Cloned (Comment) | Organism |
---|---|
gene Ntan1, chromosomal localization and expression analysis, recombinant expression of N-terminally GFP-tagged 65-kDa in NTAN1pmouse 3T3 cells | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction and analysis of mouse strains lacking the asparagine-specific N-terminal amidase (NtN-amidase), encoded by the Ntan1 gene, by deletion-disruption of the mouse Ntan1 gene | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-terminal L-asparaginyl-[protein] + H2O | Mus musculus | - |
N-terminal L-aspartyl-[protein] + NH3 | - |
? | |
N-terminal L-asparaginyl-[protein] + H2O | Mus musculus C129 | - |
N-terminal L-aspartyl-[protein] + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q64311 | - |
- |
Mus musculus C129 | Q64311 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Mus musculus | - |
embryo | in wild-type embryos, Ntan1 is strongly expressed in the branchial arches and in the tail and limb buds | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-terminal L-asparaginyl-[protein] + H2O | - |
Mus musculus | N-terminal L-aspartyl-[protein] + NH3 | - |
? | |
N-terminal L-asparaginyl-[protein] + H2O | Asp-DHFR protein bearing Asn at its N-terminus is used as substrate | Mus musculus | N-terminal L-aspartyl-[protein] + NH3 | - |
? | |
N-terminal L-asparaginyl-[protein] + H2O | - |
Mus musculus C129 | N-terminal L-aspartyl-[protein] + NH3 | - |
? | |
N-terminal L-asparaginyl-[protein] + H2O | Asp-DHFR protein bearing Asn at its N-terminus is used as substrate | Mus musculus C129 | N-terminal L-aspartyl-[protein] + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NTAN1 | - |
Mus musculus |
NTAN1p amidase | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | Ntan1-/- mice lack NtN-amidase and the asparagine-specific branch of the N-end rule pathway. The phenoytpe shows altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway. The Ntan1-/- mouse strains lacking the NtN-amidase activity but retaining glutamine-specific NtQ amidase, EC 3.5.1.122, show that the two enzymes are encoded by different genes. Among the normally short-lived N-end rule substrates, only those bearing N-terminal asparagine became long-lived in Ntan1-/- fibroblasts. The Ntan1-/- mice are fertile and outwardly normal but differ from their congenic wild-type counterparts in spontaneous activity, spatial memory, and a socially conditioned exploratory phenotype | Mus musculus |
metabolism | the enzyme is involved in the mammalian N-end rule pathway. The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. N-terminal asparagine and glutamine are tertiary destabilizing residues, in that they are enzymatically deamidated to yield secondary destabilizing residues aspartate and glutamate, which are conjugated to arginine, a primary destabilizing residue | Mus musculus |