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Reviewed, UniProtKB/Swiss-Prot P00507 (AATM_RAT)

Last modified November 3, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Aspartate aminotransferase, mitochondrial
    EC=2.6.1.1
Alternative name(s):
    mAspAT
    Transaminase A
    Glutamate oxaloacetate transaminase 2
    Fatty acid-binding protein
    FABP-1
    FABPpm
Gene names
Name: Got2
Synonyms: Maat
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Facilitates cellular uptake of long-chain free fatty acids By similarity.

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix. Cell membrane. 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. Ref.9

Tissue specificity

Expressed in all tissues tested: liver, pancreas, kidney, heart, spleen, arterioles, and lymphocytes. Ref.9

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

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Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCell membrane
Membrane
Mitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processaspartate metabolic process

Inferred from mutant phenotype. Source: RGD

biosynthetic process

Inferred from electronic annotation. Source: InterPro

dicarboxylic acid metabolic process

Inferred from direct assay. Source: RGD

fatty acid transport Ref.9

Traceable author statement. Source: RGD

   Cellular componentcell surface Ref.9

Inferred from direct assay. Source: RGD

mitochondrial inner membrane

Inferred from direct assay. Source: RGD

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

perikaryon

Inferred from direct assay. Source: RGD

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from direct assay. Source: RGD

   Molecular functionL-aspartate:2-oxoglutarate aminotransferase activity

Inferred from direct assay. Source: RGD

amino acid binding

Inferred from direct assay. Source: RGD

enzyme binding

Inferred from direct assay. Source: RGD

phospholipid binding

Inferred from direct assay. Source: RGD

protein homodimerization activity

Inferred from mutant phenotype. Source: RGD

pyridoxal phosphate binding

Inferred from direct assay. Source: RGD

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Ref.4 Ref.5 Ref.6
Chain30 – 430401Aspartate aminotransferase, mitochondrial
PRO_0000001218

Amino acid modifications

Modified residue731N6-acetyllysine By similarity
Modified residue901N6-acetyllysine By similarity
Modified residue941N6-acetyllysine By similarity
Modified residue961Phosphotyrosine By similarity
Modified residue1501N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue1851N6-acetyllysine By similarity
Modified residue2341N6-acetyllysine By similarity
Modified residue2791N6-(pyridoxal phosphate)lysine
Modified residue2961N6-acetyllysine By similarity
Modified residue3451N6-acetyllysine By similarity
Modified residue3631N6-acetyllysine By similarity
Modified residue3961N6-acetyllysine By similarity
Modified residue4011Phosphotyrosine By similarity
Modified residue4041N6-acetyllysine By similarity

Experimental info

Sequence conflict301S → R in AAC13868. Ref.3
Sequence conflict1621W → G Ref.4
Sequence conflict1621W → G Ref.5
Sequence conflict167 – 1693PIF → EIA Ref.4
Sequence conflict167 – 1693PIF → EIA Ref.5
Sequence conflict1771Q → E Ref.4
Sequence conflict1771Q → E Ref.5
Sequence conflict2321V → Y Ref.4
Sequence conflict2321V → Y Ref.5
Sequence conflict2551D → N Ref.4
Sequence conflict2551D → N Ref.5
Sequence conflict338 – 3392KQ → QG Ref.4
Sequence conflict338 – 3392KQ → QG Ref.5
Sequence conflict3521I → G Ref.4
Sequence conflict3521I → G Ref.5
Sequence conflict3861L → I Ref.4
Sequence conflict3861L → I Ref.5
Sequence conflict4001V → I Ref.4
Sequence conflict4001V → I Ref.5

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Sequences

Sequence LengthMass (Da)Tools
P00507-1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: EDC8B862A20DB736

FASTA43047,314
        10         20         30         40         50         60 
MALLHSGRVL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 

        70         80         90        100        110        120 
NLGVGAYRDD NGKPYVLPSV RKAEAQIAGK NLDKEYLPIG GLADFCKASA ELALGENSEV 

       130        140        150        160        170        180 
LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR 

       190        200        210        220        230        240 
YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEMA AVVKKKNLFA 

       250        260        270        280        290        300 
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE 

       310        320        330        340        350        360 
AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS 

