AGT2_MOUSE
ID AGT2_MOUSE Reviewed; 513 AA.
AC Q3UEG6; B9EIZ8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alanine--glyoxylate aminotransferase 2, mitochondrial;
DE Short=AGT 2;
DE EC=2.6.1.44;
DE AltName: Full=(R)-3-amino-2-methylpropionate--pyruvate transaminase;
DE EC=2.6.1.40;
DE AltName: Full=Beta-ALAAT II;
DE AltName: Full=Beta-alanine-pyruvate aminotransferase;
DE AltName: Full=D-AIBAT;
DE Flags: Precursor;
GN Name=Agxt2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23023372; DOI=10.1161/atvbaha.112.254078;
RA Caplin B., Wang Z., Slaviero A., Tomlinson J., Dowsett L., Delahaye M.,
RA Salama A., Wheeler D.C., Leiper J.;
RT "Alanine-Glyoxylate aminotransferase-2 metabolizes endogenous
RT methylarginines, regulates NO, and controls blood pressure.";
RL Arterioscler. Thromb. Vasc. Biol. 32:2892-2900(2012).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-261; LYS-303; LYS-416
RP AND LYS-419, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-70; LYS-83; LYS-261;
RP LYS-416; LYS-419 AND LYS-453, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Can metabolize asymmetric dimethylarginine (ADMA) via
CC transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid
CC (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and
CC this activity provides mechanism through which the kidney regulates
CC blood pressure. {ECO:0000269|PubMed:23023372}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-
CC oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BYV1}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are hypertensive.
CC {ECO:0000269|PubMed:23023372}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AK149538; BAE28945.1; -; mRNA.
DR EMBL; BC141248; AAI41249.1; -; mRNA.
DR CCDS; CCDS79362.1; -.
DR RefSeq; NP_001297664.1; NM_001310735.1.
DR RefSeq; NP_001297665.1; NM_001310736.1.
DR AlphaFoldDB; Q3UEG6; -.
DR SMR; Q3UEG6; -.
DR STRING; 10090.ENSMUSP00000022858; -.
DR iPTMnet; Q3UEG6; -.
DR PhosphoSitePlus; Q3UEG6; -.
DR SwissPalm; Q3UEG6; -.
DR jPOST; Q3UEG6; -.
DR MaxQB; Q3UEG6; -.
DR PRIDE; Q3UEG6; -.
DR ProteomicsDB; 285782; -.
DR Antibodypedia; 43482; 149 antibodies from 26 providers.
DR DNASU; 268782; -.
DR Ensembl; ENSMUST00000110542; ENSMUSP00000106171; ENSMUSG00000089678.
DR GeneID; 268782; -.
DR KEGG; mmu:268782; -.
DR UCSC; uc007vga.1; mouse.
DR CTD; 64902; -.
DR MGI; MGI:2146052; Agxt2.
DR VEuPathDB; HostDB:ENSMUSG00000089678; -.
DR eggNOG; KOG1404; Eukaryota.
DR GeneTree; ENSGT00940000156125; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; Q3UEG6; -.
DR BRENDA; 2.6.1.44; 3474.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR SABIO-RK; Q3UEG6; -.
DR BioGRID-ORCS; 268782; 2 hits in 60 CRISPR screens.
DR ChiTaRS; Agxt2; mouse.
DR PRO; PR:Q3UEG6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q3UEG6; protein.
DR Bgee; ENSMUSG00000089678; Expressed in left lobe of liver and 20 other tissues.
DR ExpressionAtlas; Q3UEG6; baseline and differential.
DR Genevisible; Q3UEG6; MM.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0047305; F:(R)-3-amino-2-methylpropionate-pyruvate transaminase activity; ISO:MGI.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IDA:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; ISO:MGI.
DR GO; GO:0009436; P:glyoxylate catabolic process; ISO:MGI.
DR GO; GO:0019481; P:L-alanine catabolic process, by transamination; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 41..513
FT /note="Alanine--glyoxylate aminotransferase 2,
FT mitochondrial"
FT /id="PRO_0000283753"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 261
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 261
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 303
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 349
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 416
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 416
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 419
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 419
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 453
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 513 AA; 57115 MW; 055D10974BA46A25 CRC64;
MSLAWRNLQK PFYLETSLRI LQMRPSLSLG ASRIAVPKLT LHTKHSMPPC DFSPEKYQSL
AYSRVLAIHK QHLSPVDTAY FRKPLLLHQG HMEWLFDSEG NRYLDFFSGI VTVSVGHCHP
KVSAVAKKQI DRLWHTSSVF FHSPMHEYAE KLSALLPEPL KVIFLVNSGS EANDLAMVMA
RAHSNHTDII SFRGAYHGCS PYTLGLTNVG IYKMEVPGGI GCQSTMCPDV FRGPWGGIHC
RDSPVQTVRD CSCAPDCCQA KERYIEQFKD TLNTSVATSI AGFFAEPIQG VNGVVQYPKE
FLKEAFALVR ERGGVCIADE VQTGFGRLGS HFWGFQTHDV LPDIVTMAKG IGNGFPMAAV
VTTPEIAKSL AKRLLHFSTF GGNPLACAIG SAVLEVIEEE NLQRNSQEVG TYMLLKFAKL
RDEFDIVGDV RGKGLMVGIE MVQDKISRQP LPKTEVNQIH EDCKDMGLLV GRGGNFSQTF
RIVPPMCVTK MEVDFAYEVF RAALIQHMER RAK
