ALAT2_MOUSE
ID ALAT2_MOUSE Reviewed; 522 AA.
AC Q8BGT5; Q8BVY7; Q8K1J3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Alanine aminotransferase 2;
DE Short=ALT2;
DE EC=2.6.1.2;
DE AltName: Full=Glutamate pyruvate transaminase 2;
DE Short=GPT 2;
DE AltName: Full=Glutamic--alanine transaminase 2;
DE AltName: Full=Glutamic--pyruvic transaminase 2;
GN Name=Gpt2; Synonyms=Aat2;
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], AND TISSUE SPECIFICITY.
RX PubMed=15122758; DOI=10.1002/hep.20182;
RA Jadhao S.B., Yang R.-Z., Lin Q., Hu H., Anania F.A., Shuldiner A.R.,
RA Gong D.-W.;
RT "Murine alanine aminotransferase: cDNA cloning, functional expression, and
RT differential gene regulation in mouse fatty liver.";
RL Hepatology 39:1297-1302(2004).
RN [2]
RP ERRATUM OF PUBMED:15122758.
RA Jadhao S.B., Yang R.-Z., Lin Q., Hu H., Anania F.A., Shuldiner A.R.,
RA Gong D.-W.;
RL Hepatology 40:269-269(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, Head, Skin, and Tongue;
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=Czech II; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Pancreas, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-414; LYS-504 AND LYS-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Catalyzes the reversible transamination between alanine and
CC 2-oxoglutarate to form pyruvate and glutamate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC pathway; pyruvate from L-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically induced in fatty liver. Highly
CC expressed in muscle, liver and white adipose tissue. Moderately
CC expressed in brain and kidney and expressed at low levels in the heart.
CC {ECO:0000269|PubMed:15122758}.
CC -!- MISCELLANEOUS: May be responsible for increased ALT activity in hepatic
CC steatosis.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000305}.
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DR EMBL; AK033424; BAC28282.1; -; mRNA.
DR EMBL; AK075894; BAC36035.1; -; mRNA.
DR EMBL; AK076250; BAC36274.1; -; mRNA.
DR EMBL; AK082030; BAC38395.1; -; mRNA.
DR EMBL; BC034219; AAH34219.1; -; mRNA.
DR EMBL; BK005128; DAA05290.1; -; mRNA.
DR CCDS; CCDS22499.1; -.
DR RefSeq; NP_776291.1; NM_173866.3.
DR AlphaFoldDB; Q8BGT5; -.
DR SMR; Q8BGT5; -.
DR BioGRID; 224369; 3.
DR STRING; 10090.ENSMUSP00000034136; -.
DR iPTMnet; Q8BGT5; -.
DR PhosphoSitePlus; Q8BGT5; -.
DR SwissPalm; Q8BGT5; -.
DR EPD; Q8BGT5; -.
DR jPOST; Q8BGT5; -.
DR MaxQB; Q8BGT5; -.
DR PaxDb; Q8BGT5; -.
DR PeptideAtlas; Q8BGT5; -.
DR PRIDE; Q8BGT5; -.
DR ProteomicsDB; 296170; -.
DR Antibodypedia; 28066; 240 antibodies from 29 providers.
DR DNASU; 108682; -.
DR Ensembl; ENSMUST00000034136; ENSMUSP00000034136; ENSMUSG00000031700.
DR GeneID; 108682; -.
DR KEGG; mmu:108682; -.
DR UCSC; uc009mpx.1; mouse.
DR CTD; 84706; -.
DR MGI; MGI:1915391; Gpt2.
DR VEuPathDB; HostDB:ENSMUSG00000031700; -.
DR eggNOG; KOG0258; Eukaryota.
DR GeneTree; ENSGT00940000159061; -.
DR HOGENOM; CLU_014254_3_1_1; -.
DR InParanoid; Q8BGT5; -.
DR OMA; FGFECPP; -.
DR OrthoDB; 477122at2759; -.
DR PhylomeDB; Q8BGT5; -.
DR TreeFam; TF300839; -.
DR Reactome; R-MMU-8964540; Alanine metabolism.
DR UniPathway; UPA00528; UER00586.
DR BioGRID-ORCS; 108682; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Gpt2; mouse.
DR PRO; PR:Q8BGT5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BGT5; protein.
DR Bgee; ENSMUSG00000031700; Expressed in lacrimal gland and 248 other tissues.
DR ExpressionAtlas; Q8BGT5; baseline and differential.
DR Genevisible; Q8BGT5; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042851; P:L-alanine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR045088; ALAT1/2-like.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11751; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..522
FT /note="Alanine aminotransferase 2"
FT /id="PRO_0000247533"
FT MOD_RES 340
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 414
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 504
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 511
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 252
FT /note="R -> W (in Ref. 4; AAH34219/DAA05290)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="D -> N (in Ref. 3; BAC36035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 57944 MW; 70FED064E5F6A92E CRC64;
MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE RSPRDRILTL ESMNPQVKAV
EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA MGQQPITFLR QVMALCTYPN
LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAFITRR DGVPADPDNI
YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA VISELDAVQV NYYLDEENCW
ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC IEDVIHFAWE EKLFLLADEV
YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK GYMGECGYRG GYMEVINLHP
EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ FSREKEFVLG NLAKKAKLTE
DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA PDMFYCMKLL EETGICVVPG
SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ YS
