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Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A)

 AATC_MOUSE              Reviewed;         413 AA.
P05201; Q3UJH8;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 3.
07-JUN-2017, entry version 155.
RecName: Full=Aspartate aminotransferase, cytoplasmic;
Short=cAspAT;
EC=2.6.1.1;
EC=2.6.1.3;
AltName: Full=Cysteine aminotransferase, cytoplasmic;
AltName: Full=Cysteine transaminase, cytoplasmic;
Short=cCAT;
AltName: Full=Glutamate oxaloacetate transaminase 1;
AltName: Full=Transaminase A;
Name=Got1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3782150;
Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y.;
"Cloning and sequence analysis of mRNA for mouse aspartate
aminotransferase isoenzymes.";
J. Biol. Chem. 261:16976-16983(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3379636; DOI=10.1016/0022-2836(88)90329-4;
Obaru K., Tsuzuki T., Setoyama C., Shimada K.;
"Structural organization of the mouse aspartate aminotransferase
isoenzyme genes. Introns antedate the divergence of cytosolic and
mitochondrial isoenzyme genes.";
J. Mol. Biol. 200:13-22(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-55; 61-81; 87-97; 101-166; 208-236; 260-276;
306-318 AND 347-411, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
TISSUE SPECIFICITY, AND ENZYME REGULATION.
PubMed=21937432; DOI=10.1074/jbc.M111.298208;
Mikami Y., Shibuya N., Kimura Y., Nagahara N., Yamada M., Kimura H.;
"Hydrogen sulfide protects the retina from light-induced degeneration
by the modulation of Ca2+ influx.";
J. Biol. Chem. 286:39379-39386(2011).
[9]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: 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 H(2)S via the action of 3-
mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an
important synaptic modulator and neuroprotectant in the brain (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
L-glutamate.
-!- CATALYTIC ACTIVITY: L-cysteine + 2-oxoglutarate = mercaptopyruvate
+ L-glutamate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ENZYME REGULATION: Inhibited by calcium ions.
{ECO:0000269|PubMed:21937432}.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in neurons of the retina. Localizes
to the inner and outer plexiform layers, the inner and outer
nuclear layer and the outer segments of photoreceptors.
{ECO:0000269|PubMed:21937432}.
-!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial
and chloroplastic isozymes.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J02623; AAA37263.1; -; mRNA.
EMBL; X07302; CAA30275.1; -; Genomic_DNA.
EMBL; X07303; CAA30275.1; JOINED; Genomic_DNA.
EMBL; X07304; CAA30275.1; JOINED; Genomic_DNA.
EMBL; X07305; CAA30275.1; JOINED; Genomic_DNA.
EMBL; X07306; CAA30275.1; JOINED; Genomic_DNA.
EMBL; X07307; CAA30275.1; JOINED; Genomic_DNA.
EMBL; X07308; CAA30275.1; JOINED; Genomic_DNA.
EMBL; X07309; CAA30275.1; JOINED; Genomic_DNA.
EMBL; AK146445; BAE27177.1; -; mRNA.
EMBL; BC002057; AAH02057.1; -; mRNA.
CCDS; CCDS29832.1; -.
PIR; S01076; S01076.
RefSeq; NP_034454.2; NM_010324.2.
UniGene; Mm.19039; -.
ProteinModelPortal; P05201; -.
SMR; P05201; -.
BioGrid; 199999; 1.
IntAct; P05201; 21.
MINT; MINT-1869597; -.
STRING; 10090.ENSMUSP00000026196; -.
iPTMnet; P05201; -.
PhosphoSitePlus; P05201; -.
SwissPalm; P05201; -.
SWISS-2DPAGE; P05201; -.
EPD; P05201; -.
MaxQB; P05201; -.
PaxDb; P05201; -.
PeptideAtlas; P05201; -.
PRIDE; P05201; -.
Ensembl; ENSMUST00000026196; ENSMUSP00000026196; ENSMUSG00000025190.
GeneID; 14718; -.
KEGG; mmu:14718; -.
UCSC; uc012bmb.1; mouse.
CTD; 2805; -.
MGI; MGI:95791; Got1.
eggNOG; KOG1411; Eukaryota.
eggNOG; COG1448; LUCA.
GeneTree; ENSGT00390000014081; -.
HOGENOM; HOG000185898; -.
HOVERGEN; HBG000951; -.
InParanoid; P05201; -.
KO; K14454; -.
OMA; ELFKEWT; -.
OrthoDB; EOG091G06G3; -.
TreeFam; TF314089; -.
Reactome; R-MMU-70263; Gluconeogenesis.
Reactome; R-MMU-70614; Amino acid synthesis and interconversion (transamination).
PRO; PR:P05201; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025190; -.
CleanEx; MM_GOT1; -.
ExpressionAtlas; P05201; baseline and differential.
Genevisible; P05201; MM.
GO; GO:0043679; C:axon terminus; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0031406; F:carboxylic acid binding; IEA:Ensembl.
GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:MGI.
GO; GO:0047801; F:L-cysteine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IDA:MGI.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
GO; GO:0006532; P:aspartate biosynthetic process; IDA:MGI.
GO; GO:0006533; P:aspartate catabolic process; ISO:MGI.
GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0055089; P:fatty acid homeostasis; IDA:MGI.
GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:MGI.
GO; GO:0019550; P:glutamate catabolic process to aspartate; IDA:MGI.
GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
GO; GO:0006114; P:glycerol biosynthetic process; IDA:MGI.
GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
GO; GO:0006107; P:oxaloacetate metabolic process; IDA:MGI.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR000796; Asp_trans.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
PANTHER; PTHR11879; PTHR11879; 1.
Pfam; PF00155; Aminotran_1_2; 1.
PRINTS; PR00799; TRANSAMINASE.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
1: Evidence at protein level;
Amino-acid biosynthesis; Aminotransferase; Complete proteome;
Cytoplasm; Direct protein sequencing; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08906}.
CHAIN 2 413 Aspartate aminotransferase, cytoplasmic.
/FTId=PRO_0000123880.
BINDING 39 39 Aspartate; via amide nitrogen.
{ECO:0000250}.
BINDING 141 141 Aspartate. {ECO:0000250}.
BINDING 195 195 Aspartate. {ECO:0000250}.
BINDING 387 387 Aspartate. {ECO:0000250}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:P13221}.
MOD_RES 259 259 N6-(pyridoxal phosphate)lysine.
MOD_RES 318 318 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
CONFLICT 94 94 L -> P (in Ref. 1; AAA37263, 2; CAA30275
and 4; AAH02057). {ECO:0000305}.
CONFLICT 291 291 I -> N (in Ref. 2; CAA30275).
{ECO:0000305}.
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


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