UniProtKB - Q5R432 (CNDP2_PONAB)
Cytosolic non-specific dipeptidase
CNDP2
Functioni
Catalyzes the peptide bond hydrolysis in dipeptides, displaying a non-redundant activity toward threonyl dipeptides. Mediates threonyl dipeptide catabolism in a tissue-specific way (By similarity).
Has high dipeptidase activity toward cysteinylglycine, an intermediate metabolite in glutathione metabolism. Metabolizes N-lactoyl-amino acids, both through hydrolysis to form lactic acid and amino acids, as well as through their formation by reverse proteolysis. Plays a role in the regulation of cell cycle arrest and apoptosis (By similarity).
By similarityCatalytic activityi
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.By similarity EC:3.4.13.18
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 99 | Manganese 2; via tele nitrogenBy similarity | 1 | |
Active sitei | 101 | By similarity | 1 | |
Metal bindingi | 132 | Manganese 1By similarity | 1 | |
Metal bindingi | 132 | Manganese 2By similarity | 1 | |
Active sitei | 166 | Proton acceptorBy similarity | 1 | |
Metal bindingi | 167 | Manganese 1By similarity | 1 | |
Metal bindingi | 195 | Manganese 2By similarity | 1 | |
Binding sitei | 195 | Substrate; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 228 | Substrate; shared with homodimeric partnerBy similarity | 1 | |
Sitei | 228 | Important for catalytic activityBy similarity | 1 | |
Binding sitei | 330 | Substrate; shared with homodimeric partnerBy similarity | 1 | |
Binding sitei | 343 | SubstrateBy similarity | 1 | |
Binding sitei | 417 | Substrate; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 445 | Manganese 1; via tele nitrogenBy similarity | 1 | |
Binding sitei | 445 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- alanylglutamate dipeptidase activity Source: UniProtKB-EC
- carboxypeptidase activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- metallodipeptidase activity Source: InterPro
Keywordsi
Molecular function | Carboxypeptidase, Hydrolase, Metalloprotease, Protease |
Ligand | Manganese, Metal-binding |
Protein family/group databases
MEROPSi | M20.005 |
Names & Taxonomyi
Protein namesi | Recommended name: Cytosolic non-specific dipeptidase (EC:3.4.13.18By similarity)Alternative name(s): CNDP dipeptidase 2 Threonyl dipeptidaseBy similarity |
Gene namesi | Name:CNDP2 |
Organismi | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
Taxonomic identifieri | 9601 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000288495 | 2 – 475 | Cytosolic non-specific dipeptidaseAdd BLAST | 474 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 9 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 58 | PhosphoserineBy similarity | 1 | |
Modified residuei | 299 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinInteractioni
Subunit structurei
Homodimer.
By similarityProtein-protein interaction databases
STRINGi | 9601.ENSPPYP00000010372 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 166 – 167 | Substrate bindingBy similarity | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2276, Eukaryota |
InParanoidi | Q5R432 |
OrthoDBi | 733473at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR001261, ArgE/DapE_CS IPR017153, CNDP/DUG1 IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
PIRSFi | PIRSF037242, CNDP_dipeptidase, 1 hit |
PROSITEi | View protein in PROSITE PS00759, ARGE_DAPE_CPG2_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAALTTLFKY IDENQDRYIK KLAKWVAIQS VSAWPEKRGE IRRMMEVAAA
60 70 80 90 100
DVKQLGGSVE LVDIGKQKLP DGSEIPLPPI LLGRLGSDPQ KKTVCIYGHL
110 120 130 140 150
DVQPAALEDG WDSEPFTLVE RDGKLHGRGS TDDKGPVAGW INALEAYQKT
160 170 180 190 200
DQEIPVNVRF CLEGMEESGS EGLDELIFAQ KDTFFKDVDY VCISDNYWLG
210 220 230 240 250
KKKPCITYGL RGICYFFIEV ECSNKDLHSG VYGGSVHEAM TDLILLMGSL
260 270 280 290 300
VDKRGNILIP GINEAVAAVT EEEHKLYDDI DFDIEEFAKD VGAQILLHSN
310 320 330 340 350
KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPNMTP
360 370 380 390 400
EVVSEQVTSY LTKKFAELRS PNEFKVYMGH GGKPWVSDFS HPHYVAGRRA
410 420 430 440 450
MRTVFGVEPD LTREGGSIPV TLTFQEATGK NVMLLPVGSA DDGAHSQNEK
460 470
LNRHNYIEGT KMLAAYLYEV SQLKD
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 126 | H → Y in CAH92986 (Ref. 1) Curated | 1 | |
Sequence conflicti | 190 | Y → N in CAH92986 (Ref. 1) Curated | 1 | |
Sequence conflicti | 437 | V → A in CAH92986 (Ref. 1) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CR860879 mRNA Translation: CAH92986.1 CR861428 mRNA Translation: CAH93484.1 |
RefSeqi | NP_001127615.1, NM_001134143.1 |
Genome annotation databases
GeneIDi | 100174694 |
KEGGi | pon:100174694 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CR860879 mRNA Translation: CAH92986.1 CR861428 mRNA Translation: CAH93484.1 |
RefSeqi | NP_001127615.1, NM_001134143.1 |
3D structure databases
AlphaFoldDBi | Q5R432 |
SMRi | Q5R432 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9601.ENSPPYP00000010372 |
Protein family/group databases
MEROPSi | M20.005 |
Genome annotation databases
GeneIDi | 100174694 |
KEGGi | pon:100174694 |
Organism-specific databases
CTDi | 55748 |
Phylogenomic databases
eggNOGi | KOG2276, Eukaryota |
InParanoidi | Q5R432 |
OrthoDBi | 733473at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR001261, ArgE/DapE_CS IPR017153, CNDP/DUG1 IPR002933, Peptidase_M20 IPR011650, Peptidase_M20_dimer |
Pfami | View protein in Pfam PF07687, M20_dimer, 1 hit PF01546, Peptidase_M20, 1 hit |
PIRSFi | PIRSF037242, CNDP_dipeptidase, 1 hit |
PROSITEi | View protein in PROSITE PS00759, ARGE_DAPE_CPG2_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CNDP2_PONAB | |
Accessioni | Q5R432Primary (citable) accession number: Q5R432 Secondary accession number(s): Q5R5I0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 29, 2007 |
Last sequence update: | December 21, 2004 | |
Last modified: | May 25, 2022 | |
This is version 77 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families