ID   AATC_MOUSE              Reviewed;         413 AA.
AC   P05201; Q3UJH8;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 3.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Aspartate aminotransferase, cytoplasmic {ECO:0000305};
DE            Short=cAspAT;
DE            EC=2.6.1.1 {ECO:0000250|UniProtKB:P13221};
DE            EC=2.6.1.3 {ECO:0000250|UniProtKB:P13221};
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|MGI:MGI:95791};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=3782150; DOI=10.1016/s0021-9258(19)75987-0;
RA   Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y.;
RT   "Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase
RT   isoenzymes.";
RL   J. Biol. Chem. 261:16976-16983(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3379636; DOI=10.1016/0022-2836(88)90329-4;
RA   Obaru K., Tsuzuki T., Setoyama C., Shimada K.;
RT   "Structural organization of the mouse aspartate aminotransferase isoenzyme
RT   genes. Introns antedate the divergence of cytosolic and mitochondrial
RT   isoenzyme genes.";
RL   J. Mol. Biol. 200:13-22(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   [5]
RP   PROTEIN SEQUENCE OF 2-55; 61-81; 87-97; 101-166; 208-236; 260-276; 306-318
RP   AND 347-411, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX   PubMed=21937432; DOI=10.1074/jbc.m111.298208;
RA   Mikami Y., Shibuya N., Kimura Y., Nagahara N., Yamada M., Kimura H.;
RT   "Hydrogen sulfide protects the retina from light-induced degeneration by
RT   the modulation of Ca2+ influx.";
RL   J. Biol. Chem. 286:39379-39386(2011).
RN   [9]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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:0000250|UniProtKB:P13221}.
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:0000250|UniProtKB:P13221};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
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:0000250|UniProtKB:P13221};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
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:0000250|UniProtKB:P13221};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70297;
CC         Evidence={ECO:0000250|UniProtKB:P13221};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- ACTIVITY REGULATION: Inhibited by calcium ions.
CC       {ECO:0000269|PubMed:21937432}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons of the retina. Localizes to
CC       the inner and outer plexiform layers, the inner and outer nuclear layer
CC       and the outer segments of photoreceptors.
CC       {ECO:0000269|PubMed:21937432}.
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; J02623; AAA37263.1; -; mRNA.
DR   EMBL; X07302; CAA30275.1; -; Genomic_DNA.
DR   EMBL; X07303; CAA30275.1; JOINED; Genomic_DNA.
DR   EMBL; X07304; CAA30275.1; JOINED; Genomic_DNA.
DR   EMBL; X07305; CAA30275.1; JOINED; Genomic_DNA.
DR   EMBL; X07306; CAA30275.1; JOINED; Genomic_DNA.
DR   EMBL; X07307; CAA30275.1; JOINED; Genomic_DNA.
DR   EMBL; X07308; CAA30275.1; JOINED; Genomic_DNA.
DR   EMBL; X07309; CAA30275.1; JOINED; Genomic_DNA.
DR   EMBL; AK146445; BAE27177.1; -; mRNA.
DR   EMBL; BC002057; AAH02057.1; -; mRNA.
DR   CCDS; CCDS29832.1; -.
DR   PIR; S01076; S01076.
DR   RefSeq; NP_034454.2; NM_010324.2.
DR   AlphaFoldDB; P05201; -.
DR   SMR; P05201; -.
DR   BioGRID; 199999; 12.
DR   IntAct; P05201; 20.
DR   STRING; 10090.ENSMUSP00000026196; -.
DR   GlyGen; P05201; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P05201; -.
DR   MetOSite; P05201; -.
DR   PhosphoSitePlus; P05201; -.
DR   SwissPalm; P05201; -.
DR   EPD; P05201; -.
DR   jPOST; P05201; -.
DR   MaxQB; P05201; -.
DR   PaxDb; 10090-ENSMUSP00000026196; -.
DR   PeptideAtlas; P05201; -.
DR   ProteomicsDB; 286016; -.
DR   Pumba; P05201; -.
DR   Antibodypedia; 31077; 601 antibodies from 38 providers.
DR   DNASU; 14718; -.
DR   Ensembl; ENSMUST00000026196.14; ENSMUSP00000026196.8; ENSMUSG00000025190.14.
DR   GeneID; 14718; -.
DR   KEGG; mmu:14718; -.
DR   UCSC; uc012bmb.1; mouse.
DR   AGR; MGI:95791; -.
DR   CTD; 2805; -.
DR   MGI; MGI:95791; Got1.
DR   VEuPathDB; HostDB:ENSMUSG00000025190; -.
DR   eggNOG; KOG1412; Eukaryota.
DR   GeneTree; ENSGT00950000183082; -.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   InParanoid; P05201; -.
DR   OMA; SWAIRYF; -.
DR   OrthoDB; 1123851at2759; -.
DR   PhylomeDB; P05201; -.
DR   TreeFam; TF314089; -.
DR   Reactome; R-MMU-70263; Gluconeogenesis.
DR   Reactome; R-MMU-8963693; Aspartate and asparagine metabolism.
DR   BioGRID-ORCS; 14718; 0 hits in 79 CRISPR screens.
DR   ChiTaRS; Got1; mouse.
DR   PRO; PR:P05201; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P05201; Protein.
DR   Bgee; ENSMUSG00000025190; Expressed in extra-ocular muscle and 256 other cell types or tissues.
DR   ExpressionAtlas; P05201; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:MGI.
DR   GO; GO:0047801; F:L-cysteine transaminase activity; ISS:UniProtKB.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IDA:MGI.
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; IDA:MGI.
DR   GO; GO:0006533; P:aspartate catabolic process; ISO:MGI.
DR   GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR   GO; GO:0043648; P:dicarboxylic acid metabolic process; ISO:MGI.
DR   GO; GO:0055089; P:fatty acid homeostasis; IDA:MGI.
DR   GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:MGI.
DR   GO; GO:0019550; P:glutamate catabolic process to aspartate; IDA:MGI.
DR   GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006114; P:glycerol biosynthetic process; IDA:MGI.
DR   GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR   GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISO:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IDA:MGI.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:1990267; P:response to transition metal nanoparticle; ISO:MGI.
DR   GO; GO:0060290; P:transdifferentiation; ISO:MGI.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF3; ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   SWISS-2DPAGE; P05201; -.
DR   Genevisible; P05201; MM.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW   Direct protein sequencing; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P08906"
FT   CHAIN           2..413
FT                   /note="Aspartate aminotransferase, cytoplasmic"
FT                   /id="PRO_0000123880"
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         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13221"
FT   MOD_RES         259
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   MOD_RES         318
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        94
FT                   /note="L -> P (in Ref. 1; AAA37263, 2; CAA30275 and 4;
FT                   AAH02057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        291
FT                   /note="I -> N (in Ref. 2; CAA30275)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  46248 MW;  0E37C763155EA6B5 CRC64;
     MAPPSVFAQV PQAPPVLVFK LTADFRDDPD PRKVNLGVGA YRTDESQPWV LPVVRKVEQK
     IANDNSLNHE YLPILGLAEF RSCASRLVLG DNSLAIRENR VGGVQSLGGT GALRIGADFL
     GRWYNGTDNK NTPIYVSSPT WENHNAVFSA AGFKDIRPYC YWDAEKRGLD LQGFLNDLEN
     APEFSIFVLH ACAHNPTGTD PTPEQWKQIA AVMQRRFLFP FFDSAYQGFA SGDLEKDAWA
     IRYFVSEGFE LFCAQSFSKN FGLYNERVGN LTVVGKESDS VLRVLSQMEK IVRITWSNPP
     AQGARIVAAT LSDPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT WSHITEQIGM
     FSFTGLNPKQ VEYLVNEKHI YLLPSGRINM CGLTTKNLDY VATSIHEAVT KIQ
//