       370        380        390        400        410        420 
NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY 

       430 
LAHAIHQVTK

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References

« Hide 'large scale' references
[1]"Molecular cloning and in vivo expression of a precursor to rat mitochondrial aspartate aminotransferase."
Mattingly J.R. Jr., Rodriguez-Berrocal F.J., Gordon J., Iriarte A., Martinez-Carrion M.
Biochem. Biophys. Res. Commun. 149:859-865(1987) [PubMed: 3322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]"Androgen modulation of multiple transcription start sites of the mitochondrial aspartate aminotransferase gene in rat prostate."
Juang H.H., Costello L.C., Franklin R.B.
J. Biol. Chem. 270:12629-12634(1995) [PubMed: 7759512] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
Strain: Wistar.
Tissue: Liver.
[4]"Primary structure of mitochondrial glutamic oxaloacetic transaminase from rat liver: comparison with that of the pig heart isozyme."
Huynh Q.K., Sakakibara R., Watanabe T., Wada H.
Biochem. Biophys. Res. Commun. 97:474-479(1980) [PubMed: 7470110] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-430.
Tissue: Liver.
[5]"The complete amino acid sequence of mitochondrial glutamic oxaloacetic transaminase from rat liver."
Huynh Q.K., Sakakibara R., Watanabe T., Wada H.
J. Biochem. 90:863-875(1981) [PubMed: 7309704] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-430.
Tissue: Liver.
[6]"Comparison of plasma membrane FABP and mitochondrial isoform of aspartate aminotransferase from rat liver."
Stump D.D., Zhou S.-L., Berk P.D.
Am. J. Physiol. 265:G894-G902(1993) [PubMed: 8238519] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-64.
Strain: Sprague-Dawley.
Tissue: Liver.
[7]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 60-68; 91-122; 126-147; 171-180; 186-200; 280-296; 310-337; 356-363 AND 397-404, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[8]"Molecular cloning of rat mitochondrial glutamic oxaloacetic transaminase mRNA and regulation of its expression in regenerating liver."
Horio Y., Sakakibara R., Tanaka T., Taketoshi M., Obaru K., Shimada K., Morino Y., Wada H.
Biochem. Biophys. Res. Commun. 134:803-811(1986) [PubMed: 3004464] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 279-329.
[9]"Immunogold localization of mitochondrial aspartate aminotransferase in mitochondria and on the cell surface in normal rat tissues."
Cechetto J.D., Sadacharan S.K., Berk P.D., Gupta R.S.
Histol. Histopathol. 17:353-364(2002) [PubMed: 11962739] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M18467 mRNA. Translation: AAB54275.1.
BC061792 mRNA. Translation: AAH61792.1.
U21158 Genomic DNA. Translation: AAC13868.1.
M12709 mRNA. Translation: AAA41267.1.
IPIIPI00210920.
PIRXNRTDM. A28005.
I55427.
RefSeqNP_037309.1.
UniGeneRn.98650

3D structure databases

HSSPHSSP built from PDB template 7AAT based on UniProtKB P00508.
SMRP00507. Positions 30-430.
ModBaseSearch...

Protein-protein interaction databases

STRINGP00507.

PTM databases

PhosphoSiteP00507.

Proteomic databases

PRIDEP00507.

Genome annotation databases

EnsemblENSRNOT00000015956; ENSRNOP00000015956; ENSRNOG00000011782; Rattus norvegicus. [Genome view]
GeneID25721.
KEGGrno:25721.
NMPDRfig|10116.3.peg.14535.
UCSCNM_013177. rat.

Organism-specific databases

CTD25721.
RGD2722. Got2.

Phylogenomic databases

HOVERGENP00507.
OMAIASSYSK.

Enzyme and pathway databases

BRENDA2.6.1.1. 248.

Gene expression databases

ArrayExpressP00507.
GenevestigatorP00507.
GermOnlineENSRNOG00000011782. Rattus norvegicus.

Family and domain databases

InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11879. Asp_trans. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio607817.

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Entry information

Entry nameAATM_RAT
AccessionPrimary (citable) accession number: P00507
Secondary accession number(s): Q64551, Q9QV50
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 3, 2009
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents