P05201 (AATC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate aminotransferase, cytoplasmic
Short name=cAspAT
EC=2.6.1.1
EC=2.6.1.3

Alternative name(s):
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
Short name=cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A

Gene names

Name:

Got1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 H2S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Enzyme regulation	Inhibited by calcium ions. Ref.8
Subunit structure	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. Ref.8
Miscellaneous	In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aspartate biosynthetic process Inferred from direct assay PubMed 4193185. Source: MGI aspartate catabolic process Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara fatty acid homeostasis Inferred from direct assay PubMed 17545671. Source: MGI glutamate catabolic process to 2-oxoglutarate Inferred from direct assay PubMed 4193185. Source: MGI glutamate catabolic process to aspartate Inferred from direct assay PubMed 4193185. Source: MGI glycerol biosynthetic process Inferred from direct assay PubMed 17545671. Source: MGI oxaloacetate metabolic process Inferred from direct assay PubMed 4193185. Source: MGI response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	axon terminus Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 4193185. Source: MGI lysosome Inferred from electronic annotation. Source: Compara
Molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB L-cysteine:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC carboxylic acid binding Inferred from electronic annotation. Source: Compara phosphatidylserine decarboxylase activity Inferred from direct assay PubMed 3242498. Source: MGI pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 413	412	Aspartate aminotransferase, cytoplasmic		PRO_0000123880
Sites
	Binding site	39	1	Aspartate; via amide nitrogen By similarity
	Binding site	141	1	Aspartate By similarity
	Binding site	195	1	Aspartate By similarity
	Binding site	387	1	Aspartate By similarity
Amino acid modifications
	Modified residue	66	1	Phosphoserine Ref.7
	Modified residue	71	1	Phosphotyrosine Ref.6
	Modified residue	259	1	N6-(pyridoxal phosphate)lysine
Experimental info
	Sequence conflict	94	1	L → P in AAA37263. Ref.1
	Sequence conflict	94	1	L → P in CAA30275. Ref.2
	Sequence conflict	94	1	L → P in AAH02057. Ref.4
	Sequence conflict	291	1	I → N in CAA30275. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P05201 [UniParc]. Last modified June 28, 2011. Version 3. Checksum: 0E37C763155EA6B5	FASTA	413	46,248
	10 20 30 40 50 60 MAPPSVFAQV PQAPPVLVFK LTADFRDDPD PRKVNLGVGA YRTDESQPWV LPVVRKVEQK 70 80 90 100 110 120 IANDNSLNHE YLPILGLAEF RSCASRLVLG DNSLAIRENR VGGVQSLGGT GALRIGADFL 130 140 150 160 170 180 GRWYNGTDNK NTPIYVSSPT WENHNAVFSA AGFKDIRPYC YWDAEKRGLD LQGFLNDLEN 190 200 210 220 230 240 APEFSIFVLH ACAHNPTGTD PTPEQWKQIA AVMQRRFLFP FFDSAYQGFA SGDLEKDAWA 250 260 270 280 290 300 IRYFVSEGFE LFCAQSFSKN FGLYNERVGN LTVVGKESDS VLRVLSQMEK IVRITWSNPP 310 320 330 340 350 360 AQGARIVAAT LSDPELFKEW KGNVKTMADR ILTMRSELRA RLEALKTPGT WSHITEQIGM 370 380 390 400 410 FSFTGLNPKQ VEYLVNEKHI YLLPSGRINM CGLTTKNLDY VATSIHEAVT KIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of mRNA for mouse aspartate aminotransferase isoenzymes." Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y. J. Biol. Chem. 261:16976-16983(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structural organization of the mouse aspartate aminotransferase isoenzyme genes. Introns antedate the divergence of cytosolic and mitochondrial isoenzyme genes." Obaru K., Tsuzuki T., Setoyama C., Shimada K. J. Mol. Biol. 200:13-22(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart.
[4]	"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]. Strain: C57BL/6J. Tissue: Mammary gland.
[5]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-55; 61-81; 87-97; 101-166; 208-236; 260-276; 306-318 AND 347-411, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[6]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-71, MASS SPECTROMETRY. Tissue: Brain.
[7]	Lubec G., Kang S. Submitted (APR-2007) to UniProtKB Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, MASS SPECTROMETRY. Tissue: Brain.
[8]	"Hydrogen sulfide protects the retina from light-induced degeneration by the modulation of Ca2+ influx." Mikami Y., Shibuya N., Kimura Y., Nagahara N., Yamada M., Kimura H. J. Biol. Chem. 286:39379-39386(2011) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02623 mRNA. Translation: AAA37263.1. X07302 , X07303, X07304, X07305, X07306, X07307, X07308, X07309 Genomic DNA. Translation: CAA30275.1. AK146445 mRNA. Translation: BAE27177.1. BC002057 mRNA. Translation: AAH02057.1.
IPI	IPI00230204.
PIR	S01076.
RefSeq	NP_034454.2. NM_010324.2.
UniGene	Mm.19039.
3D structure databases
ProteinModelPortal	P05201.
SMR	P05201. Positions 15-412.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05201. 17 interactions.
STRING	10090.ENSMUSP00000026196.
PTM databases
PhosphoSite	P05201.
2D gel databases
SWISS-2DPAGE	P05201.
Proteomic databases
PaxDb	P05201.
PRIDE	P05201.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026196; ENSMUSP00000026196; ENSMUSG00000025190.
GeneID	14718.
KEGG	mmu:14718.
Organism-specific databases
CTD	2805.
MGI	MGI:95791. Got1.
Phylogenomic databases
eggNOG	COG1448.
GeneTree	ENSGT00390000014081.
HOGENOM	HOG000185898.
HOVERGEN	HBG000951.
InParanoid	Q3UJH8.
KO	K14454.
OMA	IILHGCA.
OrthoDB	EOG47D9G5.
Gene expression databases
Bgee	P05201.
CleanEx	MM_GOT1.
Genevestigator	P05201.
GermOnline	ENSMUSG00000025190. Mus musculus.
Family and domain databases
Gene3D	3.40.640.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
PANTHER	PTHR11879. PTHR11879. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	286727.
SOURCE	Search...

Entry information

Entry name

AATC_MOUSE

Accession

Primary (citable) accession number: P05201
Secondary accession number(s): Q3UJH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program