CNDP2
entrez
55748
canonical
uniprot
Q96KP4
canonical
ensembl
ENSG00000133313
resolver
ensp
ENSP00000325548
resolver
ensp
ENSP00000325756
resolver
ensp
ENSP00000462311
resolver
ensp
ENSP00000550704
resolver
ensp
ENSP00000550726
resolver
ensp
ENSP00000550741
resolver
ensp
ENSP00000550747
resolver
genesymbol
CNDP2
resolver
genesymbol_syn
CN2
resolver
genesymbol_syn
CPGL
resolver
genesymbol_syn
HEL-S-13
resolver
genesymbol_syn
PEPA
resolver
hgnc
HGNC:24437
resolver
uniprot
B3KUG4
resolver
uniprot
Q8WY59
resolver
uniprot
Q9BQ94
resolver
uniprot
Q9NVB4
resolver
uniprot
V9HWE5
resolver
uniprot_entry
CNDP2_HUMAN
resolver
uniprot_sec
B3KUG4
resolver
uniprot_sec
Q8WY59
resolver
uniprot_sec
Q9BQ94
resolver
uniprot_sec
Q9NVB4
resolver
uniprot_sec
V9HWE5
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by p-hydroxymercurybenzoate. The inhibitory concentration 50% (IC(50)) is 13 uM. Inhibited by bestatin. The inhibitory concentration 50% (IC(50)) is 7 nM at pH 9.5. {ECO:0000269|PubMed:12473676}.
uniprot
proteins
amino_acid_sequence
MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQLKD
uniprot
proteins
ec_number
3.4.-.-
uniprot
proteins
ec_number
3.4.13.18
uniprot
proteins
function
FUNCTION: Cytosolic metallodipeptidase with broad substrate specificity that catalyzes the hydrolysis of amide bonds in dipeptides and pseudopeptides (PubMed:12473676, PubMed:19346245, PubMed:25964343). Substrates include L-cysteinylglycine, an intermediate metabolite of the gamma-glutamyl cycle of glutathione metabolism (PubMed:19346245, PubMed:25964343). Can also hydrolyze threonyl-containing dipeptides (By similarity). Upon physiological conditions of amino acids and lactate excess can also catalyze a reverse proteolysis reaction, generating N-[(S)-lactoyl]-L-phenylalanine and possibly other N-lactoyl-amino acids which it can also hydrolyze in vitro. N-[(S)-lactoyl]-L-phenylalanine is an exercise-induced metabolite that influences food intake and systemic energy balance (PubMed:25964343). Carnosine is probably not a physiological substrate and L-homocarnosine is not a substrate for this enzyme (PubMed:12473676). Plays a role in the regulation of cell cycle arrest and apoptosis (PubMed:17121880, PubMed:24395568). {ECO:0000250|UniProtKB:Q9D1A2, ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:17121880, ECO:0000269|PubMed:19346245, ECO:0000269|PubMed:24395568, ECO:0000269|PubMed:25964343}.
uniprot
proteins
mass_dalton
52878
uniprot
proteins
protein_family
Peptidase M20A family
uniprot
proteins
pubmed
12473676
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
16177791
uniprot
proteins
pubmed
17121880
uniprot
proteins
pubmed
19346245
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24395568
uniprot
proteins
pubmed
25964343
uniprot
proteins
sequence_length
475
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12473676, ECO:0000269|PubMed:17121880}.
uniprot
proteins