P00507 · AATM_RAT
- ProteinAspartate aminotransferase, mitochondrial
- GeneGot2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids430 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids (By similarity).
Miscellaneous
In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Catalytic activity
- 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 65 | substrate | ||||
Sequence: G | ||||||
Binding site | 162 | substrate | ||||
Sequence: W | ||||||
Binding site | 215 | substrate | ||||
Sequence: N | ||||||
Binding site | 407 | substrate | ||||
Sequence: R |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate aminotransferase, mitochondrial
- EC number
- Short namesmAspAT
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP00507
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Located in the mitochondria of liver, pancreas, spleen, heart, pituitary gland and submandibular gland cells. In kidney, located in the mitochondria, on the cell surface of regions with protrusions in distal tubules, on the apical cell surface of protrusions along the microvilli in cortical collecting ducts, in condensing vacuoles, on the cell surface at cell boundaries of adjoining kidney cells and on the cell surface of endothelial cells lining capillaries in the glomerulus. Also located at the cell surface of endothelial cells lining arterioles and on the cell surface of lymphocytes.
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-29 | Mitochondrion | ||||
Sequence: MALLHSGRVLSGMAAAFHPGLAAAASARA | ||||||
Chain | PRO_0000001218 | 30-430 | Aspartate aminotransferase, mitochondrial | |||
Sequence: SSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAGKNLDKEYLPIGGLADFCKASAELALGENSEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEMAAVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK | ||||||
Modified residue | 48 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 59 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 73 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 73 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 82 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 90 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 90 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 96 | 3'-nitrotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 96 | Phosphotyrosine; alternate | ||||
Sequence: Y | ||||||
Modified residue | 107 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 107 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 122 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 122 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 143 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 159 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 159 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 185 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 185 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 227 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 234 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 279 | N6-(pyridoxal phosphate)lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 279 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 296 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 296 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 302 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 309 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 309 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 313 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 338 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 338 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 345 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 363 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 363 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 364 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 387 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 396 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 396 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 404 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 404 | N6-succinyllysine; alternate | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues tested: liver, pancreas, kidney, heart, spleen, arterioles, and lymphocytes.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length430
- Mass (Da)47,314
- Last updated1989-07-01 v2
- ChecksumEDC8B862A20DB736
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2Q7Q0 | A0A8L2Q7Q0_RAT | Got2 | 426 | ||
A0A8I6GLH0 | A0A8I6GLH0_RAT | Got2 | 410 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 30 | in Ref. 3; AAC13868 | ||||
Sequence: S → R | ||||||
Sequence conflict | 162 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: W → G | ||||||
Sequence conflict | 167-169 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: PIF → EIA | ||||||
Sequence conflict | 177 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 232 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: V → Y | ||||||
Sequence conflict | 255 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: D → N | ||||||
Sequence conflict | 338-339 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: KQ → QG | ||||||
Sequence conflict | 352 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: I → G | ||||||
Sequence conflict | 386 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: L → I | ||||||
Sequence conflict | 400 | in Ref. 4; AA sequence and 5; AA sequence | ||||
Sequence: V → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M18467 EMBL· GenBank· DDBJ | AAB54275.1 EMBL· GenBank· DDBJ | mRNA | ||
BC061792 EMBL· GenBank· DDBJ | AAH61792.1 EMBL· GenBank· DDBJ | mRNA | ||
U21158 EMBL· GenBank· DDBJ | AAC13868.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M12709 EMBL· GenBank· DDBJ | AAA41267.1 EMBL· GenBank· DDBJ | mRNA |