Search by BoMiProt ID - Bomi241

Primary Information

BoMiProt ID Bomi241
Protein Name Dipeptidyl peptidase 1
Organism Bos taurus
Uniprot IDQ3ZCJ8
Milk FractionWhey
Ref Sequence ID NP_001028789.1
Aminoacid Length 463
Molecular Weight 51949
FASTA Sequence Download
Gene Name CTSC
Gene ID 352958
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Protein Function cystein cathepsin; involved in a normal cellular protein degradation and turnover; aminodipeptidase
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
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
PTMs Glycosylated: four glycans
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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.