AATC_RAT
ID AATC_RAT Reviewed; 413 AA.
AC P13221; Q64570; Q6P721;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic {ECO:0000305};
DE Short=cAspAT {ECO:0000303|PubMed:3053674};
DE EC=2.6.1.1 {ECO:0000269|PubMed:3053674};
DE EC=2.6.1.3 {ECO:0000269|PubMed:7113743};
DE AltName: Full=Cysteine aminotransferase, cytoplasmic;
DE AltName: Full=Cysteine transaminase, cytoplasmic;
DE Short=cCAT;
DE AltName: Full=Glutamate oxaloacetate transaminase 1;
DE AltName: Full=Transaminase A;
GN Name=Got1 {ECO:0000312|RGD:2721};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=3182856; DOI=10.1016/s0021-9258(19)77858-2;
RA Pave-Preux M., Ferry N., Bouguet J., Hanoune J., Barouki R.;
RT "Nucleotide sequence and glucocorticoid regulation of the mRNAs for the
RT isoenzymes of rat aspartate aminotransferase.";
RL J. Biol. Chem. 263:17459-17466(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3053674; DOI=10.1093/oxfordjournals.jbchem.a122349;
RA Horio Y., Tanaka T., Taketoshi M., Nagashima F., Tanase S., Morino Y.,
RA Wada H.;
RT "Rat cytosolic aspartate aminotransferase: molecular cloning of cDNA and
RT expression in Escherichia coli.";
RL J. Biochem. 103:797-804(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX PubMed=2307672; DOI=10.1016/s0021-9258(19)39584-5;
RA Pave-Preux M., Aggerbeck M., Veyssier C., Bousquet-Lemercier B.,
RA Hanoune J., Barouki R.;
RT "Hormonal discrimination among transcription start sites of aspartate
RT aminotransferase.";
RL J. Biol. Chem. 265:4444-4448(1990).
RN [5]
RP PROTEIN SEQUENCE OF 21-32; 34-42; 101-122; 217-236; 268-276 AND 388-396,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP CYSTEINE AMINOTRANSFERASE ACTIVITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=7113743; DOI=10.18926/amo/30697;
RA Akagi R.;
RT "Purification and characterization of cysteine aminotransferase from rat
RT liver cytosol.";
RL Acta Med. Okayama 36:187-197(1982).
RN [7]
RP INDUCTION, AND FUNCTION.
RX PubMed=3182750; DOI=10.1093/oxfordjournals.jbchem.a122350;
RA Horio Y., Tanaka T., Taketoshi M., Uno T., Wada H.;
RT "Rat cytosolic aspartate aminotransferase: regulation of its mRNA and
RT contribution to gluconeogenesis.";
RL J. Biochem. 103:805-808(1988).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=17545671; DOI=10.1074/jbc.m611111200;
RA Tordjman J., Leroyer S., Chauvet G., Quette J., Chauvet C., Tomkiewicz C.,
RA Chapron C., Barouki R., Forest C., Aggerbeck M., Antoine B.;
RT "Cytosolic aspartate aminotransferase, a new partner in adipocyte
RT glyceroneogenesis and an atypical target of thiazolidinedione.";
RL J. Biol. Chem. 282:23591-23602(2007).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=21361730; DOI=10.1089/ars.2011.3930;
RA Rink C., Gnyawali S., Peterson L., Khanna S.;
RT "Oxygen-inducible glutamate oxaloacetate transaminase as protective switch
RT transforming neurotoxic glutamate to metabolic fuel during acute ischemic
RT stroke.";
RL Antioxid. Redox Signal. 14:1777-1785(2011).
RN [10]
RP FUNCTION.
RX PubMed=21266983; DOI=10.1038/jcbfm.2011.3;
RA Campos F., Sobrino T., Ramos-Cabrer P., Argibay B., Agulla J.,
RA Perez-Mato M., Rodriguez-Gonzalez R., Brea D., Castillo J.;
RT "Neuroprotection by glutamate oxaloacetate transaminase in ischemic stroke:
RT an experimental study.";
RL J. Cereb. Blood Flow Metab. 31:1378-1386(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine.
CC Important regulator of levels of glutamate, the major excitatory
CC neurotransmitter of the vertebrate central nervous system. Acts as a
CC scavenger of glutamate in brain neuroprotection. The aspartate
CC aminotransferase activity is involved in hepatic glucose synthesis
CC during development and in adipocyte glyceroneogenesis. Using L-cysteine
CC as substrate, regulates levels of mercaptopyruvate, an important source
CC of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the
CC action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide
CC is an important synaptic modulator and neuroprotectant in the brain.
CC {ECO:0000269|PubMed:17545671, ECO:0000269|PubMed:21266983,
CC ECO:0000269|PubMed:21361730, ECO:0000269|PubMed:3053674,
CC ECO:0000269|PubMed:3182750, ECO:0000269|PubMed:7113743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:3053674, ECO:0000269|PubMed:7113743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825;
CC Evidence={ECO:0000269|PubMed:3053674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-
CC glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3;
CC Evidence={ECO:0000269|PubMed:7113743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442;
CC Evidence={ECO:0000269|PubMed:7113743};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:70223, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000250|UniProtKB:P17174};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70225;
CC Evidence={ECO:0000250|UniProtKB:P17174};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-sulfino-L-alanine = 3-sulfinopyruvate + L-
CC glutamate; Xref=Rhea:RHEA:70295, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:61085, ChEBI:CHEBI:140699;
CC Evidence={ECO:0000269|PubMed:7113743};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70297;
CC Evidence={ECO:0000269|PubMed:7113743};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Inhibited by L-aspartate.
CC {ECO:0000269|PubMed:7113743}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.2 mM for L-cysteine {ECO:0000269|PubMed:7113743};
CC KM=0.06 mM for 2-oxoglutarate {ECO:0000269|PubMed:7113743};
CC pH dependence:
CC Optimum pH is 9.7. {ECO:0000269|PubMed:7113743};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney.
CC {ECO:0000269|PubMed:3182856}.
CC -!- INDUCTION: In liver and kidney, by glucocorticod hormones. Levels in
CC the liver also increase 2-fold on animals fed on a high protein diet or
CC during fasting. By hypoxia during cerebral ischemia.
CC {ECO:0000269|PubMed:17545671, ECO:0000269|PubMed:21361730,
CC ECO:0000269|PubMed:3182750, ECO:0000269|PubMed:3182856}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; J04171; AAA40769.1; -; mRNA.
DR EMBL; D00252; BAA00183.1; -; mRNA.
DR EMBL; BC061877; AAH61877.1; -; mRNA.
DR EMBL; J05263; AAA40842.1; -; Genomic_DNA.
DR PIR; I55325; I55325.
DR PIR; JT0439; JT0439.
DR RefSeq; NP_036703.2; NM_012571.2.
DR AlphaFoldDB; P13221; -.
DR SMR; P13221; -.
DR BioGRID; 246568; 1.
DR IntAct; P13221; 1.
DR STRING; 10116.ENSRNOP00000022309; -.
DR iPTMnet; P13221; -.
DR PhosphoSitePlus; P13221; -.
DR SwissPalm; P13221; -.
DR World-2DPAGE; 0004:P13221; -.
DR jPOST; P13221; -.
DR PaxDb; P13221; -.
DR PRIDE; P13221; -.
DR GeneID; 24401; -.
DR KEGG; rno:24401; -.
DR UCSC; RGD:2721; rat.
DR CTD; 2805; -.
DR RGD; 2721; Got1.
DR VEuPathDB; HostDB:ENSRNOG00000016356; -.
DR eggNOG; KOG1412; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P13221; -.
DR OMA; WDQNKRQ; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P13221; -.
DR TreeFam; TF314089; -.
DR BioCyc; MetaCyc:MON-12468; -.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR Reactome; R-RNO-8963693; Aspartate and asparagine metabolism.
DR SABIO-RK; P13221; -.
DR PRO; PR:P13221; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016356; Expressed in heart and 20 other tissues.
DR Genevisible; P13221; RN.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0031406; F:carboxylic acid binding; IDA:RGD.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:RGD.
DR GO; GO:0047801; F:L-cysteine transaminase activity; IDA:UniProtKB.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; ISO:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006532; P:aspartate biosynthetic process; ISO:RGD.
DR GO; GO:0006533; P:aspartate catabolic process; ISO:RGD.
DR GO; GO:0006531; P:aspartate metabolic process; IDA:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
DR GO; GO:0043648; P:dicarboxylic acid metabolic process; IDA:RGD.
DR GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:RGD.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; ISO:RGD.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006114; P:glycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IMP:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:RGD.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:1990267; P:response to transition metal nanoparticle; IDA:RGD.
DR GO; GO:0060290; P:transdifferentiation; IMP:RGD.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..413
FT /note="Aspartate aminotransferase, cytoplasmic"
FT /id="PRO_0000123883"
FT BINDING 39
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 259
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 55
FT /note="R -> T (in Ref. 1; AAA40769)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="R -> G (in Ref. 1; AAA40769)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="G -> A (in Ref. 1; AAA40769)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="G -> A (in Ref. 1; AAA40769)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="N -> I (in Ref. 2; BAA00183)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="A -> P (in Ref. 1; AAA40769)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="L -> F (in Ref. 2; BAA00183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46429 MW; A9425BF05AC24C08 CRC64;
MAPPSFFAQV PQAPPVLVFK LIADFRDDPD PRKVNLGVGA YRTDDSQPWV LPVVRKVEQK
IANDHSLNHE YLPILGLAEF RSCASQLVLG DNSPALRENR VGGVQSLGGT GALRIGADFL
GRWYNGTDNK NTPVYVSSPT WENHNGVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN
APEFSIFVLH ACAHNPTGTD PTEEEWKQIA AVMKRRFLFP FFDSAYQGFA SGDLEKDAWA
IRYFVSEGFE LFCAQSFSKN FGLYNERVGN LTVVGKEHDS VLRVLSQMEK IVRITWSNPP
AQGARIVATT LSNPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT WSHITEQIGM
FSFTGLNPKQ VEYLVNEKHI YLMPSGRINM CGLTTKNLDY VATSINEAVT KFQ
