO Journal, 20(23), pp. 6570–6582. doi: 10.1093/emboj/20.23.6570. |
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