Detail Information for IndEnz0002018961
IED ID IndEnz0002018961
Enzyme Type ID protease018961
Protein Name Carboxypeptidase Y
EC 3.4.16.5
Carboxypeptidase YSCY
Gene Name PRC1 PAS_chr1-4_0013
Organism Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Phaffomycetaceae Komagataella Komagataella phaffii Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Enzyme Sequence MILHTYIILSLLTIFPKAIGLSLQMPMALEASYASLVEKATLAVGQEIDAIQKGIQQGWLEVETRFPTIVSQLSYSTGPKFAIKKKDATFWDFYVESQELPNYRLRVKRNNPEVLKVDFTKQYSGYLDVEADDKHFFYWFFESRNDPQNDPIILWLNGGPGCSSLTGLFFELGSSRINENLKPIFNPYSWNGNASIIYLDQPVNVGFSYSSSSVSNTVVAGEDVYAFLQLFFQHFPEYQTNDFHIAGESYAGHYIPVFADEILSQKNRNFNLTSVLIGNGLTDPLTQYRYYEPMACGEGGAPSVLPADECENMLVTQDKCLSLIQACYDSQSAFTCAPAAIYCNNAQMGPYQRTGKNVYDIRKECDGGSLCYKDLEFIDTYLNQKFVQDALGAEVDTYESCNFEINRNFLFAGDWMKPYHEHVSSLLNKGLPVLIYAGDKDFICNWLGNRAWTDVLPWVDADGFEKAEVQDWLVNGRKAGEFKNYSNFTYLRVYDAGHMAPYDQPENSHEMVNRWISGDFSFH
Enzyme Length 523
Uniprot Accession Number P52710
Absorption
Active Site ACT_SITE 249; /evidence=ECO:0000250; ACT_SITE 441; /evidence=ECO:0000250; ACT_SITE 498; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074, ECO:0000255|PROSITE-ProRule:PRU10075};
DNA Binding
EC Number 3.4.16.5
Enzyme Function FUNCTION: Involved in degradation of small peptides.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (5); Glycosylation (4); Propeptide (1); Signal peptide (1)
Keywords Carboxypeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Vacuole;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 59,448
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda