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Protein

Aspartate aminotransferase, cytoplasmic

Gene

Got1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H2S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain.6 Publications

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by L-aspartate.1 Publication

Kineticsi

  1. KM=22.2 mM for L-cysteine1 Publication
  2. KM=0.06 mM for 2-oxoglutarate1 Publication

    pH dependencei

    Optimum pH is 9.7.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391Aspartate; via amide nitrogenBy similarity
    Binding sitei141 – 1411AspartateBy similarity
    Binding sitei195 – 1951AspartateBy similarity
    Binding sitei387 – 3871AspartateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12468.
    ReactomeiR-RNO-70263. Gluconeogenesis.
    R-RNO-70614. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP13221.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartate aminotransferase, cytoplasmic (EC:2.6.1.1, EC:2.6.1.3)
    Short name:
    cAspAT
    Alternative name(s):
    Cysteine aminotransferase, cytoplasmic
    Cysteine transaminase, cytoplasmic
    Short name:
    cCAT
    Glutamate oxaloacetate transaminase 1
    Transaminase A
    Gene namesi
    Name:Got1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 1

    Organism-specific databases

    RGDi2721. Got1.

    Subcellular locationi

    GO - Cellular componenti

    • axon terminus Source: RGD
    • cytoplasm Source: RGD
    • cytosol Source: RGD
    • extracellular exosome Source: Ensembl
    • lysosome Source: RGD
    • nucleus Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedBy similarity
    Chaini2 – 413412Aspartate aminotransferase, cytoplasmicPRO_0000123883Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461PhosphoserineCombined sources
    Modified residuei149 – 1491PhosphoserineCombined sources
    Modified residuei259 – 2591N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP13221.
    PRIDEiP13221.

    2D gel databases

    World-2DPAGE0004:P13221.

    PTM databases

    iPTMnetiP13221.
    PhosphoSiteiP13221.

    Expressioni

    Tissue specificityi

    Expressed in liver and kidney.1 Publication

    Inductioni

    In liver and kidney, by glucocorticod hormones. Levels in the liver also increase 2-fold on animals fed on a high protein diet or during fasting. By hypoxia during cerebral ischemia.4 Publications

    Gene expression databases

    GenevisibleiP13221. RN.

    Interactioni

    Subunit structurei

    Homodimer.

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi246568. 1 interaction.
    STRINGi10116.ENSRNOP00000022309.

    Structurei

    3D structure databases

    ProteinModelPortaliP13221.
    SMRiP13221. Positions 2-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1411. Eukaryota.
    COG1448. LUCA.
    GeneTreeiENSGT00390000014081.
    HOGENOMiHOG000185898.
    HOVERGENiHBG000951.
    InParanoidiP13221.
    KOiK14454.
    OMAiYYSNPTW.
    OrthoDBiEOG74J980.
    PhylomeDBiP13221.
    TreeFamiTF314089.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PANTHERiPTHR11879. PTHR11879. 1 hit.
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    PRINTSiPR00799. TRANSAMINASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13221-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAPPSFFAQV PQAPPVLVFK LIADFRDDPD PRKVNLGVGA YRTDDSQPWV
    60 70 80 90 100
    LPVVRKVEQK IANDHSLNHE YLPILGLAEF RSCASQLVLG DNSPALRENR
    110 120 130 140 150
    VGGVQSLGGT GALRIGADFL GRWYNGTDNK NTPVYVSSPT WENHNGVFSA
    160 170 180 190 200
    AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIFVLH ACAHNPTGTD
    210 220 230 240 250
    PTEEEWKQIA AVMKRRFLFP FFDSAYQGFA SGDLEKDAWA IRYFVSEGFE
    260 270 280 290 300
    LFCAQSFSKN FGLYNERVGN LTVVGKEHDS VLRVLSQMEK IVRITWSNPP
    310 320 330 340 350
    AQGARIVATT LSNPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT
    360 370 380 390 400
    WSHITEQIGM FSFTGLNPKQ VEYLVNEKHI YLMPSGRINM CGLTTKNLDY
    410
    VATSINEAVT KFQ
    Length:413
    Mass (Da):46,429
    Last modified:January 23, 2007 - v3
    Checksum:iA9425BF05AC24C08
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551R → T in AAA40769 (PubMed:3182856).Curated
    Sequence conflicti100 – 1001R → G in AAA40769 (PubMed:3182856).Curated
    Sequence conflicti109 – 1091G → A in AAA40769 (PubMed:3182856).Curated
    Sequence conflicti121 – 1211G → A in AAA40769 (PubMed:3182856).Curated
    Sequence conflicti125 – 1251N → I in BAA00183 (PubMed:3053674).Curated
    Sequence conflicti254 – 2541A → P in AAA40769 (PubMed:3182856).Curated
    Sequence conflicti366 – 3661L → F in BAA00183 (PubMed:3053674).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04171 mRNA. Translation: AAA40769.1.
    D00252 mRNA. Translation: BAA00183.1.
    BC061877 mRNA. Translation: AAH61877.1.
    J05263 Genomic DNA. Translation: AAA40842.1.
    PIRiI55325.
    JT0439.
    RefSeqiNP_036703.2. NM_012571.2.
    UniGeneiRn.5819.

    Genome annotation databases

    EnsembliENSRNOT00000022309; ENSRNOP00000022309; ENSRNOG00000016356.
    GeneIDi24401.
    KEGGirno:24401.
    UCSCiRGD:2721. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04171 mRNA. Translation: AAA40769.1.
    D00252 mRNA. Translation: BAA00183.1.
    BC061877 mRNA. Translation: AAH61877.1.
    J05263 Genomic DNA. Translation: AAA40842.1.
    PIRiI55325.
    JT0439.
    RefSeqiNP_036703.2. NM_012571.2.
    UniGeneiRn.5819.

    3D structure databases

    ProteinModelPortaliP13221.
    SMRiP13221. Positions 2-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi246568. 1 interaction.
    STRINGi10116.ENSRNOP00000022309.

    PTM databases

    iPTMnetiP13221.
    PhosphoSiteiP13221.

    2D gel databases

    World-2DPAGE0004:P13221.

    Proteomic databases

    PaxDbiP13221.
    PRIDEiP13221.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000022309; ENSRNOP00000022309; ENSRNOG00000016356.
    GeneIDi24401.
    KEGGirno:24401.
    UCSCiRGD:2721. rat.

    Organism-specific databases

    CTDi2805.
    RGDi2721. Got1.

    Phylogenomic databases

    eggNOGiKOG1411. Eukaryota.
    COG1448. LUCA.
    GeneTreeiENSGT00390000014081.
    HOGENOMiHOG000185898.
    HOVERGENiHBG000951.
    InParanoidiP13221.
    KOiK14454.
    OMAiYYSNPTW.
    OrthoDBiEOG74J980.
    PhylomeDBiP13221.
    TreeFamiTF314089.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12468.
    ReactomeiR-RNO-70263. Gluconeogenesis.
    R-RNO-70614. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP13221.

    Miscellaneous databases

    PROiP13221.

    Gene expression databases

    GenevisibleiP13221. RN.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PANTHERiPTHR11879. PTHR11879. 1 hit.
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    PRINTSiPR00799. TRANSAMINASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isoenzymes of rat aspartate aminotransferase."
      Pave-Preux M., Ferry N., Bouguet J., Hanoune J., Barouki R.
      J. Biol. Chem. 263:17459-17466(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    2. "Rat cytosolic aspartate aminotransferase: molecular cloning of cDNA and expression in Escherichia coli."
      Horio Y., Tanaka T., Taketoshi M., Nagashima F., Tanase S., Morino Y., Wada H.
      J. Biochem. 103:797-804(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
    3. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Prostate.
    4. "Hormonal discrimination among transcription start sites of aspartate aminotransferase."
      Pave-Preux M., Aggerbeck M., Veyssier C., Bousquet-Lemercier B., Hanoune J., Barouki R.
      J. Biol. Chem. 265:4444-4448(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
    5. Lubec G., Afjehi-Sadat L., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 21-32; 34-42; 101-122; 217-236; 268-276 AND 388-396, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.
    6. "Purification and characterization of cysteine aminotransferase from rat liver cytosol."
      Akagi R.
      Acta Med. Okayama 36:187-197(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: CYSTEINE AMINOTRANSFERASE ACTIVITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, FUNCTION.
    7. "Rat cytosolic aspartate aminotransferase: regulation of its mRNA and contribution to gluconeogenesis."
      Horio Y., Tanaka T., Taketoshi M., Uno T., Wada H.
      J. Biochem. 103:805-808(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION.
    8. "Cytosolic aspartate aminotransferase, a new partner in adipocyte glyceroneogenesis and an atypical target of thiazolidinedione."
      Tordjman J., Leroyer S., Chauvet G., Quette J., Chauvet C., Tomkiewicz C., Chapron C., Barouki R., Forest C., Aggerbeck M., Antoine B.
      J. Biol. Chem. 282:23591-23602(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    9. "Oxygen-inducible glutamate oxaloacetate transaminase as protective switch transforming neurotoxic glutamate to metabolic fuel during acute ischemic stroke."
      Rink C., Gnyawali S., Peterson L., Khanna S.
      Antioxid. Redox Signal. 14:1777-1785(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    10. "Neuroprotection by glutamate oxaloacetate transaminase in ischemic stroke: an experimental study."
      Campos F., Sobrino T., Ramos-Cabrer P., Argibay B., Agulla J., Perez-Mato M., Rodriguez-Gonzalez R., Brea D., Castillo J.
      J. Cereb. Blood Flow Metab. 31:1378-1386(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
      Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
      Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAATC_RAT
    AccessioniPrimary (citable) accession number: P13221
    Secondary accession number(s): Q64570, Q6P721
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: July 6, 2016
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.