Reviewed, UniProtKB/Swiss-Prot P05202 (AATM_MOUSE)

Names and origin

Protein names

Recommended name:
    Aspartate aminotransferase, mitochondrial
      Short name=mAspAT
    EC=2.6.1.1
Alternative name(s):
    Transaminase A
    Glutamate oxaloacetate transaminase 2
    Fatty acid-binding protein
    FABP-1
    FABPpm

Gene names

Name:	Got2
Synonyms:	Got-2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	430 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	Facilitates cellular uptake of long-chain free fatty acids. Ref.7
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion matrix. Cell membrane. Ref.3
Post-translational modification	Acetylation of Lys-296, Lys-345 and Lys-363 is observed in liver mitochondria from fasted mice but not from fed mice.
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	Lipid transport Transport
Cellular component	Cell membrane Membrane Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation Nitration Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aspartate biosynthetic process Inferred from direct assay. Source: MGI glutamate catabolic process to 2-oxoglutarate Inferred from direct assay. Source: MGI glutamate catabolic process to aspartate Inferred from direct assay. Source: MGI lipid transport Inferred from electronic annotation. Source: UniProtKB-KW oxaloacetate metabolic process Inferred from direct assay. Source: MGI
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from direct assay. 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
	Transit peptide	1 – 29	29	Mitochondrion
	Chain	30 – 430	401	Aspartate aminotransferase, mitochondrial		PRO_0000001216
Amino acid modifications
	Modified residue	73	1	N6-acetyllysine By similarity
	Modified residue	90	1	N6-acetyllysine By similarity
	Modified residue	94	1	N6-acetyllysine Ref.9
	Modified residue	96	1	Nitrated tyrosine
	Modified residue	96	1	Phosphotyrosine By similarity
	Modified residue	150	1	N6-acetyllysine By similarity
	Modified residue	159	1	N6-acetyllysine Ref.9
	Modified residue	185	1	N6-acetyllysine Ref.9
	Modified residue	234	1	N6-acetyllysine By similarity
	Modified residue	279	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	296	1	N6-acetyllysine Ref.9
	Modified residue	345	1	N6-acetyllysine Ref.9
	Modified residue	363	1	N6-acetyllysine Ref.9
	Modified residue	396	1	N6-acetyllysine By similarity
	Modified residue	401	1	Phosphotyrosine By similarity
	Modified residue	404	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	68	1	R → G in BAE39800. Ref.4
	Sequence conflict	146	1	Q → E in AAB91426. Ref.3
	Sequence conflict	153	1	R → G in BAE39800. Ref.4
	Sequence conflict	377	1	Q → K in BAE39800. Ref.4
	Sequence conflict	421	1	L → I in BAE39800. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P05202-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: D590524CA7FFB885	FASTA	430	47,411
	10 20 30 40 50 60 MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 70 80 90 100 110 120 NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENNEV 130 140 150 160 170 180 LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR 190 200 210 220 230 240 YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA 250 260 270 280 290 300 FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE 310 320 330 340 350 360 AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS 370 380 390 400 410 420 NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY 430 LAHAIHQVTK

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: 3782150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization of the mouse mitochondrial aspartate aminotransferase gene." Tsuzuki T., Obaru K., Setoyama C., Shimada K. J. Mol. Biol. 198:21-31(1987) [PubMed: 2828632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/He. Tissue: Liver.
[3]	"Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA." Bradbury M.W., Berk P.D. Biochem. J. 345:423-427(2000) [PubMed: 10642497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Strain: FVB. Tissue: Liver.
[4]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c, C57BL/6J and NOD. Tissue: Bone marrow macrophage, Cecum, Dendritic cell and Melanocyte.
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain and Eye.
[6]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 60-81; 91-122; 126-139; 171-180; 186-200; 280-296; 310-345; 356-363 AND 397-404, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[7]	"Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake." Zhou S.-L., Stump D., Kiang C.L., Isola L.M., Berk P.D. Proc. Soc. Exp. Biol. Med. 208:263-270(1995) [PubMed: 7878064] [Abstract] Cited for: FUNCTION.
[8]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed: 16800626] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-159; LYS-185; LYS-296; LYS-345 AND LYS-363, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02622 mRNA. Translation: AAA37264.1. X06917 , X06918, X06919, X06920, X06921, X06922, X06923, X06924, X06925, X06926 Genomic DNA. Translation: CAA30015.1. M37259 , M37250, M37251, M37252, M37253, M37254, M37255, M37256, M37258 Genomic DNA. Translation: AAA37265.1. Sequence problems. U82470 mRNA. Translation: AAB91426.1. AK136556 mRNA. Translation: BAE23042.1. AK147953 mRNA. Translation: BAE28248.1. AK149886 mRNA. Translation: BAE29146.1. AK149926 mRNA. Translation: BAE29171.1. AK150194 mRNA. Translation: BAE29370.1. AK152921 mRNA. Translation: BAE31596.1. AK155075 mRNA. Translation: BAE33029.1. AK167767 mRNA. Translation: BAE39800.1. BC089015 mRNA. Translation: AAH89015.1. BC089341 mRNA. Translation: AAH89341.1.
IPI	IPI00117312.
PIR	S01174.
RefSeq	NP_034455.1.
UniGene	Mm.230169
3D structure databases
HSSP	HSSP built from PDB template 7AAT based on UniProtKB P00508.
SMR	P05202. Positions 30-430.
ModBase	Search...
Protein-protein interaction databases
STRING	P05202.
PTM databases
PhosphoSite	P05202.
Proteomic databases
PRIDE	P05202.
Genome annotation databases
Ensembl	ENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672; Mus musculus. [Genome view]
GeneID	14719.
KEGG	mmu:14719.
UCSC	uc009mzi.1. mouse.
Organism-specific databases
CTD	14719.
MGI	MGI:95792. Got2.
Phylogenomic databases
HOGENOM	P05202.
HOVERGEN	P05202.
OMA	IASSYSK.
Enzyme and pathway databases
BRENDA	2.6.1.1. 244.
Gene expression databases
ArrayExpress	P05202.
Bgee	P05202.
Genevestigator	P05202.
GermOnline	ENSMUSG00000031672. Mus musculus.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11879. Asp_trans. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	286731.
SOURCE	Search...

Entry information

Entry name

AATM_MOUSE

Accession

Primary (citable) accession number: P05202
Secondary accession number(s): O09188 , Q3TIP6, Q3UD91, Q5HZH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	November 3, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)